Descriptor: "MESH : Magnetic Resonance Spectroscopy" - Searchworks@Jio Institute Digital Library Search Results

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24 results on '"MESH : Magnetic Resonance Spectroscopy"'

1. GCKR polymorphism influences liver fat content in patients with type 2 diabetes

Author: Jean-Michel Petit, Marie-Claude Brindisi, Laurence Duvillard, Patrick Hillon, Boris Guiu, Fabien Rollot, David Masson, Benjamin Bouillet, Perrine Buffier, Bruno Vergès, Jean-Pierre Cercueil, Lipides - Nutrition - Cancer (U866) ( LNC ), Université de Bourgogne ( UB ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon ( ENSBANA ), Service d'Endocrinologie, Diabétologie et Maladies Métaboliques (CHU de Dijon), Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ), Service de radiologie et d'Imagerie médicale diagnostique et thérapeutique (CHU de Dijon), Service d'Hépato-Gastro-Entérologie (CHU de Dijon), Centre Hospitalier Universitaire de Dijon, and Conseil Regional de Bourgogne (AOI)
Subjects: Male, 0301 basic medicine, Magnetic Resonance Spectroscopy, Steatosis, MESH : Polymorphism, Genetic, Endocrinology, Diabetes and Metabolism, MESH : Aged, Type 2 diabetes, Body Mass Index, chemistry.chemical_compound, 0302 clinical medicine, Endocrinology, MESH : Diabetes Mellitus, Type 2, MESH : Lipid Metabolism, MESH : Female, MESH : Adaptor Proteins, Signal Transducing, education.field_of_study, Glucokinase regulatory protein, 1H-MR spectroscopy, General Medicine, Middle Aged, MESH : Adult, [ SDV.MHEP.EM ] Life Sciences [q-bio]/Human health and pathology/Endocrinology and metabolism, MESH : Non-alcoholic Fatty Liver Disease, Metformin, Liver, Female, medicine.drug, GCKR, Adult, Heterozygote, medicine.medical_specialty, MESH : Heterozygote, MESH : Male, Population, 030209 endocrinology & metabolism, Biology, 03 medical and health sciences, Diabetes mellitus, Internal medicine, Internal Medicine, medicine, Humans, MESH : Middle Aged, education, Alleles, Adaptor Proteins, Signal Transducing, Aged, Polymorphism, Genetic, Triglyceride, MESH : Humans, MESH : Liver, Lipid Metabolism, medicine.disease, MESH : Body Mass Index, 030104 developmental biology, Diabetes Mellitus, Type 2, chemistry, biology.protein, MESH : Magnetic Resonance Spectroscopy, MESH : Alleles, Body mass index, Non-alcoholic fatty liver disease
Abstract: IF 3.074; International audience; It has recently been shown that an allele in the glucokinase regulatory protein (GCKR) gene was associated with increased liver fat content in obese children. In this study, we set out to determine whether GCKR rs1260326 polymorphism was associated with liver fat content in patients with type 2 diabetes.Three hundred and eight patients with type 2 diabetes were included in this study. Liver fat content was evaluated using 1H-MR spectroscopy.In our population, carriers of the rs1260326 minor T allele had a higher liver fat content than did carriers of the C allele homozygote (12.4 +/- A 9.6 vs. 10.3 +/- A 9.1 %, p = 0.03). The number of patients with steatosis was significantly higher in minor T allele carriers than in C allele homozygote carriers (70.7 vs. 55.4 %; p = 0.008). In multivariate analysis, the predictive variables for steatosis were BMI [odds ratio (OR) 1.08; 95 % confidence interval (CI) 1.03-1.13; p = 0.002], statin therapy (yes) [OR 0.54; 95 % CI 0.31-0.94; p = 0.03], metformin therapy (yes) [OR 2.67; 95 % CI 1.50-4.75; p < 0.001], and rs1260326 GCKR polymorphism (TT+CT) [OR 1.99; 95 % CI 1.14-3.47; p = 0.01].This study shows that in patients with type 2 diabetes who were not selected for liver abnormalities, liver fat content was related to GCKR rs1260326 polymorphism independent of BMI, triglyceride levels, and age.
Published: 2016

2. Liver methylene fraction by dual- and triple-echo gradient-echo imaging at 3.0T: Correlation with proton MR spectroscopy and estimation of robustness after SPIO administration

Author: David Masson, Patrick Hillon, Isabelle Robin, Romaric Loffroy, Boris Guiu, Serge Aho, Jean-Michel Petit, Bruno Vergès, Jean-Pierre Cercueil, Douraied Ben Salem, Denis Krausé, Service de radiologie et d'Imagerie médicale diagnostique et thérapeutique (CHU de Dijon), Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon), Unité de Génétique Moléculaire Animale (UGMA), Université de Limoges (UNILIM)-Institut National de la Recherche Agronomique (INRA), Service d'Ophtalmologie (CHU de Dijon), Laboratoire Electronique, Informatique et Image [UMR6306] (Le2i), Université de Bourgogne (UB)-École Nationale Supérieure d'Arts et Métiers (ENSAM), Arts et Métiers Sciences et Technologies, HESAM Université (HESAM)-HESAM Université (HESAM)-Arts et Métiers Sciences et Technologies, HESAM Université (HESAM)-HESAM Université (HESAM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS), Groupe d'Etude de la Thrombose de Bretagne Occidentale (GETBO), Université de Brest (UBO)-Institut Brestois Santé Agro Matière (IBSAM), Université de Brest (UBO), Lipides - Nutrition - Cancer (U866) (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA), Service de Diabétologie, Service d'Hépato-Gastroentérologie, Hôpital du Bocage, Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon)-Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon), Unité de Génétique Moléculaire Animale (UMR GMA), Université de Brest (UBO)-Université de Brest (UBO), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Bourgogne (UB)-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Service d'Endocrinologie, Diabétologie et Maladies Métaboliques (CHU de Dijon), Service d'hépato-gastroentérologie et cancérologie digestive (CHU de Dijon), Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ), Unité de Génétique Moléculaire Animale ( UGMA ), Université de Limoges ( UNILIM ) -Institut National de la Recherche Agronomique ( INRA ), Laboratoire Electronique, Informatique et Image ( Le2i ), Université de Bourgogne ( UB ) -Centre National de la Recherche Scientifique ( CNRS ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Groupe d'Etude de la Thrombose de Bretagne Occidentale ( GETBO ), Université de Brest ( UBO ), Lipides - Nutrition - Cancer (U866) ( LNC ), Université de Bourgogne ( UB ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon ( ENSBANA ), and Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ) -Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon )
Subjects: Male, Magnetic Resonance Spectroscopy, MESH : Fatty Liver, MESH: Echo-Planar Imaging, [SDV]Life Sciences [q-bio], Carbon Compounds, Inorganic, MESH : Statistics as Topic, Statistics as Topic, MESH : Aged, Contrast Media, MESH : Carbon Compounds, Inorganic, MESH : Tissue Distribution, 030218 nuclear medicine & medical imaging, Correlation, chemistry.chemical_compound, 0302 clinical medicine, MESH : Dextrans, Non-alcoholic Fatty Liver Disease, MESH : Female, Tissue Distribution, MESH: Dextrans, Methylene, Magnetite Nanoparticles, MESH: Fatty Liver, MESH: Aged, MESH: Middle Aged, medicine.diagnostic_test, Echo-Planar Imaging, Dextrans, Nuclear magnetic resonance spectroscopy, MESH : Adult, Middle Aged, MESH: Reproducibility of Results, Adipose Tissue, Liver, Female, 030211 gastroenterology & hepatology, MESH : Sensitivity and Specificity, Protons, MESH: Adipose Tissue, Adult, Iron Overload, MESH : Male, MESH: Magnetite Nanoparticles, MESH : Adipose Tissue, Sensitivity and Specificity, MESH: Iron Overload, 03 medical and health sciences, Flip angle, Robustness (computer science), MESH: Contrast Media, Linear regression, medicine, MESH : Protons, Humans, MESH : Middle Aged, Radiology, Nuclear Medicine and imaging, MESH: Tissue Distribution, MESH: Statistics as Topic, Aged, MESH : Contrast Media, MESH : Iron Overload, MESH: Humans, MESH : Echo-Planar Imaging, [ SDV ] Life Sciences [q-bio], MESH: Magnetic Resonance Spectroscopy, business.industry, MESH : Reproducibility of Results, MESH : Humans, MESH: Biological Markers, MESH: Carbon Compounds, Inorganic, MESH : Liver, MESH : Magnetite Nanoparticles, Reproducibility of Results, MESH: Adult, Magnetic resonance imaging, MESH: Male, MESH: Sensitivity and Specificity, Proton mr spectroscopy, MESH : Biological Markers, Fatty Liver, chemistry, MESH : Magnetic Resonance Spectroscopy, MESH: Protons, Nuclear medicine, business, MESH: Female, Biomarkers, MESH: Liver
Abstract: Purpose To assess the systematic errors in liver methylene fraction (LMF) resulting from fat–fat interference effects with dual- and triple-echo gradient-recalled-echo Dual/Triple GRE) sequences and to test the robustness of these sequences after iron overloading. Materials and Methods Forty type-2 diabetic patients underwent LMF measurement by 3.0T 1H magnetic resonance spectroscopy (corrected for T1 and T2 decays) as the reference standard and liver fat fraction (%Fat) measurement by four Dual/Triple GRE sequences with 20° and 60° flip angle (α), corrected for T1 recovery. The same four sequences were repeated in eight patients after ferumoxide injection. Corrections for systematic errors were determined from the linear regressions (spectroscopy LMF values over Dual/Triple GRE %Fat values). Robustness was tested using Wilcoxon's signed-rank test. Results Fat–fat interference effects produced a ∼10% relative systematic error and T2* decay produced a 1.9%–4.2% absolute systematic error in LMF. When comparing before and after ferumoxide, dual-echo imaging with α = 20° and α = 60°, even when corrected, showed absolute differences of 7.23% [2.81%–10.25%] (P = 0.0117) and 5.65% [1.89%–8.216.8%] (P = 0.0117), respectively; compared to only 1.17% [0.08%–2.83%] (P = 0.0251) and 1.15% [0.37%–2.73%] (P = 0.2626) with triple-echo imaging and α = 20° and α = 60°, respectively. Conclusion Triple-echo imaging with α = 60° corrected for both T1 recovery and fat–fat interference effects is robust after superparamagnetic iron oxide (SPIO) administration and can reliably quantify LMF. J. Magn. Reson. Imaging 2011;33:119–127. © 2010 Wiley-Liss, Inc.
Published: 2010

3. Effects of particulate air pollution on systolic blood pressure: A population-based approach

Author: J.F. Tessier, Jean-François Dartigues, Virginie Rondeau, Imed Harrabi, Laurent Filleul, Laboratoire santé, travail, environnement, Université Bordeaux Segalen - Bordeaux 2, Equipe de Biostatistique, Université Bordeaux Segalen - Bordeaux 2-Institut National de la Santé et de la Recherche Médicale ( INSERM ) -IFR99-ISPED, Epidémiologie, santé publique et développement, Cire Aquitaine, Institut de Veille Sanitaire ( INVS ), and Rondeau, Virginie
Subjects: Male, Pollution, MESH : Male, media_common.quotation_subject, Population, MESH : Aged, MESH : Air Pollutants, Air pollution, MESH : Brain Chemistry, Hemodynamics, Blood Pressure, medicine.disease_cause, Biochemistry, Air Pollution, MESH : Particle Size, Environmental health, MESH : Dust, Linear regression, MESH : Blood Pressure, medicine, Humans, MESH : Protons, MESH : Female, Particle Size, MESH : Environmental Monitoring, MESH : Brain Neoplasms, MESH : France, MESH : Aged, 80 and over, education, Air quality index, Aged, General Environmental Science, media_common, Aged, 80 and over, Air Pollutants, education.field_of_study, MESH : Humans, Dust, [ SDV.SPEE ] Life Sciences [q-bio]/Santé publique et épidémiologie, Confidence interval, Blood pressure, [SDV.SPEE] Life Sciences [q-bio]/Santé publique et épidémiologie, MESH : Air Pollution, MESH : Magnetic Resonance Spectroscopy, Environmental science, Female, France, Environmental Monitoring
Abstract: Given the hypothesis that particulate air pollution is associated with systolic blood pressure, the effect of daily concentrations of air pollution on blood pressure was assessed in 2612 elderly subjects in the urban area of Bordeaux, France. Blood pressure was measured by a digital monitor. Particle concentrations (PM10) were obtained from the AIRAQ association that operates a local monitoring network of the air quality. To represent the ambient urban air pollution, stations had to be sufficiently correlated (i.e., correlation >0.70) and to have sufficiently similar mean levels of pollution. Linear regression was used to model the association between concentrations of particles (PM10) and systolic blood pressure. We observed associations between the fifth lag hour and systolic blood pressure for an increase of 10 microg/m3 of PM10 (beta = -1.12, 95% confidence interval: [-1.90; -0.30]). Despite contradictory results, fine particles must be considered nowadays as a major component of atmospheric air pollution in which everything must be put into practice in terms of public health actions in order to protect the general population and particularly the elderly group.
Published: 2006

4. NMR-Guided Fragment-Based Approach for the Design of tRNALys3 Ligands

Author: Carine Tisné, Laurent Micouin, Frédéric Dardel, Thomas Lecourt, Florence Chung, Synthèse et structure de molécules d'interet pharmacologique (SSMIP), Université Paris Descartes - Paris 5 (UPD5) - Centre National de la Recherche Scientifique (CNRS), Laboratoire de cristallographie et RMN biologiques (LCRB - UMR 8015), ANRS, STREP SVG-V-RNA FP6, Université Paris Descartes - Paris 5 (UPD5)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5), and Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)
Subjects: MESH: Antiviral Agents, MESH : Drug Design, Magnetic Resonance Spectroscopy, Stereochemistry, [CHIM.THER] Chemical Sciences/Medicinal Chemistry, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, MESH: Drug Design, MESH: RNA, Transfer, Lys, Ligands, Antiviral Agents, 01 natural sciences, Catalysis, 03 medical and health sciences, Fragment (logic), MESH: Ligands, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Molecule, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH : Reverse Transcriptase Inhibitors, 030304 developmental biology, MESH : Ligands, 0303 health sciences, MESH: Magnetic Resonance Spectroscopy, 010405 organic chemistry, Ligand, Chemistry, General Medicine, General Chemistry, Combinatorial chemistry, Reverse transcriptase, MESH : Antiviral Agents, 3. Good health, 0104 chemical sciences, Dissociation constant, MESH : RNA, Transfer, Lys, Drug Design, Transfer RNA, MESH : Magnetic Resonance Spectroscopy, RNA, Transfer, Lys, Reverse Transcriptase Inhibitors, MESH: Reverse Transcriptase Inhibitors
Abstract: Despite recent breakthroughs, the de novo design of new compounds that specifically bind to structured RNAs is still a standing challenge. The aim of this study was to find molecules that bind to tRNALys3 and serve as leads for inhibitors of the formation of the HIV-1 reverse transcription initiation complex. We used NMR screening to identify ligands from spectral changes induced by their binding on the target. Using a fragment-based approach, a selective ligand of tRNALys3 with micromolar dissociation constant has been synthesised for the first time.
Published: 2007

5. Intravoxel incoherent motion diffusion-weighted imaging in nonalcoholic fatty liver disease: a 3.0-T MR study

Author: Romaric Loffroy, Jean-Michel Petit, Patrick Hillon, Bruno Vergès, Boris Guiu, Serge Aho, Pierre-Henri Lefevre, Sylvain Favelier, David Masson, Violaine Capitan, Denis Krausé, Jean-Pierre Cercueil, Service de radiologie et d'Imagerie médicale diagnostique et thérapeutique (CHU de Dijon), Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ), Service de Diabétologie, Service d'épidémiologie et d'hygiène hospitalières (CHU de Dijon), Lipides - Nutrition - Cancer (U866) ( LNC ), Université de Bourgogne ( UB ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon ( ENSBANA ), Laboratoire Electronique, Informatique et Image ( Le2i ), Université de Bourgogne ( UB ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique ( CNRS ), Service d'Hépato-Gastroentérologie, Hôpital du Bocage, Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ) -Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ), Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon), Service d'Endocrinologie, Diabétologie et Maladies Métaboliques (CHU de Dijon), Lipides - Nutrition - Cancer (U866) (LNC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Bourgogne (UB)-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Laboratoire Electronique, Informatique et Image [UMR6306] (Le2i), Université de Bourgogne (UB)-École Nationale Supérieure d'Arts et Métiers (ENSAM), Arts et Métiers Sciences et Technologies, HESAM Université (HESAM)-HESAM Université (HESAM)-Arts et Métiers Sciences et Technologies, HESAM Université (HESAM)-HESAM Université (HESAM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS), and Service d'hépato-gastroentérologie et cancérologie digestive (CHU de Dijon)
Subjects: Male, Cirrhosis, Magnetic Resonance Spectroscopy, MESH : Fatty Liver, [SDV.IB.IMA]Life Sciences [q-bio]/Bioengineering/Imaging, MESH : Aged, MESH : Prospective Studies, 030218 nuclear medicine & medical imaging, MESH: Linear Models, 0302 clinical medicine, Nuclear magnetic resonance, MESH: Aged, 80 and over, MESH : Diabetes Mellitus, Type 2, Non-alcoholic Fatty Liver Disease, MESH : Linear Models, Nonalcoholic fatty liver disease, MESH : Female, Prospective Studies, MESH: Fatty Liver, Intravoxel incoherent motion, [ SDV.IB.IMA ] Life Sciences [q-bio]/Bioengineering/Imaging, Aged, 80 and over, MESH: Aged, MESH: Statistics, Nonparametric, MESH: Middle Aged, [ INFO.INFO-IM ] Computer Science [cs]/Medical Imaging, Fatty liver, Middle Aged, MESH : Adult, MESH : Diffusion Magnetic Resonance Imaging, 3. Good health, 030220 oncology & carcinogenesis, Potential confounder, Female, Radiology, MESH: Diabetes Mellitus, Type 2, Adult, medicine.medical_specialty, MESH : Male, MESH: Diffusion Magnetic Resonance Imaging, Statistics, Nonparametric, 03 medical and health sciences, medicine, [INFO.INFO-IM]Computer Science [cs]/Medical Imaging, Humans, Radiology, Nuclear Medicine and imaging, MESH : Middle Aged, MESH : Aged, 80 and over, MESH : Statistics, Nonparametric, Aged, MESH: Humans, business.industry, MESH: Magnetic Resonance Spectroscopy, MESH : Humans, MESH: Biological Markers, MESH: Adult, medicine.disease, Mr imaging, MESH: Male, MESH: Prospective Studies, Fatty Liver, MESH : Biological Markers, Diffusion Magnetic Resonance Imaging, Diabetes Mellitus, Type 2, Linear Models, MESH : Magnetic Resonance Spectroscopy, Steatosis, business, MESH: Female, Biomarkers, Diffusion MRI
Abstract: International audience; PURPOSE: To compare pure molecular diffusion, D, perfusion-related diffusion, D*, and perfusion fraction, f, determined from diffusion-weighted (DW) magnetic resonance (MR) imaging on the basis of the intravoxel incoherent motion (IVIM) theory in patients with type 2 diabetes with and without liver steatosis. MATERIALS AND METHODS: This prospective study was approved by the appropriate ethics committee, and written informed consent was obtained from all patients. Between December 2009 and September 2011, 108 patients with type 2 diabetes (51 men, 57 women; mean age, 50 years) underwent 3.0-T single-voxel point-resolved proton MR spectroscopy of the liver (segment VII) to calculate the liver fat fraction from water (4.76 ppm) and methylene (1.33 ppm) peaks, corrected for T1 and T2 decay. Steatosis was defined as a liver fat fraction of at least 5.56%. DW imaging was performed by using a single-shot echo-planar sequence with 11 b values (0, 5, 15, 25, 35, 50, 100, 200, 400, 600, 800 sec/mm2). Liver D, D*, and f were measured and compared in patients with and patients without steatosis (Mann-Whitney test). RESULTS: The mean liver fat fraction was 7.8% (standard deviation, 9%; range, 0.99%-45%). Forty patients had liver steatosis. D was significantly lower in steatotic compared with nonsteatotic livers (mean, 1.03×10(-3) mm2/sec±0.23 [standard deviation] vs 1.24×10(-3) mm2/sec±0.15, respectively; P
Published: 2012

6. Chemical optimization of new ligands of the low-density lipoprotein receptor as potential vectors for central nervous system targeting

Author: Jean Martinez, Michel Khrestchatisky, Vincent Lisowski, Marion David, Franck Debarbieux, Patrick Vlieghe, Karima Abouzid, Aude Faucon, Nadine Payrot, Geneviève Rougon, Guillaume Jacquot, Nicolas Floquet, Jean-Daniel Malcor, Neurobiologie des interactions cellulaires et neurophysiopathologie - NICN (NICN), Université de la Méditerranée - Aix-Marseille 2-Centre National de la Recherche Scientifique (CNRS), Centre de génétique et de physiologie moléculaire et cellulaire (CGPhiMC), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Institut Cochin (UMR_S567 / UMR 8104), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5), Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut de Biologie du Développement de Marseille (IBDM), Aix Marseille Université (AMU)-Collège de France (CdF)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université de la Méditerranée - Aix-Marseille 2, Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Neurobiologie des interactions cellulaires et neurophysiopathologie - NICN ( NICN ), Centre National de la Recherche Scientifique ( CNRS ) -Université de la Méditerranée - Aix-Marseille 2, Centre de génétique et de physiologie moléculaire et cellulaire ( CGPhiMC ), Centre National de la Recherche Scientifique ( CNRS ) -Université Claude Bernard Lyon 1 ( UCBL ), Institut Cochin ( UMR_S567 / UMR 8104 ), Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] ( IBMM ), Ecole Nationale Supérieure de Chimie de Montpellier ( ENSCM ) -Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ), Institut de Biologie du Développement de Marseille ( IBDM ), Aix Marseille Université ( AMU ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Institut National de la Recherche Agronomique ( INRA ) -Aix Marseille Université ( AMU ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), and Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)
Subjects: Models, Molecular, Magnetic Resonance Spectroscopy, Phage display, MESH: Transcytosis, MESH : Receptors, LDL, Peptide, Ligands, 01 natural sciences, MESH : Blood-Brain Barrier, MESH: Blood-Brain Barrier, MESH: Spinal Cord, Mice, MESH: Structure-Activity Relationship, MESH : Peptides, Cyclic, MESH : Structure-Activity Relationship, Drug Discovery, MESH: Ligands, MESH : Fluorescent Dyes, MESH: Animals, Receptor, chemistry.chemical_classification, MESH : Ligands, 0303 health sciences, MESH : Transcytosis, Chemistry, MESH: Fluorescent Dyes, Cell biology, Spinal Cord, Transcytosis, Biochemistry, Blood-Brain Barrier, Drug delivery, MESH: Oligopeptides, Molecular Medicine, Oligopeptides, MESH: Models, Molecular, MESH : Oligopeptides, MESH : Models, Molecular, MESH : Mice, Inbred C57BL, Biopanning, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, 010402 general chemistry, Peptides, Cyclic, Structure-Activity Relationship, 03 medical and health sciences, MESH: Mice, Inbred C57BL, MESH : Mice, Animals, Humans, MESH: Mice, MESH: Peptides, Cyclic, Fluorescent Dyes, 030304 developmental biology, MESH: Humans, [ SDV.BC ] Life Sciences [q-bio]/Cellular Biology, MESH: Magnetic Resonance Spectroscopy, MESH : Humans, MESH : Spinal Cord, 0104 chemical sciences, Mice, Inbred C57BL, Receptors, LDL, Docking (molecular), MESH: Receptors, LDL, LDL receptor, MESH : Magnetic Resonance Spectroscopy, MESH : Animals
Abstract: International audience; Drug delivery to the central nervous system is hindered by the presence of physiological barriers such as the blood-brain barrier. To accomplish the task of nutrient transport, the brain endothelium is endowed with various transport systems, including receptor-mediated transcytosis (RMT). This system can be used to shuttle therapeutics into the central nervous system (CNS) in a noninvasive manner. Therefore, the low-density lipoprotein receptor (LDLR) is a relevant target for delivering drugs. From an initial phage display biopanning, a series of peptide ligands for the LDLR was optimized leading to size reduction and improved receptor binding affinity with the identification of peptide 22 and its analogues. Further real-time biphoton microscopy experiments on living mice demonstrated the ability of peptide 22 to efficiently and quickly cross CNS physiological barriers. This validation of peptide 22 led us to explore its binding on the extracellular LDLR domain from an NMR-oriented structural study and docking experiments.
Published: 2012

7. Tumor volume and metabolism of prostate cancer determined by proton magnetic resonance spectroscopic imaging at 3T without endorectal coil reveal potential clinical implications in the context of radiation oncology

Author: Mathilde Funes de la Vega, Céline Mirjolet, Philippe Maingon, Alexandre Cochet, Paul Walker, François Brunotte, Douraied Ben Salem, Sébastien Parfait, Franck Bonnetain, Mélanie Liegard, Gilles Créhange, Luc Cormier, Centre Régional de Lutte contre le cancer Georges-François Leclerc [Dijon] (UNICANCER/CRLCC-CGFL), UNICANCER, Laboratoire Electronique, Informatique et Image [UMR6306] (Le2i), Université de Bourgogne (UB)-École Nationale Supérieure d'Arts et Métiers (ENSAM), Arts et Métiers Sciences et Technologies, HESAM Université (HESAM)-HESAM Université (HESAM)-Arts et Métiers Sciences et Technologies, HESAM Université (HESAM)-HESAM Université (HESAM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS), Centre d'épidémiologie des populations (CEP), Université de Bourgogne (UB)-Centre Régional de Lutte contre le cancer Georges-François Leclerc [Dijon] (UNICANCER/CRLCC-CGFL), UNICANCER-UNICANCER, Department of Anatomo-Pathology, Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon), Service d'Urologie [CHU de Dijon], Université de Bourgogne (UB)-Centre National de la Recherche Scientifique (CNRS)-École Nationale Supérieure d'Arts et Métiers (ENSAM), HESAM Université (HESAM)-HESAM Université (HESAM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Groupe d'Etude de la Thrombose de Bretagne Occidentale (GETBO), Institut Brestois Santé Agro Matière (IBSAM), Université de Brest (UBO)-Université de Brest (UBO)-Université de Brest (UBO), Centre Régional de Lutte contre le cancer - Centre Georges-François Leclerc ( CRLCC - CGFL ), Laboratoire Electronique, Informatique et Image ( Le2i ), Université de Bourgogne ( UB ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique ( CNRS ), Groupe d'Etude de la Thrombose de Bretagne Occidentale ( GETBO ), Université de Brest ( UBO ), Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ), Service d'urologie, Centre d'épidémiologie des populations ( CEP ), Université de Bourgogne ( UB ) -Centre Régional de Lutte contre le cancer - Centre Georges-François Leclerc ( CRLCC - CGFL ), Université de Brest (UBO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Brestois Santé Agro Matière (IBSAM), Université de Brest (UBO)-Université de Brest (UBO), and Université de Brest (UBO)-Institut Brestois Santé Agro Matière (IBSAM)
Subjects: Male, Cancer Research, MESH : Polyamines, MESH: Tumor Burden, Magnetic Resonance Spectroscopy, MESH : Retrospective Studies, [SDV]Life Sciences [q-bio], MESH : Aged, MESH: Risk Assessment, MESH : Choline, Choline, 030218 nuclear medicine & medical imaging, chemistry.chemical_compound, Prostate cancer, 0302 clinical medicine, Prostate, MESH : Tumor Markers, Biological, Polyamines, MESH : Neoplasm Staging, Stage (cooking), MESH : Prostate-Specific Antigen, MESH : Risk Assessment, MESH: Aged, Radiation, MESH : Prognosis, MESH: Middle Aged, medicine.diagnostic_test, [ INFO.INFO-IM ] Computer Science [cs]/Medical Imaging, MESH : Tumor Burden, MESH: Creatine, MESH: Choline, Magnetic resonance spectroscopic imaging, MESH: Neoplasm Staging, Middle Aged, Prognosis, MESH : Creatine, Tumor Burden, 3. Good health, MESH: Prostate-Specific Antigen, medicine.anatomical_structure, Oncology, 030220 oncology & carcinogenesis, MESH : Prostatic Neoplasms, MESH: Citric Acid, MESH : Male, Context (language use), MESH : Citric Acid, Creatine, Risk Assessment, Citric Acid, MESH: Prognosis, 03 medical and health sciences, Biomarkers, Tumor, medicine, [INFO.INFO-IM]Computer Science [cs]/Medical Imaging, Humans, Radiology, Nuclear Medicine and imaging, MESH : Middle Aged, MESH: Polyamines, Aged, Neoplasm Staging, Retrospective Studies, MESH: Humans, [ SDV ] Life Sciences [q-bio], business.industry, MESH: Magnetic Resonance Spectroscopy, MESH : Humans, Prostatic Neoplasms, Magnetic resonance imaging, MESH: Retrospective Studies, Prostate-Specific Antigen, medicine.disease, MESH: Male, chemistry, MESH: Prostatic Neoplasms, MESH: Tumor Markers, Biological, MESH : Magnetic Resonance Spectroscopy, business, Nuclear medicine
Abstract: International audience; Abstract PURPOSE: To determine whether a relationship exists between the tumor volume (TV) or relative choline content determined using magnetic resonance spectroscopy imaging (MRSI) at 3T and the clinical prognostic parameters for patients with localized prostate cancer (PCa). METHODS AND MATERIALS: A total of 72 men (mean age, 67.8 ± 6.2 years) were stratified as having low-risk (n = 26), intermediate-risk (n = 24), or high-risk (n = 22) PCa. MRSI was performed at 3T using a phased-array coil. Spectra are expressed as the total choline/citrate, total choline plus creatine/citrate, and total choline plus polyamines plus creatine/citrate ratios. The mean ratio of the most pathologic voxels and the MRSI-based TV were also determined. RESULTS: The mean values of the total choline/citrate, total choline plus creatine/citrate, and total choline plus polyamine plus creatine/citrate ratios were greater for Stage T2b or greater tumors vs. Stage T2a or less tumors: 7.53 ± 13.60 vs. 2.31 ± 5.65 (p = .018), 8.98 ± 14.58 vs. 2.56 ± 5.70 (p = .016), and 10.32 ± 15.47 vs. 3.55 ± 6.16 (p = .014), respectively. The mean MRSI-based TV for Stage T2b or greater and Stage T2a or less tumors was significantly different (2.23 ± 2.62 cm(3) vs. 1.26 ± 2.06 cm(3), respectively; p = .030). This TV correlated with increased prostate-specific antigen levels (odds ratio, 1.293; p = .012). Patients with high-risk PCa had a larger TV than did the patients with intermediate-risk PCa. A similar result was found for the intermediate-risk group compared with the low-risk group (odds ratio, 1.225; p = .041). CONCLUSION: Biomarkers expressing the relative choline content and TV were significant parameters for the localization of PCa and could be helpful for determining the prognosis more accurately.
Published: 2011

8. Cadmium-glutathione solution structures provide new insights into heavy metal detoxification

Author: Delalande, Olivier, Desvaux, Hervé, Godat, Emmanuel, Valleix, Alain, Junot, Christophe, Labarre, Jean, Boulard, Yves, Service de Biologie Intégrative et Génétique Moléculaire ( SBIGeM ), Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), Laboratoire Claude Fréjacques ( LCF - URA 331 ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire d'Etude du Métabolisme des Médicaments ( LEMM ), Service de Pharmacologie et Immunoanalyse ( SPI ), Département Médicaments et Technologies pour la Santé ( DMTS ), Direction de Recherche Fondamentale (CEA) ( DRF (CEA) ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) ( DRF (CEA) ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Département Médicaments et Technologies pour la Santé ( DMTS ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay, Service de Chimie Bio-Organique et de Marquage ( SCBM ), De Villemeur, Hervé, Service de Biologie Intégrative et Génétique Moléculaire (SBIGeM), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Laboratoire Claude Fréjacques (LCF - URA 331), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire d'Etude du Métabolisme des Médicaments (LEMM), Service de Pharmacologie et Immunoanalyse (SPI), Médicaments et Technologies pour la Santé (MTS), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Médicaments et Technologies pour la Santé (MTS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), and Service de Chimie Bio-Organique et de Marquage (SCBM)
Subjects: Models, Molecular, MESH: Hydrogen-Ion Concentration, Magnetic Resonance Spectroscopy, MESH : Models, Molecular, MESH: Molecular Structure, [ SDV.TOX ] Life Sciences [q-bio]/Toxicology, MESH: Cadmium, MESH : Saccharomyces cerevisiae, Saccharomyces cerevisiae, MESH: Solutions, MESH : Hydrogen-Ion Concentration, MESH : Solutions, MESH : Cadmium, MESH: Glutathione, Molecular Structure, MESH: Magnetic Resonance Spectroscopy, MESH : Metabolic Detoxication, Drug, MESH : Glutathione, Hydrogen-Ion Concentration, MESH: Metabolic Detoxication, Drug, MESH: Saccharomyces cerevisiae, Glutathione, [SDV.TOX] Life Sciences [q-bio]/Toxicology, Solutions, MESH: Dimerization, MESH : Dimerization, [SDV.TOX]Life Sciences [q-bio]/Toxicology, Inactivation, Metabolic, MESH : Magnetic Resonance Spectroscopy, Dimerization, MESH: Models, Molecular, MESH : Molecular Structure, Cadmium
Abstract: International audience; Cadmium is a heavy metal and a pollutant that can be found in large quantities in the environment from industrial waste. Its toxicity for living organisms could arise from its ability to alter thiol-containing cellular components. Glutathione is an abundant tripeptide (γ-Glu-Cys-Gly) that is described as the first line of defence against cadmium in many cell types. NMR experiments for structure and dynamics determination, molecular simulations, competition reactions for metal chelation by different metabolites (γ-Glu-Cys-Gly, α-Glu-Cys-Gly and γ-Glu-Cys) combined with biochemical and genetics experiments have been performed to propose a full description of bio-inorganic reactions occurring in the early steps of cadmium detoxification processes. Our results give unambiguous information about the spontaneous formation, under physiological conditions, of the Cd(GS)(2) complex, about the nature of ligands involved in cadmium chelation by glutathione, and provide insights on the structures of Cd(GS)(2) complexes in solution at different pH. We also show that γ-Glu-Cys, the precursor of glutathione, forms a stable complex with cadmium, but biological studies of the first steps of cadmium detoxification reveal that this complex does not seem to be relevant for this purpose.
Published: 2010

9. Insight into the structure of the pUL89 C-terminal domain of the human cytomegalovirus terminase complex

Author: Couvreux, S, Hantz, S., Marquant, R., Champier, G., Alain, S., Morellet, N., Bouaziz, S., Couvreux, A., Teaching hospital, CHU Limoges, Ecosystèmes forestiers (UR EFNO), Institut national de recherche en sciences et technologies pour l'environnement et l'agriculture (IRSTEA), Institut d'électronique fondamentale (IEF), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), Raherison, Sophie, Unité de Pharmacologie Chimique et Génétique (UPCG - UMR_S 640/UMR 8151), Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut des sciences du Médicament -Toxicologie - Chimie - Environnement (IFR71), Institut de Recherche pour le Développement (IRD)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Biologie moléculaire et cellulaire des microorganismes (EA3175), Université de Limoges (UNILIM)-Génomique, Environnement, Immunité, Santé, Thérapeutique (GEIST FR CNRS 3503)-Institut National de la Santé et de la Recherche Médicale (INSERM), Service de Bactériologie, Virologie, Hygiène [CHU Limoges], Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Descartes - Paris 5 (UPD5)-Institut des sciences du Médicament -Toxicologie - Chimie - Environnement (IFR71), Institut National de la Santé et de la Recherche Médicale (INSERM)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Ecole Nationale Supérieure de Chimie de Paris - Chimie ParisTech-PSL (ENSCP), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD)-Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC), Centre National de la Recherche Scientifique (CNRS) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Université Paris Descartes - Paris 5 (UPD5) - Institut des sciences du Médicament -Toxicologie - Chimie - Environnement (IFR71), Institut National de la Santé et de la Recherche Médicale (INSERM) - Ecole Nationale Supérieure de Chimie de Paris- Chimie ParisTech-PSL (ENSCP) - Centre National de la Recherche Scientifique (CNRS) - Institut de Recherche pour le Développement (IRD) - Université Paris Descartes - Paris 5 (UPD5) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Ecole Nationale Supérieure de Chimie de Paris- Chimie ParisTech-PSL (ENSCP) - Centre National de la Recherche Scientifique (CNRS) - Institut de Recherche pour le Développement (IRD) - Université Paris Descartes - Paris 5 (UPD5), and Université de Limoges (UNILIM) - Génomique, Environnement, Immunité, Santé, Thérapeutique (GEIST FR CNRS 3503) - Institut National de la Santé et de la Recherche Médicale (INSERM)
Subjects: Models, Molecular, Magnetic Resonance Spectroscopy, MESH : Molecular Sequence Data, MESH : DNA, Cytomegalovirus, MESH: Protein Structure, Secondary, MESH: Amino Acid Sequence, Protein Structure, Secondary, MESH: Protein Structure, Tertiary, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, MESH: Endonucleases, MESH : RNA, MESH : Endonucleases, MESH : Viral Proteins, [SDV.MP.VIR] Life Sciences [q-bio]/Microbiology and Parasitology/Virology, MESH : Sequence Alignment, MESH : Amino Acid Sequence, MESH: DNA, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, [SDV.MHEP.MI] Life Sciences [q-bio]/Human health and pathology/Infectious diseases, MESH : Protein Structure, Tertiary, MESH: Biocatalysis, MESH: Models, Molecular, MESH: Cytomegalovirus, MESH : Models, Molecular, Molecular Sequence Data, MESH: Sequence Alignment, MESH : Endodeoxyribonucleases, MESH : Cytomegalovirus, Viral Proteins, MESH: RNA, Humans, Amino Acid Sequence, MESH: Endodeoxyribonucleases, Endodeoxyribonucleases, MESH: Humans, MESH: Molecular Sequence Data, MESH: Magnetic Resonance Spectroscopy, MESH : Humans, DNA, Endonucleases, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, MESH: Viral Proteins, Protein Structure, Tertiary, Biocatalysis, RNA, MESH : Magnetic Resonance Spectroscopy, MESH : Protein Structure, Secondary, MESH : Biocatalysis, [SDV.MP.BAC] Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, Sequence Alignment
Abstract: International audience; In a previous study, we identified 12 conserved domains within pUL89, the small terminase subunit of the human cytomegalovirus. A latter study showed that the fragment pUL89(580-600) plays an important role in the formation of the terminase complex by interacting with the large terminase subunit pUL56. In this study, analysis was performed to solve the structure of pUL89(568-635) in 50% H2O/50% acetonitrile (v/v). We showed that pUL89(568-635) consists of four alpha helices, but we did not identify any tertiary structure. The fragment 580-600 formed an amphipathic alpha helix, which had a hydrophobic side highly conserved among herpesviral homologs of pUL89; this was not observed for its hydrophilic side. The modeling of pUL89(457-612) using the recognition fold method allowed us to position pUL89(580-600) within this domain. The theoretical structure highlighted three important features. First, we identified a metal-binding pocket containing residues Asp(463), Glu(534), and Glu(588), which are highly conserved among pUL89 homologs. Second, the model predicted a positively charged surface able to interact with the DNA duplex during the nicking event. Third, a hydrophobic patch on the top of the catalytic site suggested that this may constitute part of the pUL89 site recognized by pUL56 potentially involved in DNA binding.
Published: 2010

10. Complications and failure of uterine artery embolisation for intractable postpartum haemorrhage

Author: Tixier, Hervé, Loffroy, Romaric, Guiu, Boris, Coulange, L., Butori, Noémie, Cercueil, Jean-Pierre, Douvier, Serge, Krausé, Denis, Sagot, Paul, Service de gynécologie obstétrique, Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ) -Hôpital du Bocage, Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ), Service de radiologie et d'Imagerie médicale diagnostique et thérapeutique (CHU de Dijon), Centre d'épidémiologie des populations ( CEP ), Université de Bourgogne ( UB ) -Centre Régional de Lutte contre le cancer - Centre Georges-François Leclerc ( CRLCC - CGFL ), Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon)-Hôpital du Bocage, Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon), Centre d'épidémiologie des populations (CEP), Université de Bourgogne (UB)-Centre Régional de Lutte contre le cancer Georges-François Leclerc [Dijon] (UNICANCER/CRLCC-CGFL), UNICANCER-UNICANCER, Guiu, Boris, and Service de Gynécologie Obstétrique, Médecine Foetale et Stérilité Conjugale - Chirurgie Gynécologie et Oncologique [CHU de Dijon]
Subjects: MESH: Humans, MESH : Fatty Liver, MESH: Uterine Artery Embolization, MESH: Magnetic Resonance Spectroscopy, MESH: Treatment Failure, MESH : Humans, MESH : Liver, [SDV.MHEP.HEG]Life Sciences [q-bio]/Human health and pathology/Hépatology and Gastroenterology, MESH: Gelatin Sponge, Absorbable, MESH : Postpartum Hemorrhage, [SDV.MHEP.HEG] Life Sciences [q-bio]/Human health and pathology/Hépatology and Gastroenterology, MESH: Postpartum Hemorrhage, MESH : Uterine Artery Embolization, MESH : Pregnancy, MESH: Pregnancy, MESH : Treatment Failure, MESH : Magnetic Resonance Spectroscopy, MESH : Female, MESH : Gelatin Sponge, Absorbable, [ SDV.MHEP.HEG ] Life Sciences [q-bio]/Human health and pathology/Hépatology and Gastroenterology, MESH: Fatty Liver, MESH: Female, ComputingMilieux_MISCELLANEOUS, MESH: Liver
Abstract: International audience
Published: 2009

11. Structure-activity relationship analysis of the peptide deformylase inhibitor 5-bromo-1H-indole-3-acetohydroxamic acid

Author: Frédéric Dardel, Valéry Larue, Thierry Meinnel, Coralie Soulama, Carmela Giglione, Isabelle Artaud, Yann Duroc, Alexis Denis, Sylvain Petit, Carole Léon, Laboratoire Léon Brillouin (LLB - UMR 12), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay, Institut Jean-Pierre Bourgin (IJPB), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Laboratoire de cristallographie et RMN biologiques (LCRB - UMR 8015), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut des sciences du végétal (ISV), Centre National de la Recherche Scientifique (CNRS), Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques (LCBPT - UMR 8601), CNRS Region Ile-de-France Agence Nationale de la Recherche (ANR, France) ANR-06-MIME-010, Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5), Laboratoire Léon Brillouin ( LLB - UMR 12 ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), Institut Jean-Pierre Bourgin ( IJPB ), Institut National de la Recherche Agronomique ( INRA ) -AgroParisTech, Laboratoire de cristallographie et RMN biologiques ( LCRB - UMR 8015 ), Université Paris Descartes - Paris 5 ( UPD5 ) -Centre National de la Recherche Scientifique ( CNRS ), Institut des sciences du végétal ( ISV ), Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques ( LCBPT - UMR 8601 ), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), and Université Paris Descartes - Paris 5 (UPD5)-Centre National de la Recherche Scientifique (CNRS)
Subjects: Models, Molecular, MESH: Amidohydrolases, MESH: Hydroxamic Acids, [ SDV.BV ] Life Sciences [q-bio]/Vegetal Biology, Magnetic Resonance Spectroscopy, Peptide, Hydroxamic Acids, 01 natural sciences, Biochemistry, antibiotics, chemistry.chemical_compound, Peptide deformylase, MESH: Structure-Activity Relationship, MESH : Indoles, Drug Discovery, MESH : Structure-Activity Relationship, inhibitors, Enzyme Inhibitors, General Pharmacology, Toxicology and Pharmaceutics, MESH : Anti-Bacterial Agents, Actinonin, chemistry.chemical_classification, MESH: Indoles, 0303 health sciences, peptide deformylase, MESH: Microbial Sensitivity Tests, Chemistry, MESH : Spectrometry, Mass, Electrospray Ionization, Anti-Bacterial Agents, MESH : Amidohydrolases, MESH: Enzyme Inhibitors, Molecular Medicine, Antibacterial activity, Lead compound, MESH: Models, Molecular, Spectrometry, Mass, Electrospray Ionization, Stereochemistry, MESH : Models, Molecular, Microbial Sensitivity Tests, MESH: Spectrometry, Mass, Electrospray Ionization, Amidohydrolases, Structure-Activity Relationship, 03 medical and health sciences, NMR spectroscopy, MESH: Anti-Bacterial Agents, Structure–activity relationship, Potency, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, 030304 developmental biology, Pharmacology, Indole test, MESH : Enzyme Inhibitors, MESH : Hydroxamic Acids, 010405 organic chemistry, MESH: Magnetic Resonance Spectroscopy, Organic Chemistry, indoles, 0104 chemical sciences, MESH : Magnetic Resonance Spectroscopy, MESH : Microbial Sensitivity Tests
Abstract: International audience; The lead compound 5-bromoindolyl-3-acetohydroxamic acid (10) was recently identified as a potent inhibitor of bacterial peptide deformylases (PDFs). The synthesis and associated activities of new variants were investigated at position 5 to optimize the fit at the S1' subsite and at position 1 to improve both potency and antibacterial activity. A morphomimetic series, termed "reverse-indole" was synthesized. The indole derivatives remain selective in vitro inhibitors of PDF2 over PDF1. Bromide is the best group at position 5 and cannot be replaced by bulkier substituents. In this series, an N-benzyl group at position 1 in 19 e improves the potency relative to 10. In the case of PDF1, and unlike PDF2, potency is increased as the alkyl chain becomes longer and more ramified. These data support the results of NMR footprinting experiments that were performed with (15)N-labeled Ni-PDF and the corresponding 3-acetic acid derivatives. Most of the compounds have antibacterial activities toward B. subtilis, but are inefficient toward E. coli owing to active removal by the major efflux pumps. Among the reverse-indole derivatives, 23 c, which is the exact mirror image of 19 e, shows strong potency in vitro against PDF2, but little against PDF1, although this compound displays significant antibacterial activity toward an efflux-minus mutant of E. coli. All the compounds were assessed with major pathogenic bacteria, but most of them are inefficient antibacterial agents. The reverse-indole compounds 23 a and 23 c have potency against S. pneumoniae that is similar to that of actinonin.
Published: 2009

12. Magnetic resonance imaging and spectroscopy for quantification of hepatic steatosis: urgent need for standardization!

Author: Patrick Hillon, Boris Guiu, Romaric Loffroy, Jean-Michel Petit, Guiu, Boris, Service de radiologie et d'Imagerie médicale diagnostique et thérapeutique (CHU de Dijon), Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon), Lipides - Nutrition - Cancer (U866) (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA), Service d'hépato-gastroentérologie et cancérologie digestive (CHU de Dijon), Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ), Lipides - Nutrition - Cancer (U866) ( LNC ), Université de Bourgogne ( UB ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon ( ENSBANA ), Service d'Hépato-Gastroentérologie, Hôpital du Bocage, Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ) -Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Bourgogne (UB)-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement
Subjects: medicine.medical_specialty, MESH : Fatty Liver, 030218 nuclear medicine & medical imaging, MESH: Magnetic Resonance Imaging, 03 medical and health sciences, 0302 clinical medicine, Nuclear magnetic resonance, MESH : Lipid Metabolism, MESH : Magnetic Resonance Imaging, medicine, MESH : Predictive Value of Tests, Spectroscopy, MESH: Fatty Liver, ComputingMilieux_MISCELLANEOUS, MESH: Lipid Metabolism, MESH: Humans, medicine.diagnostic_test, Hepatology, business.industry, MESH: Magnetic Resonance Spectroscopy, MESH : Humans, Fatty liver, Magnetic resonance imaging, Lipid metabolism, [SDV.MHEP.HEG]Life Sciences [q-bio]/Human health and pathology/Hépatology and Gastroenterology, Nuclear magnetic resonance spectroscopy, medicine.disease, [SDV.MHEP.HEG] Life Sciences [q-bio]/Human health and pathology/Hépatology and Gastroenterology, MESH: Predictive Value of Tests, 3. Good health, 030220 oncology & carcinogenesis, Predictive value of tests, MESH : Magnetic Resonance Spectroscopy, [ SDV.MHEP.HEG ] Life Sciences [q-bio]/Human health and pathology/Hépatology and Gastroenterology, Radiology, Steatosis, business
Abstract: International audience
Published: 2009

13. Quantification of liver fat content: comparison of triple-echo chemical shift gradient-echo imaging and in vivo proton MR spectroscopy

Author: David Masson, Denis Krausé, Jean-Michel Petit, Romaric Loffroy, Patrick Hillon, Douraied Ben Salem, Jean-Pierre Cercueil, Boris Guiu, Serge Aho, Service de radiologie et d'Imagerie médicale diagnostique et thérapeutique (CHU de Dijon), Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ), Unité de Génétique Moléculaire Animale ( UGMA ), Université de Limoges ( UNILIM ) -Institut National de la Recherche Agronomique ( INRA ), Groupe d'Etude de la Thrombose de Bretagne Occidentale ( GETBO ), Université de Brest ( UBO ), Département de radiologie [Brest] ( DR - Brest ), Centre Hospitalier Régional Universitaire de Brest ( CHRU Brest ), Service d'Ophtalmologie (CHU de Dijon), Lipides - Nutrition - Cancer (U866) ( LNC ), Université de Bourgogne ( UB ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon ( ENSBANA ), Service d'Hépato-Gastroentérologie, Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ) -Hôpital du Bocage, Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon), Unité de Génétique Moléculaire Animale (UGMA), Université de Limoges (UNILIM)-Institut National de la Recherche Agronomique (INRA), Groupe d'Etude de la Thrombose de Bretagne Occidentale (GETBO), Université de Brest (UBO)-Institut Brestois Santé Agro Matière (IBSAM), Université de Brest (UBO), Département de radiologie [Brest] (DR - Brest), Centre Hospitalier Régional Universitaire de Brest (CHRU Brest), Lipides - Nutrition - Cancer (U866) (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA), Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon)-Hôpital du Bocage, Unité de Génétique Moléculaire Animale (UMR GMA), Université de Brest (UBO)-Université de Brest (UBO), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Bourgogne (UB)-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, and Service d'hépato-gastroentérologie et cancérologie digestive (CHU de Dijon)
Subjects: Male, Magnetic Resonance Spectroscopy, MESH: Echo-Planar Imaging, MESH : Fatty Liver, [SDV]Life Sciences [q-bio], MESH : Aged, MESH : Prospective Studies, MESH : Mathematical Computing, 030218 nuclear medicine & medical imaging, MESH: Magnetic Resonance Imaging, 0302 clinical medicine, Nuclear magnetic resonance, MESH: Aged, 80 and over, MESH : Diabetes Mellitus, Type 2, Image Processing, Computer-Assisted, Medicine, MESH : Female, Prospective Studies, MESH: Mathematical Computing, MESH: Fatty Liver, Mathematical Computing, MESH: Aged, Aged, 80 and over, MESH: Middle Aged, medicine.diagnostic_test, Echo-Planar Imaging, Echo (computing), Middle Aged, MESH: Image Processing, Computer-Assisted, Magnetic Resonance Imaging, Liver, Content (measure theory), 030211 gastroenterology & hepatology, Female, MESH : Software, MESH: Image Enhancement, MESH : Sensitivity and Specificity, MESH : Image Processing, Computer-Assisted, MESH: Diabetes Mellitus, Type 2, MESH : Male, Sensitivity and Specificity, 03 medical and health sciences, MESH: Software, Flip angle, In vivo, MESH : Magnetic Resonance Imaging, Liver fat, Humans, Radiology, Nuclear Medicine and imaging, MESH : Middle Aged, Spectroscopy, MESH : Aged, 80 and over, Aged, MESH: Humans, MESH : Echo-Planar Imaging, [ SDV ] Life Sciences [q-bio], business.industry, MESH: Magnetic Resonance Spectroscopy, MESH : Humans, MESH : Liver, Magnetic resonance imaging, Image Enhancement, Proton mr spectroscopy, MESH: Male, MESH: Prospective Studies, MESH: Sensitivity and Specificity, Fatty Liver, Diabetes Mellitus, Type 2, MESH : Magnetic Resonance Spectroscopy, MESH : Image Enhancement, business, Nuclear medicine, MESH: Female, Software, MESH: Liver
Abstract: International audience; PURPOSE: To validate a triple-echo gradient-echo sequence for measuring the fat content of the liver, by using hydrogen 1((1)H) magnetic resonance (MR) spectroscopy as the reference standard. MATERIALS AND METHODS: This prospective study was approved by the appropriate ethics committee, and written informed consent was obtained from all patients. In 37 patients with type 2 diabetes (31 men, six women; mean age, 56 years), 3.0-T single-voxel point-resolved (1)H MR spectroscopy of the liver (Couinaud segment VII) was performed to calculate the liver fat fraction from the water (4.7 ppm) and methylene (1.3 ppm) peaks, corrected for T1 and T2 decay. Liver fat fraction was also computed from triple-echo (consecutive in-phase, opposed-phase, and in-phase echo times) breath-hold spoiled gradient-echo sequence (flip angle, 20 degrees), by estimating T2* and relative signal intensity loss between in- and opposed-phase values, corrected for T2* decay. Pearson correlation coefficient, Bland-Altman 95% limit of agreement, and Lin concordance coefficient were calculated. RESULTS: Mean fat fractions calculated from the triple-echo sequence and (1)H MR spectroscopy were 10% (range, 0.7%-35.6%) and 9.7% (range, 0.2%-34.1%), respectively. Mean T2* time was 14.7 msec (range, 5.4-25.4 msec). Pearson correlation coefficient was 0.989 (P < .0001) and Lin concordance coefficient was 0.988 (P < .0001). With the Bland-Altman method, all data points were within the limits of agreement. CONCLUSION: A breath-hold triple-echo gradient-echo sequence with a low flip angle and correction for T2* decay is accurate for quantifying fat in segment VII of the liver. Given its excellent correlation and concordance with (1)H MR spectroscopy, this triple-echo sequence could replace (1)H MR spectroscopy in longitudinal studies.
Published: 2009

14. STD and TRNOESY NMR studies for the epitope mapping of the phosphorylation motif of the oncogenic protein beta-catenin recognized by a selective monoclonal antibody

Author: Simon Megy, Gildas Bertho, Richard Benarous, Françoise Baleux, Josyane Gharbi-Benarous, Jean-Pierre Girault, Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques (LCBPT - UMR 8601), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Chimie Organique, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Institut Cochin (UMR_S567 / UMR 8104), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques ( LCBPT - UMR 8601 ), Université Paris Descartes - Paris 5 ( UPD5 ) -Centre National de la Recherche Scientifique ( CNRS ), Chimie Organique ( UCO ), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique ( CNRS ), Institut Cochin ( UMR_S567 / UMR 8104 ), Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes - Paris 5 (UPD5)-Centre National de la Recherche Scientifique (CNRS), Chimie Organique (UCO), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5)
Subjects: Models, Molecular, MESH: Neoplasm Proteins, Magnetic Resonance Spectroscopy, Amino Acid Motifs, MESH: beta Catenin, Peptide, Nuclear Overhauser effect, 01 natural sciences, Biochemistry, Epitope, MESH: Antibodies, Monoclonal, MESH : Phosphorylation, Epitopes, MESH: Amino Acid Motifs, MESH: Protein Structure, Tertiary, Structural Biology, Neoplasms, MESH: Nuclear Magnetic Resonance, Biomolecular, TRNOESY, MESH: Neoplasms, Phosphorylation, beta Catenin, MESH : Ubiquitin, chemistry.chemical_classification, 0303 health sciences, biology, Chemistry, MESH : Peptides, MESH: Peptides, Antibodies, Monoclonal, Nuclear magnetic resonance spectroscopy, P-β-Catenin/antibody complex, Ubiquitin ligase, Neoplasm Proteins, Restrained molecular dynamics, MESH : Antibodies, Monoclonal, MESH : SKP Cullin F-Box Protein Ligases, Two-dimensional nuclear magnetic resonance spectroscopy, MESH : Protein Structure, Tertiary, Binding fragment, MESH: Models, Molecular, MESH: SKP Cullin F-Box Protein Ligases, MESH : Amino Acid Motifs, MESH: Ubiquitin, MESH: Epitopes, MESH : Models, Molecular, Biophysics, MESH : Epitopes, MESH : Nuclear Magnetic Resonance, Biomolecular, Bound structure, 010402 general chemistry, 03 medical and health sciences, MESH : Neoplasm Proteins, P-β-Catenin phosphorylated peptide, Genetics, Humans, Molecular Biology, Nuclear Magnetic Resonance, Biomolecular, Antibody, 030304 developmental biology, MESH : Protein Processing, Post-Translational, MESH: Epitope Mapping, SKP Cullin F-Box Protein Ligases, MESH: Humans, MESH: Phosphorylation, Ubiquitin, MESH: Magnetic Resonance Spectroscopy, β-Catenin oncogenic protein, MESH : Humans, Cell Biology, MESH : beta Catenin, MESH : Neoplasms, 0104 chemical sciences, Protein Structure, Tertiary, STD NMR, Epitope mapping, MESH : Epitope Mapping, MESH: Protein Processing, Post-Translational, biology.protein, MESH : Magnetic Resonance Spectroscopy, Peptides, Protein Processing, Post-Translational, Epitope Mapping, Conformational epitope
Abstract: International audience; The interaction of the P-beta-Cat(19-44) peptide, a 26 amino acid peptide (K(19)AAVSHWQQQSYLDpSGIHpSGATTTAP(44)) that mimics the phosphorylated beta-Catenin antigen, has been studied with its monoclonal antibody BC-22, by transferred nuclear Overhauser effect NMR spectroscopy (TRNOESY) and saturation transfer difference NMR (STD NMR) spectroscopy. This antibody is specific to diphosphorylated beta-Catenin and does not react with the non-phosphorylated protein. Phosphorylation of beta-Catenin at sites Ser33 and Ser37 on the DSGXXS motif is required for the interaction of beta-Catenin with the ubiquitin ligase SCF(beta-TrCP). beta-TrCP is involved in the ubiquitination and proteasome targeting of the oncogenic protein beta-Catenin, the accumulation of which has been implicated in various human cancers. The three-dimensional structure of the P-beta-Cat(19-44) in the bound conformation was determined by TRNOESY NMR experiments; the peptide adopts a compact structure in the presence of mAb with formation of turns around Trp25 and Gln26, with a tight bend created by the DpS(33)GIHpS(37) motif; the peptide residues (D32-pS37) forming this bend are recognized by the antibody as demonstrated by STD NMR experiments. STD NMR studies provide evidence for the existence of a conformational epitope containing tandem repeats of phosphoserine motifs. The peptide's epitope is predominantly located in the large bend and in the N-terminal segment, implicating bidentate association. These findings are in excellent agreement with a recently published NMR structure required for the interaction of beta-Catenin with the SCF(beta-TrCP) protein.
Published: 2006

15. Structural changes of Escherichia coli ferric uptake regulator during metal-dependent dimerization and activation explored by NMR and X-ray crystallography

Author: Ludovic Pecqueur, Lilian Jacquamet, Bernhard Brutscher, Benoît D'Autréaux, Isabelle Michaud-Soret, Beate Bersch, Yvain Nicolet, Jérôme Dupuy, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Institut de biologie structurale (IBS - UMR 5075), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Laboratoire de Chimie et Biologie des Métaux ( LCBM - UMR 5249 ), Université Joseph Fourier - Grenoble 1 ( UJF ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Grenoble Alpes ( UGA ), and Institut de biologie structurale ( IBS - UMR 5075 )
Subjects: Models, Molecular, Protein Denaturation, Protein Folding, MESH : Escherichia coli, Magnetic Resonance Spectroscopy, MESH : Molecular Sequence Data, MESH: Protein Structure, Quaternary, MESH: Sequence Homology, Amino Acid, MESH : DNA, Dimer, MESH : Antigens, MESH : Trinitrobenzenes, MESH: Protein Structure, Secondary, Nuclear Overhauser effect, MESH: Amino Acid Sequence, Crystallography, X-Ray, Biochemistry, MESH: Zinc, Protein Structure, Secondary, chemistry.chemical_compound, [ SDV.BBM.BC ] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Protein structure, MESH : Bacterial Proteins, MESH: Animals, Protein Dimerization, MESH: Bacterial Proteins, 0303 health sciences, MESH: Escherichia coli, MESH : Amino Acid Sequence, MESH: DNA, MESH : Sequence Homology, Amino Acid, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Zinc, Monomer, MESH : Dimerization, MESH: Repressor Proteins, MESH : Protein Denaturation, Protein folding, MESH: Antigens, MESH : Repressor Proteins, Dimerization, MESH: Models, Molecular, MESH : Protein Folding, MESH : Bile, MESH : Models, Molecular, Protein subunit, MESH: Protein Folding, MESH: Biological Transport, MESH: Intestinal Absorption, Molecular Sequence Data, MESH: Mice, Inbred BALB C, MESH: Serum Albumin, MESH : Immunoglobulin A, MESH : Serum Albumin, 03 medical and health sciences, Bacterial Proteins, MESH : Protein Structure, Quaternary, MESH : Mice, Escherichia coli, Amino Acid Sequence, MESH: Immunoglobulin A, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Protein Structure, Quaternary, Molecular Biology, MESH: Mice, MESH : Mice, Inbred BALB C, MESH: Bile, 030304 developmental biology, MESH: Molecular Sequence Data, MESH: Trinitrobenzenes, MESH: Humans, Sequence Homology, Amino Acid, 030306 microbiology, MESH: Magnetic Resonance Spectroscopy, MESH : Humans, MESH : Intestinal Absorption, DNA, MESH : Zinc, Cell Biology, MESH: Crystallography, X-Ray, Repressor Proteins, MESH : Biological Transport, Crystallography, chemistry, MESH: Dimerization, MESH : Magnetic Resonance Spectroscopy, Protein quaternary structure, MESH: Protein Denaturation, MESH : Animals, MESH : Protein Structure, Secondary, MESH : Crystallography, X-Ray
Abstract: International audience; Ferric uptake regulator (Fur) is a global bacterial regulator that uses iron as a cofactor to bind to specific DNA sequences. Escherichia coli Fur is usually isolated as a homodimer with two metal sites per subunit. Metal binding to the iron site induces protein activation; however the exact role of the structural zinc site is still unknown. Structural studies of three different forms of the Escherichia coli Fur protein (nonactivated dimer, mono-mer, and truncated Fur-(1-82)) were performed. Dimerization of the oxidized monomer was followed by NMR in the presence of a reductant (dithiothreitol) and Zn(II). Reduction of the disul-fide bridges causes only local structure variations, whereas zinc addition to reduced Fur induces protein dimerization. This demonstrates for the first time the essential role of zinc in the stabilization of the quaternary structure. The secondary structures of the mono-and dimeric forms are almost conserved in the N-terminal DNA-binding domain, except for the first helix, which is not present in the nonactivated dimer. In contrast, the C-terminal dimerization domain is well structured in the dimer but appears flexible in the monomer. This is also confirmed by heteronuclear Overhauser effect data. The crystal structure at 1.8 Å resolution of a truncated protein (Fur-(1-82)) is described and found to be identical to the N-terminal domain in the mono-meric and in the metal-activated state. Altogether, these data allow us to propose an activation mechanism for E. coli Fur involving the folding/unfolding of the N-terminal helix.
Published: 2006

16. Self-organisation of an oligodeoxynucleotide containing the G- and C-rich stretches of the direct repeats of the human mitochondrial DNA

Author: Frédéric Dardel, Sylvie Nonin-Lecomte, Patrick Lestienne, Laboratoire de cristallographie et RMN biologiques (LCRB - UMR 8015), Université Paris Descartes - Paris 5 (UPD5) - Centre National de la Recherche Scientifique (CNRS), Laboratoire de pharmacologie des agents anticancéreux (LPAA), Université Bordeaux Segalen - Bordeaux 2 - Institut Bergonié - CRLCC Bordeaux - Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5), Laboratoire de Cristallographie et Résonance Magnétique Nucléaire Biologiques, affiliation inconnue, Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Université Bordeaux Segalen - Bordeaux 2-Institut Bergonié [Bordeaux], UNICANCER-UNICANCER-Centre National de la Recherche Scientifique (CNRS), and Université Bordeaux Segalen - Bordeaux 2-Institut Bergonié - CRLCC Bordeaux-Centre National de la Recherche Scientifique (CNRS)
Subjects: Models, Molecular, Magnetic Resonance Spectroscopy, MESH : Molecular Sequence Data, MESH : Nucleic Acid Conformation, MESH: Base Sequence, MESH : Oligodeoxyribonucleotides, 01 natural sciences, Biochemistry, Genome, Heavy strand, MESH : DNA, Mitochondrial, Direct repeat, MESH : Temperature, ComputingMilieux_MISCELLANEOUS, Genetics, 0303 health sciences, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Temperature, General Medicine, MESH: Temperature, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], MESH: Nucleic Acid Conformation, Oligodeoxyribonucleotides, Two-dimensional nuclear magnetic resonance spectroscopy, MESH: Models, Molecular, Triple helix, Stereochemistry, Base pair, MESH : Models, Molecular, Molecular Sequence Data, Context (language use), Biology, 010402 general chemistry, DNA, Mitochondrial, MESH : GC Rich Sequence, 03 medical and health sciences, Tetramer, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Humans, MESH: GC Rich Sequence, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Repetitive Sequences, Nucleic Acid, 030304 developmental biology, MESH: Humans, MESH: Molecular Sequence Data, MESH: Repetitive Sequences, Nucleic Acid, Base Sequence, MESH: Magnetic Resonance Spectroscopy, MESH : Humans, MESH: DNA, Mitochondrial, GC Rich Sequence, 0104 chemical sciences, MESH : Repetitive Sequences, Nucleic Acid, MESH: Oligodeoxyribonucleotides, Nucleic Acid Conformation, MESH : Magnetic Resonance Spectroscopy, MESH : Base Sequence
Abstract: Stretches of cytosines and guanosines have been shown in vitro to adopt non-canonical structures known as i-motifs and G-quartets, respectively. When combined, such sequences are expected to either retain their structure or form duplexes or triple helices. All these structures may occur in vivo whenever the sequence criteria are met. Such stretches are present in the circular genome of human mitochondria, as two 10 nucleotide-long perfect tandem direct repeats (DR1 and DR2). The DR1 and DR2 repeats are G-rich on the heavy strand and C-rich on the light strand. Previous results suggested that during replication, transient formation of a parallel GGC triple helix between the neosynthesised G-rich DR1 and the double-stranded homologous DR2 could be involved in a rearrangement process leading to genome instability. In order to get structural insights into the interaction between the two repeats, we have studied by nuclear magnetic resonance (NMR) the assembly properties of a 24-mer oligodeoxyribonucleotide in which the C- and G-rich segments of the DRs are covalently tethered by a TTTT linker. We show here that this 24-mer self-associates into a triplex-containing symmetrical tetramer. The core of the structure is composed of anti-parallel Watson–Crick (WC) base pairs. Two additional strands are hydrogen-bonded to the Hoogsteen side of the Gs, thus forming CGC + triple helices, with G-rich ends folding into G-quartets. These results suggest that such structures could occur when the two DRs are put to close proximity in a biological context. © 2005 Elsevier SAS. All rights reserved.
Published: 2005

17. Double molecular mimicry in Escherichia coli: binding of ribosomal protein L20 to its two sites in mRNA is similar to its binding to 23S rRNA

Author: Mathias Springer, Frédéric Dardel, Claude Chiaruttini, Maude Guillier, Catherine A. Royer, Frédéric Allemand, Régulation de l'expression génétique chez les microorganismes (REGCM), Centre National de la Recherche Scientifique (CNRS), Laboratoire de cristallographie et RMN biologiques (LCRB - UMR 8015), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Centre de Biochimie Structurale [Montpellier] (CBS), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes - Paris 5 (UPD5) - Centre National de la Recherche Scientifique (CNRS), and Institut National de la Santé et de la Recherche Médicale (INSERM) - Université de Montpellier (UM) - Centre National de la Recherche Scientifique (CNRS)
Subjects: Models, Molecular, MESH : Escherichia coli, MESH : Molecular Sequence Data, MESH : RNA, Messenger, Magnetic Resonance Spectroscopy, MESH : Nucleic Acid Conformation, MESH: Escherichia coli Proteins, MESH : Ribosomal Proteins, MESH: Base Sequence, Ribosome, MESH : RNA, Ribosomal, 23S, 50S, 0303 health sciences, MESH: Escherichia coli, MESH : Escherichia coli Proteins, Escherichia coli Proteins, 030302 biochemistry & molecular biology, MESH: RNA, Ribosomal, 23S, MESH: Ribosomal Proteins, RNA, Ribosomal, 23S, MESH: Nucleic Acid Conformation, MESH: Molecular Mimicry, MESH: Models, Molecular, Ribosomal Proteins, MESH : Models, Molecular, Molecular Sequence Data, Biology, Microbiology, 03 medical and health sciences, Ribosomal protein, 23S ribosomal RNA, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Escherichia coli, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, RNA, Messenger, Binding site, Molecular Biology, 030304 developmental biology, MESH: RNA, Messenger, Binding Sites, MESH: Molecular Sequence Data, Base Sequence, MESH: Magnetic Resonance Spectroscopy, Molecular Mimicry, Ribosomal RNA, Molecular biology, MESH : Molecular Mimicry, Ribosomal binding site, A-site, MESH: Binding Sites, MESH : Magnetic Resonance Spectroscopy, Nucleic Acid Conformation, MESH : Base Sequence, MESH : Binding Sites
Abstract: Escherichia coli ribosomal L20 is one of five proteins essential for the first reconstitution step of the 50S ribosomal subunit in vitro. It is purely an assembly protein, because it can be withdrawn from the mature subunit without effect on ribosome activity. In addition, L20 represses the translation of its own gene by binding to two sites in its mRNA. The first site is a pseudoknot formed by a base-pairing interaction between nucleotide sequences separated by more than 280 nucleotides, whereas the second site is an irregular helix formed by base-pairing between neighbouring nucleotide sequences. Despite these differences, the mRNA folds in such a way that both L20 binding sites share secondary structure similarity with the L20 binding site located at the junction between helices H40 and H41 in 23S rRNA. Using a set of genetic, biochemical, biophysical, and structural experiments, we show here that all three sites are recognized similarly by L20.
Published: 2005

18. Cytochrome c and SDS: a molten globule protein with altered axial ligation

Author: Arnaud Bondon, Paul R. Vasos, Paola Turano, Gérard Simonneaux, Ivano Bertini, Soizic Chevance, Dept Chem Ugo Schiff, Università degli Studi di Firenze = University of Florence [Firenze] (UNIFI), Magnet Resonance Ctr CERM, Magnet Resonance Center (CERM), Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques (LCBPT - UMR 8601), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut des Sciences Chimiques de Rennes (ISCR), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Firenze = University of Florence (UniFI), Université de Rennes (UR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), University of Florence (UNIFI), Université Paris Descartes - Paris 5 (UPD5)-Centre National de la Recherche Scientifique (CNRS), Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Chimie de Rennes-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES), University of Florence, Magnet Resonance Center ( CERM ), Laboratoire de Chimie et de Biochimie Pharmacologiques et Toxicologiques ( LCBPT - UMR 8601 ), Université Paris Descartes - Paris 5 ( UPD5 ) -Centre National de la Recherche Scientifique ( CNRS ), Institut des Sciences Chimiques de Rennes ( ISCR ), Université de Rennes 1 ( UR1 ), and Université de Rennes ( UNIV-RENNES ) -Université de Rennes ( UNIV-RENNES ) -Ecole Nationale Supérieure de Chimie de Rennes-Institut National des Sciences Appliquées ( INSA ) -Centre National de la Recherche Scientifique ( CNRS )
Subjects: Magnetic Resonance Spectroscopy, Time Factors, Cytochrome, MESH : Cytochromes c, Protein Conformation, MESH : Saccharomyces cerevisiae, MESH : Rotation, 01 natural sciences, Protein structure, MESH: Protein Conformation, MESH: Rotation, MESH: Saccharomyces cerevisiae Proteins, Structural Biology, MESH : Myocardium, MESH: Animals, MESH : Protein Conformation, MESH : Viscosity, 0303 health sciences, biology, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Chemistry, Viscosity, Cytochrome c, Cytochromes c, Sodium Dodecyl Sulfate, Nuclear magnetic resonance spectroscopy, MESH: Cytochromes c, Ligand (biochemistry), MESH: Saccharomyces cerevisiae, Molten globule, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Protons, MESH : Time Factors, MESH: Sodium Dodecyl Sulfate, Saccharomyces cerevisiae Proteins, MESH: Myocardium, Rotation, MESH: Viscosity, Saccharomyces cerevisiae, 010402 general chemistry, MESH : Saccharomyces cerevisiae Proteins, 03 medical and health sciences, MESH : Protons, Animals, Horses, MESH: Horses, Molecular Biology, Rotational correlation time, MESH : Sodium Dodecyl Sulfate, 030304 developmental biology, MESH: Magnetic Resonance Spectroscopy, Myocardium, MESH: Time Factors, Random coil, 0104 chemical sciences, Crystallography, biology.protein, MESH : Horses, MESH : Magnetic Resonance Spectroscopy, MESH : Animals, MESH: Protons, [ SDV.BBM.BS ] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]
Abstract: International audience; Saccharomices cerevisiae (yeast iso-1) cytochrome c has been investigated in the presence of 100 mM SDS in order to simulate the interaction of cytochrome c with membrane. Under these circumstances, a high spin species with detached methionine axial ligand is observed through NMR, in analogy to findings on the horse heart protein. However, at variance with the latter system, for the yeast protein also a low spin species is detected, which appears to be present with a concentration of about 40% with respect to that of the high spin species. The R(1), R(2), [1H]-15N NOE of backbone amides which are not affected by paramagnetism are homogeneous and allow a simultaneous analysis of the data for the two species. The result is that the rotational correlation time is larger than in water and larger than expected on the basis of viscosity of the SDS-containing solution. This finding suggests interactions of cytochrome c with SDS. Furthermore, it appears that there is subnanosecond backbone mobility, which also accounts for the decreased intensity of NOE cross-peaks and may be associated with equilibria between helical and random coil structure. The dynamic behavior appears to be a common feature of the high spin and low spin species and is consistent with the presence of a molten globule state. The molten globule nature of the protein could account for the presence of the different axial coordination of the heme iron. Such findings are meaningful with respect to the physiology of cytochrome c as electron transfer protein and as promoter of apoptosis.
Published: 2004

19. The tRNA-like domains of E coli and A.aeolicus transfer-messenger RNA: structural and functional studies

Author: Valérie Bordeau, Frédéric Dardel, Sophie Corvaisier, Sylvie Nonin-Lecomte, Brice Felden, Cyril Gaudin, Carine Tisné, Laboratoire de cristallographie et RMN biologiques (LCRB - UMR 8015), Université Paris Descartes - Paris 5 (UPD5)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Etude du 'Rnome' bacterien. Identification et Caracterisation d'Acides Ribonucleiques Impliques Dans la Survie et la Virulence', Université de Rennes (UR)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de cristallographie et RMN biologiques ( LCRB - UMR 8015 ), Université Paris Descartes - Paris 5 ( UPD5 ) -Centre National de la Recherche Scientifique ( CNRS ), Université de Rennes 1 ( UR1 ), Université de Rennes ( UNIV-RENNES ) -Université de Rennes ( UNIV-RENNES ) -IFR140-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre National de la Recherche Scientifique (CNRS)-Université Paris Descartes - Paris 5 (UPD5), and Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-IFR140-Institut National de la Santé et de la Recherche Médicale (INSERM)
Subjects: MESH : Escherichia coli, MESH: Hydrogen-Ion Concentration, Magnetic Resonance Spectroscopy, MESH : RNA, Messenger, MESH : Molecular Sequence Data, Protein Conformation, MESH: Protein Structure, Secondary, MESH: Base Sequence, Crystallography, X-Ray, Ribosome, Protein Structure, Secondary, MESH: Recombinant Proteins, chemistry.chemical_compound, MESH: Protein Structure, Tertiary, Protein structure, MESH: Protein Conformation, MESH: Structure-Activity Relationship, RNA, Transfer, Structural Biology, MESH : Structure-Activity Relationship, MESH : RNA, RNA Processing, Post-Transcriptional, MESH : Protein Conformation, MESH : RNA Processing, Post-Transcriptional, 0303 health sciences, Alanine, biology, MESH : Peptides, MESH: Escherichia coli, MESH: Peptides, 030302 biochemistry & molecular biology, MESH : Protein Binding, Hydrogen-Ion Concentration, Recombinant Proteins, Biochemistry, Transfer RNA, MESH : Protein Structure, Tertiary, Protein Binding, MESH: RNA Processing, Post-Transcriptional, MESH : Recombinant Proteins, MESH: Alanine, Molecular Sequence Data, MESH : RNA, Transfer, Pseudouridine, 03 medical and health sciences, Structure-Activity Relationship, MESH : Hydrogen-Ion Concentration, MESH: RNA, Escherichia coli, MESH: Protein Binding, MESH : Bacteria, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, RNA, Messenger, Molecular Biology, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, 030304 developmental biology, MESH: RNA, Messenger, Aquifex aeolicus, MESH: Molecular Sequence Data, Bacteria, Base Sequence, MESH: Magnetic Resonance Spectroscopy, RNA, biology.organism_classification, MESH: RNA, Transfer, MESH: Crystallography, X-Ray, Protein Structure, Tertiary, MESH: Bacteria, chemistry, MESH : Magnetic Resonance Spectroscopy, MESH : Base Sequence, MESH : Protein Structure, Secondary, MESH : Alanine, MESH : Crystallography, X-Ray, Peptides, Trans-translation, Transfer-messenger RNA
Abstract: International audience; Transfer-messenger RNA (tmRNA, 10Sa RNA or ssrA) acts to rescue stalled bacterial ribosomes while encoding a peptide tag added trans-translationally to the nascent peptide, targeting it for proteolysis. The understanding at molecular level of this ubiquitous quality control system in eubacteria requires structural information. Here, we describe the purification and structural analysis of a functional fragment of both Aquifex aeolicus and Escherichia coli tmRNA, recapitulating their tRNA-like domain, which were expressed in vivo from synthetic genes. Both recombinant RNA are correctly processed at both 5' and 3' ends and are produced in quantities suitable for structural analysis by NMR and/or X-ray crystallography. The sequence and solution structure of the tRNA-like domains were analysed by various methods including structural mapping with chemical and enzymatic probes and 2D NMR spectroscopy. The minimalist RNAs contain two post-transcriptional base modifications, 5-methyluridine and pseudouridine, as the full-length tmRNA. Both RNAs fold into three stems, a D-analogue, a T-loop and a GAAA tetra-loop. 2D NMR analysis of the imino proton resonances of both RNAs allowed the assignment of the three stems and of a number of tertiary interactions. It shows the existence of interactions between the TPsiC-loop and the D-analogue, exhibiting a number of similarities and also differences with the canonical tRNA fold, indicating that RNA tertiary interactions can be modulated according to the sequence and secondary structure contexts. Furthermore, the E.coli minimalist RNA is aminoacylatable with alanine with a catalytic efficiency an order of magnitude higher than that for full-length tmRNA.
Published: 2003

20. The H-NS dimerization domain defines a new fold contributing to DNA recognition

Author: Vanessa Bloch, Marie Thérèse Augé, Bruno Robert, Stefan T. Arold, Yinshan Yang, Sylvie Rimsky, Emmanuel Margeat, Alain Chavanieu, Michel Kochoyan, Centre de Biochimie Structurale [Montpellier] ( CBS ), Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire Bioénergétique, Métalloprotéines et Stress ( LBMS ), Département Biochimie, Biophysique et Biologie Structurale ( B3S ), Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de Biologie et de Pharmacologie Appliquée ( LBPA ), École normale supérieure - Cachan ( ENS Cachan ) -Centre National de la Recherche Scientifique ( CNRS ), Centre de Biochimie Structurale [Montpellier] (CBS), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire Bioénergétique Membranaire et Stress (LBMS), Département Biochimie, Biophysique et Biologie Structurale (B3S), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biologie et de Pharmacologie Appliquée (LBPA), Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Cachan (ENS Cachan), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), and École normale supérieure - Cachan (ENS Cachan)-Centre National de la Recherche Scientifique (CNRS)
Subjects: Models, Molecular, Protein Folding, Magnetic Resonance Spectroscopy, MESH : Molecular Sequence Data, Protein Conformation, MESH : DNA, MESH: Amino Acid Sequence, MESH: Protein Structure, Tertiary, chemistry.chemical_compound, MESH: Protein Conformation, Structural Biology, MESH : Bacterial Proteins, MESH: Peptide Fragments, MESH: Bacterial Proteins, Conserved Sequence, MESH : Protein Conformation, 0303 health sciences, MESH: Conserved Sequence, MESH : Amino Acid Sequence, MESH: DNA, DNA-Binding Proteins, Biochemistry, MESH : Dimerization, MESH : DNA-Binding Proteins, MESH : Mutation, Dimerization, MESH : Protein Structure, Tertiary, MESH: Models, Molecular, Binding domain, MESH : Protein Folding, MESH: Mutation, HMG-box, MESH : Models, Molecular, MESH: Protein Folding, Molecular Sequence Data, Fluorescence Polarization, Computational biology, Biology, DNA-binding protein, 03 medical and health sciences, Bacterial Proteins, MESH : Conserved Sequence, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, B3 domain, Molecular Biology, Gene, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, 030304 developmental biology, MESH: Fluorescence Polarization, MESH: Molecular Sequence Data, MESH: Magnetic Resonance Spectroscopy, 030306 microbiology, Circular bacterial chromosome, MESH : Peptide Fragments, DNA, Peptide Fragments, Protein Structure, Tertiary, MESH: Dimerization, Heteronuclear molecule, chemistry, Mutation, MESH : Fluorescence Polarization, MESH : Magnetic Resonance Spectroscopy, MESH: DNA-Binding Proteins
Abstract: International audience; H-NS, a protein found in Gram-negative bacteria, is involved in structuring the bacterial chromosome and acts as a global regulator for the expression of a wide variety of genes. These functions are correlated with both its DNA-binding and oligomerization properties. We have identified the minimal dimerization domain of H-NS, a 46 amino acid-long N-terminal fragment, and determined its structure using heteronuclear NMR spectroscopy. The highly intertwined structure of the dimer, reminiscent of a handshake, defines a new structural fold, which may offer a possibility for discriminating prokaryotic from eukaryotic proteins in drug design. Using mutational analysis, we also show that this N-terminal domain actively contributes to DNA binding, conversely to the current paradigm. Together, our data allows us to propose a model for the action of full length H-NS.
Published: 2003

21. Spectroscopic data following stroke reveal tissue abnormality beyond the region of T2-weighted hyperintensity

Author: François Brunotte, Alain Beley, Christine Marie, Maurice Giroud, Céline Demougeot, Paul Walker, Olivier Rouaud, Fonctions et dysfonctions épithéliales - UFC (EA 4267) (FDE), Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Service de neurologie (hôpital général, CHU Dijon), Hôpital général (CHU Dijon), Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon)-Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon), Service de RMN Spectroscopie, Médecine Nucléaire (CHU de Dijon), Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon), Fonctions et dysfonctions épithéliales - UFC (EA 4267) ( FDE ), Université de Franche-Comté ( UFC ), Neuroépidémiologie, Université Pierre et Marie Curie - Paris 6 ( UPMC ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), Centre d'Imagerie par Résonance Magnétique, Centre Hospitalier Universitaire, Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand ( CHU Dijon ), Laboratoire Electronique, Informatique et Image ( Le2i ), Université de Bourgogne ( UB ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique ( CNRS ), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire Electronique, Informatique et Image [UMR6306] (Le2i), Université de Bourgogne (UB)-Centre National de la Recherche Scientifique (CNRS)-École Nationale Supérieure d'Arts et Métiers (ENSAM), Arts et Métiers Sciences et Technologies, HESAM Université (HESAM)-HESAM Université (HESAM)-Arts et Métiers Sciences et Technologies, HESAM Université (HESAM)-HESAM Université (HESAM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, and Winninger, Anne-Marie
Subjects: Male, Pathology, Magnetic Resonance Spectroscopy, Time Factors, MESH : Stroke, MESH : Aspartic Acid, Severity of Illness Index, MESH: Aspartic Acid, MESH : Choline, Choline, 030218 nuclear medicine & medical imaging, MESH: Magnetic Resonance Imaging, 0302 clinical medicine, MESH : Female, Stroke, MESH: Middle Aged, medicine.diagnostic_test, MESH: Creatine, MESH: Choline, MESH: Infarction, Middle Cerebral Artery, Infarction, Middle Cerebral Artery, Middle Aged, [SDV.SP]Life Sciences [q-bio]/Pharmaceutical sciences, MESH : Creatine, Magnetic Resonance Imaging, MESH: Predictive Value of Tests, [SDV.SP] Life Sciences [q-bio]/Pharmaceutical sciences, Neurology, Female, MESH : Severity of Illness Index, Abnormality, T2 weighted, MESH : Time Factors, medicine.medical_specialty, MESH : Male, Ischemia, MESH: Stroke, Central nervous system disease, 03 medical and health sciences, Predictive Value of Tests, MESH : Magnetic Resonance Imaging, MESH: Severity of Illness Index, MESH : Infarction, Middle Cerebral Artery, medicine, Humans, MESH : Middle Aged, Lactic Acid, MESH : Predictive Value of Tests, Aspartic Acid, MESH: Humans, Vascular disease, business.industry, MESH: Magnetic Resonance Spectroscopy, MESH : Humans, MESH: Time Factors, Magnetic resonance imaging, Creatine, medicine.disease, Hyperintensity, MESH: Male, [ SDV.SP ] Life Sciences [q-bio]/Pharmaceutical sciences, MESH : Lactic Acid, MESH : Magnetic Resonance Spectroscopy, MESH: Lactic Acid, Neurology (clinical), Nuclear medicine, business, MESH: Female, 030217 neurology & neurosurgery
Abstract: International audience; Cerebral tissue with T2 magnetic resonance imaging (MRI) abnormalities following stroke is generally considered infarcted, while surrounding regions with normal MRI appearance are believed to be healthy. To assess whether these surrounding regions consist of normal tissue, we explored the distribution of N-acetylaspartate (NAA) and lactate within and around the hyperintense area on T2-weighted MRI using proton MR spectroscopy. The study was carried out in 25 patients with middle cerebral artery occlusion imaged between 1 and 42 days after stroke onset. NAA/choline (Cho) ratios were significantly reduced in both areas of T2 hyperintensity and in surrounding tissue. The reduction was greater in the region of T2 hyperintensity than in the surrounding region (-50% vs. -28%, respectively) and was unrelated to the delay after the ictus. Lactate/Cho ratios increased massively within the abnormal T2 area, but did not differ from control values beyond the margin of hyperintensity. Overall data indicate that T2 visible lesions on MRI do not infer the entire injured tissue.
Published: 2002

22. Anomalous transverse relaxation in 1H spectroscopy in human brain at 4 Tesla

Author: Robert C. Risinger, Denis Le Bihan, S. Posse, Robert S. Balaban, Charles A. Cuenod, Department of Health and Human Services, National Institutes of Health [Bethesda] (NIH), Méthodes d'imagerie des échanges transcapillaires (LRI), IFR94-Université Paris Descartes - Paris 5 (UPD5), Laboratoire de Recherche en Imagerie LRI-EA4062, Université Paris Descartes - Paris 5 (UPD5), Service NEUROSPIN (NEUROSPIN), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Univ Fed Rio Grande do Norte, Dept Chem (LAPET), Univ Fed Rio Grande do Norte, Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), National Institutes of Health ( NIH ), Méthodes d'imagerie des échanges transcapillaires ( LRI ), IFR94-Université Paris Descartes - Paris 5 ( UPD5 ), Université Paris Descartes - Paris 5 ( UPD5 ), National Institutes of Health [Bethesda] ( NIH ), Service NEUROSPIN ( NEUROSPIN ), Direction de Recherche Fondamentale (CEA) ( DRF (CEA) ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay, Univ Fed Rio Grande do Norte, Dept Chem ( LAPET ), and Le Bihan, Denis
Subjects: Intracellular Fluid, MESH : Motion, Magnetic Resonance Spectroscopy, Proton, Phosphocreatine, [SDV.IB.IMA]Life Sciences [q-bio]/Bioengineering/Imaging, Analytical chemistry, MESH : Aspartic Acid, MESH: Signal Processing, Computer-Assisted, MESH: Aspartic Acid, MESH : Artifacts, MESH : Choline, 030218 nuclear medicine & medical imaging, Choline, Diffusion, Paramagnetism, chemistry.chemical_compound, 0302 clinical medicine, Nuclear magnetic resonance, [ SDV.IB.IMA ] Life Sciences [q-bio]/Bioengineering/Imaging, Fourier Analysis, MESH: Creatine, MESH: Intracellular Fluid, MESH : Hydrogen, Relaxation (NMR), MESH: Hydrogen, MESH: Choline, Brain, Pulse sequence, Signal Processing, Computer-Assisted, MESH: Diffusion, Nuclear magnetic resonance spectroscopy, Human brain, MESH : Creatine, medicine.anatomical_structure, MESH: Artifacts, MESH : Electron Spin Resonance Spectroscopy, Occipital Lobe, MESH: Image Enhancement, Artifacts, MESH: Occipital Lobe, MESH: Motion, MESH: Phosphocreatine, 03 medical and health sciences, Motion, MESH: Brain, MESH: Body Water, Body Water, medicine, Humans, Radiology, Nuclear Medicine and imaging, MESH : Phosphocreatine, Spectroscopy, MESH : Diffusion, Aspartic Acid, MESH : Signal Processing, Computer-Assisted, MESH : Body Water, MESH : Occipital Lobe, MESH: Humans, MESH: Magnetic Resonance Spectroscopy, MESH : Humans, Electron Spin Resonance Spectroscopy, Creatine, Image Enhancement, nervous system diseases, MESH : Fourier Analysis, [SDV.IB.IMA] Life Sciences [q-bio]/Bioengineering/Imaging, chemistry, MESH : Brain, nervous system, MESH : Image Enhancement, MESH : Magnetic Resonance Spectroscopy, MESH: Electron Spin Resonance Spectroscopy, 030217 neurology & neurosurgery, MESH: Fourier Analysis, Hydrogen, MESH : Intracellular Fluid
Abstract: International audience; Longitudinal (T1) and apparent transverse relaxation times (T2) of choline-containing compounds (Cho), creatine/phosphocreatine (Cr/PCr), and N-acetyl aspartate (NAA) were measured in vivo in human brain at 4 Tesla. Measurements were performed using a water suppressed stimulated echo pulse sequence with complete outside volume presaturation to improve volume localization at short echo times. T1-values of Cho (1.2 +/- 0.1 s), Cr (1.6 +/- 0.3 s), and NAA (1.6 +/- 0.2 s) at 4 Tesla in occipital brain were only slightly larger than those reported in the literature at 1.5 Tesla. Thus, TR will not adversely affect the expected enhancement of signal-to-noise at 4 Tesla. Surprisingly, apparent T2-values of Cho (142 +/- 34 ms), Cr (140 +/- 13 ms), and NAA (185 +/- 24 ms) at 4 Tesla were significantly smaller than those at 1.5 Tesla and further decreased when increasing the mixing interval TM. Potential contributing factors, such as diffusion in local susceptibility related gradients, dipolar relaxation due to intracellular paramagnetic substances and motion effects are discussed. The results suggest that short echo time spectroscopy is advantageous to maintain signal to noise at 4 Tesla.
Published: 1995

23. Galactosaminogalactan, a New Immunosuppressive Polysaccharide of Aspergillus fumigatus

Author: Silvia Moretti, Markus Aebi, Jean-Paul Latgé, Muriel Delepierre, Flavio Schwarz, Aurélie Delangle, Sandra J. van Vliet, Catherine Simenel, Yvette van Kooyk, Bernadette Coddeville, Coline Trichot, Luigina Romani, Silvia Bozza, Carole Elbim, Thierry Fontaine, Aspergillus, Institut Pasteur [Paris], Résonance Magnétique Nucléaire des Biomolécules, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), VU University Medical Center [Amsterdam], Università degli Studi di Perugia (UNIPG), Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich), Immunité et Infection, Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR113-Sorbonne Université (SU), This work was partly supported by a grant from Agence Nationale de la Recherche (ANR-06-EMPB-011-01) and by European grants Allfun, Fungwall, ANRpathogenomics. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript., ANR-06-EMPB-0011,GALNACGAL,Développement d'un nouveau test de diagnostic de l'aspergillose(2006), European Project: 260338,EC:FP7:HEALTH,FP7-HEALTH-2010-single-stage,ALLFUN(2010), European Project: 511952,FUNGWALL(2005), European Project: 27618,PATHOGENOMICS, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique ( CNRS ), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 ( UGSF ), Institut National de la Recherche Agronomique ( INRA ) -Université de Lille-Centre National de la Recherche Scientifique ( CNRS ), University of Amsterdam [Amsterdam] ( UvA ), Università degli Studi di Perugia ( UNIPG ), Eidgenössische Technische Hochschule [Zürich] ( ETH Zürich ), Université Pierre et Marie Curie - Paris 6 ( UPMC ) -IFR113-Institut National de la Santé et de la Recherche Médicale ( INSERM ), This work was partly supported by a grant from Agence Nationale de la Recherche (ANR-06-EMPB-011-01) and by European grants Allfun, Fungwall, ANRpathogenomics., ANR-06-EMPB-0011,GALNACGAL,Développement d'un nouveau test de diagnostic de l'aspergillose ( 2006 ), Institut Pasteur [Paris] (IP), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Perugia = University of Perugia (UNIPG), IFR113-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology in Zürich [Zürich] (ETH Zürich), CCA - Immuno-pathogenesis, Molecular cell biology and Immunology, Andriakoto, Nirina, Emergence et maturation de projets de biotechnologie à fort potentiel de valorisation (EMPB) - Développement d'un nouveau test de diagnostic de l'aspergillose - - GALNACGAL2006 - ANR-06-EMPB-0011 - EMPB - VALID, Fungi in the setting of inflammation, allergy and autoimmune diseases:Translating basic science into clinical practices - ALLFUN - - EC:FP7:HEALTH2010-12-01 - 2014-05-31 - 260338 - VALID, The Fungal cell wall as a target for antifungal therapies - FUNGWALL - 2005-01-01 - 2007-12-31 - 511952 - OLD, and Trans-European cooperation and coordination of genome sequencing and functional genomics of human-pathogenic microorganisms - PATHOGENOMICS - 27618 - OLD
Subjects: Magnetic Resonance Spectroscopy, MESH : Polysaccharides, Galactosaminogalactan, Apoptosis, MESH: Neutrophils, Biochemistry, Epitope, Aspergillus fumigatus, MESH : Neutrophils, Epitopes, Mice, MESH : Antigens, Fungal, Cell Wall, MESH : Antibodies, Fungal, MESH : Aspergillosis, MESH: Animals, Fungal Biochemistry, MESH : Immunosuppressive Agents, Immune Response, lcsh:QH301-705.5, [ SDV.MP.MYC ] Life Sciences [q-bio]/Microbiology and Parasitology/Mycology, [SDV.MP.MYC]Life Sciences [q-bio]/Microbiology and Parasitology/Mycology, MESH : Macrophages, chemistry.chemical_classification, 0303 health sciences, education.field_of_study, MESH : Cross Reactions, 3. Good health, Neutrophil Infiltration, Carbohydrate conformation, MESH: Immunosuppressive Agents, Antigens, Fungal, MESH: Epitopes, Immunology, Cross Reactions, MESH : Epitopes, Microbiology, 03 medical and health sciences, MESH: Cell Wall, Genetics, Aspergillosis, Humans, education, Biology, Molecular Biology, Antibodies, Fungal, MESH: Antigens, Fungal, Aspergillus, MESH: Humans, [ SDV ] Life Sciences [q-bio], 030306 microbiology, MESH: Magnetic Resonance Spectroscopy, Macrophages, MESH : Humans, MESH: Host-Pathogen Interactions, [SDV.MP.MYC] Life Sciences [q-bio]/Microbiology and Parasitology/Mycology, Mice, Inbred C57BL, MESH : Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, chemistry, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, MESH : Magnetic Resonance Spectroscopy, Parasitology, lcsh:RC581-607, MESH: Female, MESH : Apoptosis, Neutrophils, Glycobiology, MESH: Cross Reactions, chemistry.chemical_compound, Carbohydrate Conformation, MESH : Female, MESH: Carbohydrate Conformation, MESH : Host-Pathogen Interactions, biology, Host-Pathogen Interaction, MESH : Neutrophil Infiltration, Carbohydrate Sequence, Host-Pathogen Interactions, MESH : Carbohydrate Sequence, Female, MESH: Aspergillus fumigatus, Immunosuppressive Agents, Research Article, lcsh:Immunologic diseases. Allergy, Population, Immunopathology, Mycology, MESH : Mice, Inbred C57BL, Polysaccharide, Campylobacter jejuni, Polysaccharides, MESH: Mice, Inbred C57BL, Virology, MESH : Mice, Animals, MESH: Aspergillosis, MESH: Mice, 030304 developmental biology, MESH : Cell Wall, MESH: Carbohydrate Sequence, MESH: Apoptosis, MESH: Antibodies, Fungal, Fungi, MESH: Macrophages, biology.organism_classification, MESH: Neutrophil Infiltration, MESH: Polysaccharides, MESH: Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, lcsh:Biology (General), MESH : Aspergillus fumigatus, MESH : Carbohydrate Conformation, MESH : Animals
Abstract: A new polysaccharide secreted by the human opportunistic fungal pathogen Aspergillus fumigatus has been characterized. Carbohydrate analysis using specific chemical degradations, mass spectrometry, 1H and 13C nuclear magnetic resonance showed that this polysaccharide is a linear heterogeneous galactosaminogalactan composed of α1-4 linked galactose and α1-4 linked N-acetylgalactosamine residues where both monosacharides are randomly distributed and where the percentage of galactose per chain varied from 15 to 60%. This polysaccharide is antigenic and is recognized by a majority of the human population irrespectively of the occurrence of an Aspergillus infection. GalNAc oligosaccharides are an essential epitope of the galactosaminogalactan that explains the universal antibody reaction due to cross reactivity with other antigenic molecules containing GalNAc stretches such as the N-glycans of Campylobacter jejuni. The galactosaminogalactan has no protective effect during Aspergillus infections. Most importantly, the polysaccharide promotes fungal development in immunocompetent mice due to its immunosuppressive activity associated with disminished neutrophil infiltrates., Author Summary Aspergillus fumigatus is an opportunistic human fungal pathogen that causes a wide range of diseases including allergic reactions and local or systemic infections such as invasive pulmonary aspergillosis that has emerged in the recent years as a leading cause of infection related mortality among immunocompromised patients. Polysaccharides from the fungal cell wall play essential biological functions in the fungal cell biology and in host-pathogen interactions. Indeed, it has been shown that polysaccharides can modulate the human immune response; some of them (β-glucan and α-glucans) having a protective effect against Aspergillus infection. We report here the purification and chemical characterization of a new antigenic polysaccharide (galactosaminogalactan) produced by A. fumigatus. This polymer is secreted during infection. In murine models of aspergillosis, this galactosaminogalactan is not protective but it is immunosuppressive and favors A. fumigatus infection. Particularly it induces the apoptotic death of neutrophils that are the phagocytes playing an essential role in the killing of fungal pathogens.
Published: 2011
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24. Human brain: proton diffusion MR spectroscopy

Author: Charles A. Cuenod, D. Le Bihan, S. Posse, Department of Health and Human Services, National Institutes of Health [Bethesda] (NIH), Méthodes d'imagerie des échanges transcapillaires (LRI), IFR94-Université Paris Descartes - Paris 5 (UPD5), Laboratoire de Recherche en Imagerie LRI-EA4062, Université Paris Descartes - Paris 5 (UPD5), Service NEUROSPIN (NEUROSPIN), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Le Bihan, Denis, National Institutes of Health ( NIH ), Méthodes d'imagerie des échanges transcapillaires ( LRI ), IFR94-Université Paris Descartes - Paris 5 ( UPD5 ), Université Paris Descartes - Paris 5 ( UPD5 ), National Institutes of Health [Bethesda] ( NIH ), Service NEUROSPIN ( NEUROSPIN ), Direction de Recherche Fondamentale (CEA) ( DRF (CEA) ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay, Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)
Subjects: In vivo magnetic resonance spectroscopy, Male, Magnetic Resonance Spectroscopy, Proton, Phosphocreatine, [SDV.IB.IMA]Life Sciences [q-bio]/Bioengineering/Imaging, MESH : Aspartic Acid, MESH : Brain Chemistry, MESH: Aspartic Acid, MESH : Choline, 030218 nuclear medicine & medical imaging, Choline, chemistry.chemical_compound, 0302 clinical medicine, Nuclear magnetic resonance, Medicine, MESH : Female, MESH: Brain Chemistry, Diffusion (business), [ SDV.IB.IMA ] Life Sciences [q-bio]/Bioengineering/Imaging, medicine.diagnostic_test, MESH: Creatine, MESH: Choline, Pulse sequence, Human brain, MESH : Adult, MESH : Creatine, medicine.anatomical_structure, Female, Adult, MESH : Male, MESH: Phosphocreatine, 03 medical and health sciences, Humans, Radiology, Nuclear Medicine and imaging, MESH : Phosphocreatine, Spectroscopy, Brain Chemistry, Aspartic Acid, MESH: Humans, business.industry, MESH: Magnetic Resonance Spectroscopy, MESH : Humans, Magnetic resonance imaging, MESH: Adult, Creatine, MESH: Male, [SDV.IB.IMA] Life Sciences [q-bio]/Bioengineering/Imaging, chemistry, MESH : Magnetic Resonance Spectroscopy, business, MESH: Female, 030217 neurology & neurosurgery
Abstract: International audience; Diffusion of brain metabolites was measured in 10 healthy volunteers by using localized proton diffusion magnetic resonance (MR) spectroscopy. Measurements were conducted with a clinical MR imager by using a stimulated-echo pulse sequence (3,000/60 [repetition time msec/echo time msec], 200-msec mixing time) with additional outside-volume suppression. Motion artifacts due to macroscopic brain movements were compensated by means of peripheral cardiac gating and separate collection of individual spectroscopic acquisitions into a two-dimensional data matrix. Phase errors due to macroscopic motion were subsequently corrected in individual data traces prior to spectral averaging. Mean (+/- 1 standard deviation) apparent diffusion coefficients of choline-containing compounds ([0.13 +/- 0.03] x 10(-3) mm2/sec), creatine and phosphocreatine ([0.15 +/- 0.03] x 10(-3) mm2/sec), and N-acetyl aspartate ([0.18 +/- 0.02] x 10(-3) mm2/sec) were substantially smaller than that of water and were consistent with recently published data obtained in anesthetized and paralyzed animals. Adequate diffusion sensitivity for metabolites in the human brain can be obtained with clinical whole-body imagers despite macroscopic head and brain movements.
Published: 1993

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24 results on '"MESH : Magnetic Resonance Spectroscopy"'

1. GCKR polymorphism influences liver fat content in patients with type 2 diabetes

2. Liver methylene fraction by dual- and triple-echo gradient-echo imaging at 3.0T: Correlation with proton MR spectroscopy and estimation of robustness after SPIO administration

3. Effects of particulate air pollution on systolic blood pressure: A population-based approach

4. NMR-Guided Fragment-Based Approach for the Design of tRNALys3 Ligands

5. Intravoxel incoherent motion diffusion-weighted imaging in nonalcoholic fatty liver disease: a 3.0-T MR study

6. Chemical optimization of new ligands of the low-density lipoprotein receptor as potential vectors for central nervous system targeting

7. Tumor volume and metabolism of prostate cancer determined by proton magnetic resonance spectroscopic imaging at 3T without endorectal coil reveal potential clinical implications in the context of radiation oncology

8. Cadmium-glutathione solution structures provide new insights into heavy metal detoxification

9. Insight into the structure of the pUL89 C-terminal domain of the human cytomegalovirus terminase complex

10. Complications and failure of uterine artery embolisation for intractable postpartum haemorrhage

11. Structure-activity relationship analysis of the peptide deformylase inhibitor 5-bromo-1H-indole-3-acetohydroxamic acid

12. Magnetic resonance imaging and spectroscopy for quantification of hepatic steatosis: urgent need for standardization!

13. Quantification of liver fat content: comparison of triple-echo chemical shift gradient-echo imaging and in vivo proton MR spectroscopy

14. STD and TRNOESY NMR studies for the epitope mapping of the phosphorylation motif of the oncogenic protein beta-catenin recognized by a selective monoclonal antibody

15. Structural changes of Escherichia coli ferric uptake regulator during metal-dependent dimerization and activation explored by NMR and X-ray crystallography

16. Self-organisation of an oligodeoxynucleotide containing the G- and C-rich stretches of the direct repeats of the human mitochondrial DNA

17. Double molecular mimicry in Escherichia coli: binding of ribosomal protein L20 to its two sites in mRNA is similar to its binding to 23S rRNA

18. Cytochrome c and SDS: a molten globule protein with altered axial ligation

19. The tRNA-like domains of E coli and A.aeolicus transfer-messenger RNA: structural and functional studies

20. The H-NS dimerization domain defines a new fold contributing to DNA recognition

21. Spectroscopic data following stroke reveal tissue abnormality beyond the region of T2-weighted hyperintensity

22. Anomalous transverse relaxation in 1H spectroscopy in human brain at 4 Tesla

23. Galactosaminogalactan, a New Immunosuppressive Polysaccharide of Aspergillus fumigatus

24. Human brain: proton diffusion MR spectroscopy

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24 results on '"MESH : Magnetic Resonance Spectroscopy"'

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