Search

Your search keyword '"Luchinat C."' showing total 96 results
Start Over Author "Luchinat C." Database OpenAIRE
96 results on '"Luchinat C."'

1. Combining Solid-State NMR with Structural and Biophysical Techniques to Design Challenging Protein-Drug Conjugates

Author

Cerofolini, L., Vasa, K., Bianconi, E., Salobehaj, M., Cappelli, G., Bonciani, A., Licciardi, G., Perez-Rafols, A., Padilla-Cortes, L., Antonacci, S., Rizzo, D., Ravera, E., Viglianisi, C., Calderone, V., Parigi, G., Luchinat, C., Macchiarulo, A., Menichetti, S., and Fragai, M.

Subjects
Structural Biology, Drug Design, Protein-Drug Conjugates, Drug Delivery, NMR Spectroscopy
Published
2023

2. Early downregulation of hsa-miR-144-3p in serum from drug-naïve Parkinson's disease patients

Author

Zago E., Dal Molin A., Dimitri G. M., Xumerle L., Pirazzini C., Bacalini M. G., Maturo M. G., Azevedo T., Spasov S., Gomez-Garre P., Perinan M. T., Jesus S., Baldelli L., Sambati L., Calandra Buonaura G., Garagnani P., Provini F., Cortelli P., Mir P., Trenkwalder C., Mollenhauer B., Franceschi C., Lio P., Nardini C., Adarmes-Gomez A., Bartoletti-Stella A., Bhatia K. P., Marta B. -T., Boninsegna C., Broli M., Dolores B. -R., Calandra-Buonaura G., Capellari S., Carrion-Claro M., Cilea R., Clayton R., Molin A. D., De Luca S., De Massis P., Doykov I., Escuela-Martin R., Fabbri G., Gabellini A., Giuliani C., Guaraldi P., Hagg S., Hallqvist J., Halsband C., Heywood W., Houlden H., Huertas I., Jylhava J., Labrador-Espinosa M. A., Licari C., Luchinat C., Macias D., Macri S., Magrinelli F., Rodriguez J. F. M., Massimo D., Mengozzi G., Meoni G., Mignani F., Milazzo M., Mills K., Nassetti S. A., Pedersen N. L., Perinan-Tocino M. T., Ravaioli F., Sala C., Scaglione C. L. M., Schade S., Schreglmann S., Strom S., Tejera-Parrado C., Tenori L., Turano P., Valzania F., Ortega R. V., Williams D., Apollo - University of Cambridge Repository, Zago E., Dal Molin A., Dimitri G.M., Xumerle L., Pirazzini C., Bacalini M.G., Maturo M.G., Azevedo T., Spasov S., Gomez-Garre P., Perinan M.T., Jesus S., Baldelli L., Sambati L., Calandra Buonaura G., Garagnani P., Provini F., Cortelli P., Mir P., Trenkwalder C., Mollenhauer B., Franceschi C., Lio P., Nardini C., Adarmes-Gomez A., Bartoletti-Stella A., Bhatia K.P., Marta B.-T., Boninsegna C., Broli M., Dolores B.-R., Calandra-Buonaura G., Capellari S., Carrion-Claro M., Cilea R., Clayton R., Molin A.D., De Luca S., De Massis P., Doykov I., Escuela-Martin R., Fabbri G., Gabellini A., Giuliani C., Guaraldi P., Hagg S., Hallqvist J., Halsband C., Heywood W., Houlden H., Huertas I., Jylhava J., Labrador-Espinosa M.A., Licari C., Luchinat C., Macias D., Macri S., Magrinelli F., Rodriguez J.F.M., Massimo D., Mengozzi G., Meoni G., Mignani F., Milazzo M., Mills K., Nassetti S.A., Pedersen N.L., Perinan-Tocino M.T., Ravaioli F., Sala C., Scaglione C.L.M., Schade S., Schreglmann S., Strom S., Tejera-Parrado C., Tenori L., Turano P., Valzania F., Ortega R.V., and Williams D.

Subjects
Male, Aging, Molecular biology, Science, Immunology, Article, Cohort Studies, 03 medical and health sciences, 0302 clinical medicine, Medical research, Humans, Parkinson, 030304 developmental biology, Aged, 0303 health sciences, Multidisciplinary, Biological techniques, Parkinson Disease, Middle Aged, 3. Good health, nervous system diseases, Computational biology and bioinformatics, MicroRNAs, Neurology, ageing, Medicine, Female, 030217 neurology & neurosurgery, Biomarkers
Abstract

Advanced age represents one of the major risk factors for Parkinson's Disease. Recent biomedical studies posit a role for microRNAs, also known to be remodelled during ageing. However, the relationship between microRNA remodelling and ageing in Parkinson's Disease, has not been fully elucidated. Therefore, the aim of the present study is to unravel the relevance of microRNAs as biomarkers of Parkinson's Disease within the ageing framework. We employed Next Generation Sequencing to profile serum microRNAs from samples informative for Parkinson's Disease (recently diagnosed, drug-naïve) and healthy ageing (centenarians) plus healthy controls, age-matched with Parkinson's Disease patients. Potential microRNA candidates markers, emerging from the combination of differential expression and network analyses, were further validated in an independent cohort including both drug-naïve and advanced Parkinson's Disease patients, and healthy siblings of Parkinson's Disease patients at higher genetic risk for developing the disease. While we did not find evidences of microRNAs co-regulated in Parkinson's Disease and ageing, we report that hsa-miR-144-3p is consistently down-regulated in early Parkinson's Disease patients. Moreover, interestingly, functional analysis revealed that hsa-miR-144-3p is involved in the regulation of coagulation, a process known to be altered in Parkinson's Disease. Our results consistently show the down-regulation of hsa-mir144-3p in early Parkinson's Disease, robustly confirmed across a variety of analytical and experimental analyses. These promising results ask for further research to unveil the functional details of the involvement of hsa-mir144-3p in Parkinson's Disease., This work was supported by the Horizon 2020 Framework Programme (Grant number 634821, PROPAG-AGING).

Published
2022

3. NMR Spectroscopy Combined with Machine Learning Approaches for Age Prediction in Healthy and Parkinson’s Disease Cohorts through Metabolomic Fingerprints

Author

Dimitri, GM, Meoni, G, Tenori, L, Luchinat, C, Lió, P, Dimitri, GM [0000-0002-2728-4272], Meoni, G [0000-0002-8608-4641], Tenori, L [0000-0001-6438-059X], Luchinat, C [0000-0003-2271-8921], and Apollo - University of Cambridge Repository

Subjects
Fluid Flow and Transfer Processes, metabolomics aging, Process Chemistry and Technology, Parkinson's disease, machine learning, spectrum, metabolites, lipids, Parkinson’s disease, biological age, General Engineering, Computer Science Applications, General Materials Science, Instrumentation
Abstract

Peer reviewed: True, Biological aging can be affected by several factors such as drug treatments and pathological conditions. Metabolomics can help in the estimation of biological age by analyzing the differences between predicted and actual chronological age in different subjects. In this paper, we compared three different and well-known machine learning approaches—SVM, ElasticNet, and PLS—to build a model based on the 1H-NMR metabolomic data of serum samples, able to predict chronological age in control individuals. Then, we tested these models in two pathological cohorts of de novo and advanced PD patients. The discrepancies observed between predicted and actual age in patients are interpreted as a sign of a (pathological) biological aging process.

Published
2022

5. Early downregulation of hsa-miR-144-3p in serum from drug-naïve Parkinson’s disease patients

Author

Zago, E., Dal Molin, A., Dimitri, G. M., Xumerle, L., Pirazzini, C., Bacalini, M. G., Maturo, M. G., Azevedo, T., Spasov, S., Gomez-Garre, P., Perinan, M. T., Jesus, S., Baldelli, L., Sambati, L., Calandra-Buonaura, G., Garagnani, P., Provini, F., Cortelli, P., Mir, P., Trenkwalder, C., Mollenhauer, B., Franceschi, C., Lio, P., Nardini, C., Adarmes-Gomez, A., Bartoletti-Stella, A., Bhatia, K. P., Marta, B. -T., Boninsegna, C., Broli, M., Dolores, B. -R., Capellari, S., Carrion-Claro, M., Cilea, R., Clayton, R., Molin, A. D., De Luca, S., De Massis, P., Doykov, I., Escuela-Martin, R., Fabbri, G., Gabellini, A., Giuliani, C., Guaraldi, P., Hagg, S., Hallqvist, J., Halsband, C., Heywood, W., Houlden, H., Huertas, I., Jylhava, J., Labrador-Espinosa, M. A., Licari, C., Luchinat, C., Macias, D., Macri, S., Magrinelli, F., Rodriguez, J. F. M., Massimo, D., Mengozzi, G., Meoni, G., Mignani, F., Milazzo, M., Mills, K., Nassetti, S. A., Pedersen, N. L., Perinan-Tocino, M. T., Ravaioli, F., Sala, C., Scaglione, C. L. M., Schade, S., Schreglmann, S., Strom, S., Tejera-Parrado, C., Tenori, L., Turano, P., Valzania, F., Ortega, R. V., and Williams, D.

Subjects
hsa‑miR‑144‑3p, serum, Parkinson’s disease patients
Published
2022

7. Protein-protein interactions

Author

Di Savino, A., Ubbink, M., Luchinat, C., Parigi, G., Ravera, E., Luchinat, C., Parigi, G., and Ravera, E.

Subjects
chemistry.chemical_compound, Paramagnetism, Electron transfer, Chemistry, Chemical physics, Docking (molecular), Dimer, Intermolecular force, Protein complex formation, Crystal structure, Protein–protein interaction
Abstract

Paramagnetic NMR methods are excellently suited for the study of protein–protein complexes in solution. Intermolecular pseudocontact shifts (PCSs), residual dipolar couplings (RDCs) and paramagnetic relaxations enhancements (PREs) can be used, ideally in combination, for docking proteins and determining their orientation in the complex. PCSs can be used for breaking the structure symmetry in dimer complexes. PCSs also can be applied to detect structural differences in proteins and protein complexes in solution in comparison to crystal structures. RDCs are sensitive to the degree of alignment of both partners in a protein complex and are thus very useful to detect dynamics within complexes. PREs can detect states in which nuclei approach a paramagnetic centre closely, even if it exists only for a small fraction of the time. Thus, PREs are used to detect minor states and characterize ensembles. PRE studies have been the foundation for characterizing encounter states and the process of protein complex formation. In weak complexes, such as are found in electron transfer chains, proteins can be in an encounter state for a large fraction of the complex lifetime. Paramagnetic NMR tools thus have found many applications for studying protein complexes, and more may be on the horizon.

Published
2018

8. Mixing Aβ(1-40) and Aβ(1-42) peptides generates unique amyloid fibrils

Author

Cerofolini, L., Ravera, E., Bologna, S., Wiglenda, T., Boddrich, A., Purfurst, B., Benilova, I., Korsak, M., Gallo, G., Rizzo, D., Gonnelli, L., Fragai, M., De Strooper, B., Wanker, E. E., and Luchinat, C.

Subjects
Solid-state NMR spectroscopy, Beta-amyloid, fibrils
Published
2020

9. Sarcolab pilot study into skeletal muscle's adaptation to long-term spaceflight

Author

Rittweger J, Albracht K, Flück M, Ruoss S, Brocca L, Longa E, Moriggi M, Seynnes O, Di Giulio I, Tenori L, Vignoli A, Capri M, Gelfi C, Luchinat C, Franceschi C, Bottinelli R, Cerretelli P, Narici M., and Rittweger J, Albracht K, Flück M, Ruoss S, Brocca L, Longa E, Moriggi M, Seynnes O, Di Giulio I, Tenori L, Vignoli A, Capri M, Gelfi C, Luchinat C, Franceschi C, Bottinelli R, Cerretelli P, Narici M.

Subjects
skeletal-muscle, Spaceflight
Abstract

Spaceflight causes muscle wasting. The Sarcolab pilot study investigated two astronauts with regards to plantar flexor muscle size, architecture, and function, and to the underlying molecular adaptations in order to further the understanding of muscular responses to spaceflight and exercise countermeasures. Two crew members (A and B) spent 6 months in space. Crew member A trained less vigorously than B. Postflight, A showed substantial decrements in plantar flexor volume, muscle architecture, in strength and in fiber contractility, which was strongly mitigated in B. The difference between these crew members closely reflected FAK-Y397 abundance, a molecular marker of muscle's loading history. Moreover, crew member A showed downregulation of contractile proteins and enzymes of anaerobic metabolism, as well as of systemic markers of energy and protein metabolism. However, both crew members exhibited decrements in muscular aerobic metabolism and phosphate high energy transfer. We conclude that countermeasures can be effective, particularly when resistive forces are of sufficient magnitude. However, to fully prevent space-related muscular deterioration, intersubject variability must be understood, and intensive exercise countermeasures programs seem mandatory. Finally, proteomic and metabolomic analyses suggest that exercise benefits in space may go beyond mere maintenance of muscle mass, but rather extend to the level of organismic metabolism.

Published
2018

14. Expression and purification of Human S100A2

Author

Albanese S., Bertini I., Bhaumik A., Luchinat C., BABINI, ELENA, Albanese S., Babini E., Bertini I., Bhaumik A., and Luchinat C.

Subjects
protein purification, calcium binding protein, S100A2, recombinant protein, S100
Published
2005

15. The High-throughput production of recombinant proteins for structural and functional characterization by NMR spectroscopy

Author

CASADEI, FEDERICA, BABINI, ELENA, CAPOZZI, FRANCESCO, Bertini I., Chirivino E., Luchinat C., Casadei F., Babini E., Bertini I., Capozzi F., Chirivino E., and Luchinat C.

Subjects
S100A16, high-throughput protein purification, gateway technology, recombinant protein
Abstract

With the identification of >35000 genes in the human genome, there is an increasing demand for high-throughput expression of recombinant proteins. An immediate challenge of the post genomic era is to assign biological function to all the proteins encoded by the genome1.This work is part of an high-throughput project faced to the production of recombinant proteins belonging to the calcium-binding family and their targets, selected for the high interest in human cellular function. The aim is to obtain pure recombinant protein samples correctly folded for structural determination by NMR. This information is essential to understand the mechanism of protein function and for the general purpose to identify new drug targets. To increase the number of folded samples, many different cloning and expression conditions were tested, applying Gateway technology. The genes coding for selected proteins were recombined into five different expression vectors (pETG-20A, pETG-30A, pETG-60A, pDEST17, pDEST15) carrying specific protein fusion tags. Three different E.coli host strains were used for proteins expression (BL21 Gold, pLys, Codon plus). The proteins mainly expressed in a soluble form were produced on a large-scale and purified for spectroscopic analysis. Results so far obtained on one of the protein selected, S100A16, are here reported and discussed.

Published
2005

17. Examination of Matrix Metalloproteinase-1 in Solution: A PREFERENCE FOR THE PRE-COLLAGENOLYSIS STATE

Author

Cerofolini, L., Fields, G. B., Fragai, M., Geraldes, C. F. G. C., Luchinat, C., Parigi, G., Ravera, E., Svergun, Dmitri, and Teixeira, J. M. C.

Subjects
ddc:570, Scattering, Small Angle, Enzymology, Humans, Matrix Metalloproteinase 1, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Secondary, Protein Structure, Tertiary
Abstract

The journal of biological chemistry 288(42), 30659 - 30671 (2013). doi:10.1074/jbc.M113.477240, Catalysis of collagen degradation by matrix metalloproteinase 1 (MMP-1) has been proposed to critically rely on flexibility between the catalytic (CAT) and hemopexin-like (HPX) domains. A rigorous assessment of the most readily accessed conformations in solution is required to explain the onset of substrate recognition and collagenolysis. The present study utilized paramagnetic NMR spectroscopy and small angle x-ray scattering (SAXS) to calculate the maximum occurrence (MO) of MMP-1 conformations. The MMP-1 conformations with large MO values (up to 47%) are restricted into a relatively small conformational region. All conformations with high MO values differ largely from the closed MMP-1 structures obtained by x-ray crystallography. The MO of the latter is ~20%, which represents the upper limit for the presence of this conformation in the ensemble sampled by the protein in solution. In all the high MO conformations, the CAT and HPX domains are not in tight contact, and the residues of the HPX domain reported to be responsible for the binding to the collagen triple-helix are solvent exposed. Thus, overall analysis of the highest MO conformations indicated that MMP-1 in solution was poised to interact with collagen and then could readily proceed along the steps of collagenolysis., Published by Soc., Bethesda, Md.

Published
2013
Full Text
View/download PDF

21. NMR in the SPINE Structural Proteomics project

Author

AB, E., Atkinson, A.R., Banci, L., Bertini, I., Ciofi-Baffoni, S., Brunner, K., Diercks, T., Doetsch, V, Engelke, F., Folkers, G.E., Griesinger, C., Gronwald, W., Gunther, U., Habeck, M., de Jong, R.N., Kalbitzer, H.R., Kieffer, B., Leeflang, B.R., Loss, S., Luchinat, C., Marquardsen, T., Moskau, D., Neidig, K.P., Nilges, M., Piccioli, M., Pierattelli, R., Rieping, W., Schippmann, T., Schwalbe, H., Travé, G., Trenner, J., Wöhnert, J., Zweckstetter, M., Kaptein, R., Chemie van glyco-conjugaten, NMR-spectroscopie, and Dep Scheikunde

Published
2006

34. NMR of Transferrins

Author

Luchinat, C. and Sola, Marco

Subjects
NMR, transferrins
Published
1996

36. Zinc Enzymes

Author

Luchinat, C. and Sola, Marco

Subjects
Zinc, enzymes
Published
1994

43. NMR applications in food analysis: Part B

Author

Proietti, N., Capitani, D., Aru, V., Bellomaria, A., Bertocchi, F., Botta, B., Cagliani, L. R., Caligiani, A., Capozzi, F., Çela, D., Marincola, F. C., alessandra ciampa, Coco, L. D., Consonni, R., Corsaro, C., Delfini, M., Fanizzio, F. P., Gallo, V., Ghirga, F., Gianferri, R., Girellio, C. R., Ingallina, C., Laghi, L., Latronico, M., Longobardi, F., Luchinat, C., Mallamace, D., Mammi, S., Mandaliti, W., Mannina, L., Marini, F., Mastrorilli, P., Mazzei, P., Miccheli, A., Micozzio, A., Miloneo, S., Mucci, A., Nepravishta, R., Paci, M., Palisi, A., Sobolev, A. P., Piccolo, A., Picone, G., Randazzo, A., Righi, V., Rotondo, A., Salvo, A., Savorani, F., Scano, P., Schievano, E., Sciubba, F., Tenori, L., Trimigno, A., Turano, P., Vasi, S., Tullio, V. D., Proietti N., Capitani D., Aru V., Bellomaria A., Bertocchi F., Botta B., Cagliani L.R., Caligiani A., Capozzi F., Cela D., Marincola F.C., Ciampa A., Coco L.D., Consonni R., Corsaro C., Delfini M., Fanizzio F.P., Gallo V., Ghirga F., Gianferri R., Girellio C.R., Ingallina C., Laghi L., Latronico M., Longobardi F., Luchinat C., Mallamace D., Mammi S., Mandaliti W., Mannina L., Marini F., Mastrorilli P., Mazzei P., Miccheli A., Micozzio A., Miloneo S., Mucci A., Nepravishta R., Paci M., Palisi A., Sobolev A.P., Piccolo A., Picone G., Randazzo A., Righi V., Rotondo A., Salvo A., Savorani F., Scano P., Schievano E., Sciubba F., Tenori L., Trimigno A., Turano P., Vasi S., and Tullio V.D.

Subjects
low-field NMR relaxometry, NMR-imaging, food science, food composition, food composition, Food composition, Food science, Low-field NMR relaxometry, NMR-imaging, Chemistry (all), low-field NMR relaxometry, food science, chemometrics, NMR
Abstract

Multifarious applications of NMR (high-resolution NMR in liquid-state and in semi-solid matrices, low-field NMR relaxometry, and NMR-imaging) in the analysis of food components and entire food samples are described using examples of different food matrices and different problems related to food safety, traceability, geographical and botanical origin, farming methods, food processing, maturation and ageing, etc. Althoug NMR has not yet been recognized as an official methodology for the food control the numerous applications of NMR reported in the literature show the potenziality of this methodology also as an approach complementary to the other recognized conventional methodologies.

Catalog

Books, media, physical & digital resources
See catalog results