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1. The NEREA Augmented Observatory: an integrative approach to marine coastal ecology

Author

Campese, Lucia, Russo, Luca, Abagnale, Maria, Alberti, Adriana, Bachi, Giancarlo, Balestra, Cecilia, Bellardini, Daniele, Buondonno, Angela, Cardini, Ulisse, Carotenuto, Ylenia, Checcucci, Giovanni, Chiusano, Maria Luisa, D’Ambra, Isabella, d’Ippolito, Giuliana, Di Capua, Iole, Donnarumma, Vincenzo, Fontana, Angelo, Furia, Marta, Galarza-Verkovitch, Denisse, Gallia, Roberto, Labadie, Karine, Leone, Serena, Licandro, Priscilla, Longo, Antonio, Maselli, Maira, Merquiol, Louise, Murano, Carola, Oliveira, Pedro H., Passarelli, Augusto, Percopo, Isabella, Perdereau, Aude, Piredda, Roberta, Raffini, Francesca, Roncalli, Vittoria, Ruscheweyh, Hans-Joachim, Russo, Ennio, Saggiomo, Maria, Santinelli, Chiara, Sarno, Diana, Sunagawa, Shinichi, Tramontano, Ferdinando, Trano, Anna Chiara, Uttieri, Marco, Wincker, Patrick, Zampicinini, Gianpaolo, Casotti, Raffaella, Conversano, Fabio, D’Alelio, Domenico, Iudicone, Daniele, Margiotta, Francesca, and Montresor, Marina

Published
2024
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4. Evolution of the ribbon-like organization of the Golgi apparatus in animal cells

Author

Benvenuto,Giovanna, Leone, Serena, Astoricchio, Emanuele, Bormke, Sophia, Jasek, Sanja, D’Aniello, Enrico, Kittelmann, Maike, McDonald, Kent, Hartenstein, Volker, Baena, Valentina, Escrivà, Héctor, Bertrand, Stephanie, Schierwater, Bernd, Burkhardt, Pawel, Ruiz-Trillo, Iñaki, Jékely, Gáspár, Ullrich-Luter, Jack, Luter, Carsten, D’Aniello, Salvatore, Arnone, Maria Ina, Ferraro, Francesco, Benvenuto,Giovanna, Leone, Serena, Astoricchio, Emanuele, Bormke, Sophia, Jasek, Sanja, D’Aniello, Enrico, Kittelmann, Maike, McDonald, Kent, Hartenstein, Volker, Baena, Valentina, Escrivà, Héctor, Bertrand, Stephanie, Schierwater, Bernd, Burkhardt, Pawel, Ruiz-Trillo, Iñaki, Jékely, Gáspár, Ullrich-Luter, Jack, Luter, Carsten, D’Aniello, Salvatore, Arnone, Maria Ina, and Ferraro, Francesco

Abstract

The ‘‘ribbon,’’ a structural arrangement in which Golgi stacks connect to each other, is considered to be restricted to vertebrate cells. Although ribbon disruption is linked to various human pathologies, its functional role in cellular processes remains unclear. In this study, we investigate the evolutionary origin of the Golgi ribbon. We observe a ribbon-like architecture in the cells of several metazoan taxa suggesting its early emergence in animal evolution predating the appearance of vertebrates. Supported by AlphaFold2 modeling, we propose that the evolution of Golgi reassembly and stacking protein (GRASP) binding by golgin tethers may have driven the joining of Golgi stacks resulting in the ribbon-like configuration. Additionally, we find that Golgi ribbon assembly is a shared developmental feature of deuterostomes, implying a role in embryogenesis. Overall, our study points to the functional significance of the Golgi ribbon beyond vertebrates and underscores the need for further investigations to unravel its elusive biological roles.

Published
2024

6. Evolution of the ribbon-like organization of the Golgi apparatus in animal cells

Author

Benvenuto, Giovanna, primary, Leone, Serena, additional, Astoricchio, Emanuele, additional, Bormke, Sophia, additional, Jasek, Sanja, additional, D’Aniello, Enrico, additional, Kittelmann, Maike, additional, McDonald, Kent, additional, Hartenstein, Volker, additional, Baena, Valentina, additional, Escrivà, Héctor, additional, Bertrand, Stephanie, additional, Schierwater, Bernd, additional, Burkhardt, Pawel, additional, Ruiz-Trillo, Iñaki, additional, Jékely, Gáspár, additional, Ullrich-Lüter, Jack, additional, Lüter, Carsten, additional, D’Aniello, Salvatore, additional, Arnone, Maria Ina, additional, and Ferraro, Francesco, additional

Published
2024
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13. Oxidoreductases and metal cofactors in the functioning of the earth

Author

Hay Mele, Bruno, additional, Monticelli, Maria, additional, Leone, Serena, additional, Bastoni, Deborah, additional, Barosa, Bernardo, additional, Cascone, Martina, additional, Migliaccio, Flavia, additional, Montemagno, Francesco, additional, Ricciardelli, Annarita, additional, Tonietti, Luca, additional, Rotundi, Alessandra, additional, Cordone, Angelina, additional, and Giovannelli, Donato, additional

Published
2023
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16. Oxidoreductases and metal cofactors in the functioning of Earth

Author

Hay Mele, Bruno, primary, Monticelli, Maria, additional, Leone, Serena, additional, Bastoni, Deborah, additional, Barosa, Bernardo, additional, Cascone, Martina, additional, Migliaccio, Flavia, additional, Montemagno, Francesco, additional, Ricciardelli, Annarita, additional, Tonietti, Luca, additional, Rotundi, Alessandra, additional, Cordone, Angelina, additional, and Giovannelli, Donato, additional

Published
2023
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19. Evolution of the ribbon-like organization of the Golgi apparatus in animal cells

Author

Benvenuto, Giovanna, primary, Leone, Serena, additional, Astoricchio, Emanuele, additional, Bormke, Sophia, additional, Jasek, Sanja, additional, D’Aniello, Enrico, additional, Kittelmann, Maike, additional, McDonald, Kent, additional, Hartenstein, Volker, additional, Baena, Valentina, additional, Escrivà, Héctor, additional, Bertrand, Stephanie, additional, Schierwater, Bernd, additional, Burkhardt, Pawel, additional, Ruiz-Trillo, Iñaki, additional, Jékely, Gáspár, additional, Ullrich-Lüter, Jack, additional, Lüter, Carsten, additional, D’Aniello, Salvatore, additional, Arnone, Maria Ina, additional, and Ferraro, Francesco, additional

Published
2023
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23. Toxicological Impacts of Microplastics: Effects on Levels of Cellular Thiols in Mytilus galloprovincialis.

Author

Murano, Carola, Palumbo, Anna, and Leone, Serena

Subjects
PLASTIC marine debris, MYTILUS galloprovincialis, MICROPLASTICS, BIOCOMPLEXITY, OXIDIZING agents, OXIDATIVE stress, THIOLS
Abstract

Over the last decade, the biological impact of microplastics in marine environments has become a serious global concern. Beyond their biological complexity, it is believed that many lethal and sublethal effects related to microplastic toxicity are triggered by oxidative stress and subsequently activated pathways. Thus, for marine organisms, having efficient mechanisms to fight the accumulation of oxidizing agents becomes indispensable to counteract the effects of microplastics. To date, our knowledge of the physiological effects of microplastics and the response of the antioxidant system in benthic species remains limited. The purpose of our study was to investigate the effects of short‐term exposure on the levels of two fundamental nonprotein antioxidants, glutathione (GSH) and ovothiol (OSH), in different tissues of Mytilus galloprovincialis. Our results show that the metabolism of OSH and GSH in mussels is clearly affected by acute microplastic exposure, and that the antioxidant response differs based on sex and reproductive stage. Indeed, although in the reproductive season the overall levels of GSH and OSH in different tissues significantly increase with respect to the control condition, the antioxidant response of the organisms, especially males, in the spent stage often exhibits a biphasic U‐shaped dose–response effect. Our study represents a pivotal investigation on the effects of microplastic exposure on the pools of two fundamental cellular antioxidants, with potential ecodiagnostic implications to forecast the stress status after exposure to microplastics, and highlights the possibility that the effects of these contaminants may vary over time based on the physiological condition of the animals. Environ Toxicol Chem 2023;42:1607–1613. © 2023 SETAC [ABSTRACT FROM AUTHOR]

Published
2023
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26. Cost analysis of extended half-life recombinant factor IX products in the treatment of haemophilia B in Italy: an update

Author

Aiello, Andrea, Mancuso, Maria E., Leone, Serena, Rossi, Letizia, Cioni, Lorenzo, Teruzzi, Cristina, Aiello, Andrea, Mancuso, Maria E., Leone, Serena, Rossi, Letizia, Cioni, Lorenzo, and Teruzzi, Cristina

Abstract

Haemophilia B (HB) is a rare disease which may lead to chronic disabling arthropathy, resulting in a significant clinical, social and economic impact. In recent years, new extended half-life (EHL) factor IX concentrates produced by recombinant technology (rFIX) have been developed. They have shown significantly prolonged half-life as compared to other rFIX products and improved bleeding control when used as prophylaxis. To date, EHL rFIX products reimbursed in Italy are a recombinant coagulation factor IX produced with Fc technology (rFIXFc) and a recombinant fusion protein containing rFIX fused with recombinant albumin (rIX-FP). The results of extension studies with injection intervals with a median of almost every 14 days for the complete individualized interval prophylaxis (IP) group on rFIXFc and 21 days for a selected subgroup of patients on rIX-FP have recently been published.The aim of this analysis was to estimate the cost of prophylactic treatment with rFIXFc and rIX-FP in adult patients, in the light of new clinical evidence and current average prices in Italy.The cost of therapy was estimated on the basis of the results of extension studies, the average prices reported in regional drug tenders and assuming an average patient weight of 70 kg.The analysis estimated a cost per patient/year between €224,407 and €230,355 for rFIXFc and between €242,259 and €368,587 for rIX-FP. The sensitivity analysis confirmed the robustness of the results.The use of rFIXFc over rIX-FP proves to be the least expensive choice for the treatment of HB in Italy.

Published
2022

35. Disordered Peptides Looking for Their Native Environment: Structural Basis of CB1 Endocannabinoid Receptor Binding to Pepcans

Author

Emendato, Alessandro, Guerrini, Remo, Marzola, Erika, Wienk, Hans, Boelens, Rolf, Leone, Serena, Picone, Delia, Sub NMR Spectroscopy, NMR Spectroscopy, Emendato, Alessandro, Guerrini, Remo, Marzola, Erika, Wienk, Han, Boelens, Rolf, Leone, Serena, Picone, Delia, Sub NMR Spectroscopy, and NMR Spectroscopy

Subjects
0301 basic medicine, Allosteric modulator, Cannabinoid receptor, CB1 endocannabinoid receptor, Endocannabinoid system, Hemopressin, Intrinsically unfolded peptides, Pepcans, Structure-activity relationships, Allosteric regulation, Peptide, Biochemistry, Biochemistry, Genetics and Molecular Biology (miscellaneous), NO, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Molecular Biosciences, Receptor, lcsh:QH301-705.5, Molecular Biology, intrinsically unfolded peptides, Original Research, chemistry.chemical_classification, Pepcan, hemopressin, structure-activity relationships, Biological activity, pepcans, Structure-activity relationship, 3. Good health, 030104 developmental biology, lcsh:Biology (General), chemistry, Biophysics, lipids (amino acids, peptides, and proteins), Intrinsically unfolded peptide, 030217 neurology & neurosurgery
Abstract

Endocannabinoid peptides, or "pepcans," are endogenous ligands of the CB1 cannabinoid receptor. Depending on their length, they display diverse activity: For instance, the nona-peptide Pepcan-9, also known as hemopressin, is a powerful inhibitor of CB1, whereas the longer variant Pepcan-12, which extends by only three amino acid residues at the N-terminus, acts on both CB1 and CB2 as an allosteric modulator, although with diverse effects. Despite active research on their pharmacological applications, very little is known about structure-activity relationships of pepcans. Different structures have been proposed for the nona-peptide, which has also been reported to form fibrillar aggregates. This might have affected the outcome and reproducibility of bioactivity studies. In an attempt of elucidating the determinants of both biological activity and aggregation propensity of Pepcan-9 and Pepcan-12, we have performed their structure characterization in solvent systems characterized by different polarity and pH. We have found that, while disordered in aqueous environment, both peptides display helical structure in less polar environment, mimicking the proteic receptor milieu. In the case of Pepcan-9, this structure is fully consistent with the observed modulation of the CB1. For Pepcan-12, whose allosteric binding site is still unknown, the presented structure is compatible with the binding at one of the previously proposed allosteric sites on CB1. These findings open the way to structure-driven design of selective peptide modulators of CB1.

Published
2018
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41. Production and characterization of a fusion form of hepatitis E virus tORF2 capsid protein in Escherichia coli.

Author

Boumaiza, Mohamed, Trabelsi, Khaled, Choucha, Zeineb, Akrouti, Ines, Leone, Serena, Picone, Delia, and Kallel, Héla

Subjects
HEPATITIS E virus, ESCHERICHIA coli, CYTOSKELETAL proteins, CHIMERIC proteins, ZIKA virus, PROTEINS, CLONORCHIS sinensis, RECOMBINANT viruses
Abstract

Hepatitis E virus (HEV) is a nonenveloped virus causing an emerging zoonotic disease posing a severe threat to the public health in the world, especially to pregnant women. In this study, a truncated form (aa 368–606) of the open reading frame 2 of the capsid protein (tORF2-HEV), a major structural protein of HEV, was expressed in Escherichia coli. This work characterizes for the first time, the fused Glutathione-S-Transferase-tagged tORF2 (GST-tORF2) and tORF2-HEV forms in E. coli. The fusion protein was purified by affinity chromatography with a purity higher than 90% and to yield about 27% after thrombin digestion. The purified GST-tORF2 protein was then characterized by western blot, using anti-GST antibodies, and CD spectroscopy. The GST-tORF2 and tORF2-HEV proteins were shown to be efficient to develop an ELISA test to detect anti-HEV IgG in mice sera immunized with a recombinant full length ORF2 protein. Sera showed a significant increase of the absorbance signal at 450 nm, in plate wells coated with a quantity of 0.5, 1 and 2 µg of proteins. ELISA plates coated with the purified GST-tORF2 and tORF2-HEV showed similar response when compared to the HEV ELISA where total insect cell lysate, infected with the recombinant baculovirus expressing full ORF2, was used as positive control. [ABSTRACT FROM AUTHOR]

Published
2021
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43. Side-Chain Protons are Back with > 100kHz MAS

Author

Stanek, Jan, Andreas, Loren B, Jaudzems, Kristaps, Cala - De Paepe, Diane, Lalli, Daniela, Bertarello, Andrea, Schubeis, Tobias, Akopjana, Inara, Kotelovica, Svetlana, Tars, Kaspars, Pica, Andrea, Leone, Serena, Picone, Delia, Xu, Zhi-Qiang, Dixon, Nicholas E., Martinez, Denis, Berbon, Mélanie, El Mammeri, Nadia, Noubhani, Abdelmajid, Saupe, Sven, Habenstein, Birgit, Loquet, Antoine, Pintacuda, Guido, Biological Solid-State NMR Methods - Méthodes de RMN à l'état solide en biologie, Institut des Sciences Analytiques (ISA), Institut de Chimie du CNRS (INC)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Biomed Res & Study Ctr, Dipartimento di Scienze Chimiche, Università degli studi di Napoli Federico II, School of Chemistry [Wollongong], University of Wollongong [Australia], Chimie et Biologie des Membranes et des Nanoobjets (CBMN), Université de Bordeaux (UB)-École Nationale d'Ingénieurs des Travaux Agricoles - Bordeaux (ENITAB)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut de biochimie et génétique cellulaires (IBGC), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), and École Nationale d'Ingénieurs des Travaux Agricoles - Bordeaux (ENITAB)-Institut de Chimie du CNRS (INC)-Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[CHIM.ANAL]Chemical Sciences/Analytical chemistry, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2017

44. Probing structural changes during amyloid aggregation of the sweet protein MNEI.

Author

Donnarumma, Federica, Leone, Serena, Delfi, Masoud, Emendato, Alessandro, Ami, Diletta, Laurents, Douglas V., Natalello, Antonino, Spadaccini, Roberta, and Picone, Delia

Subjects
*SURFACE dynamics, *IONIC strength, *ELECTRON spectroscopy, *PROTEINS, *INFRARED spectroscopy, *GEL electrophoresis, *DENATURING gradient gel electrophoresis, *CLUSTERING of particles
Abstract

Protein self‐assembly is a ubiquitous phenomenon, traditionally studied for its links to amyloid pathologies, which has also gained attention as its physiological roles and possible biotechnological applications emerged over time. It is also known that varying the conditions to which proteins are exposed can lead to aggregate polymorphism. To understand the factors that trigger aggregation and/or direct it toward specific outcomes, we performed a multifaceted structural characterization of the thermally induced self‐assembly process of MNEI, a model protein able to form amyloid aggregates under nondenaturing conditions. MNEI is also known for its extreme sweetness which, combined with a considerable thermal stability, makes the protein a promising alternative sweetener. Fourier‐transformed infrared spectroscopy and electron microscopy data showed that the presence of NaCl accelerates the kinetics of fibrillar aggregation, while disfavoring the population of off‐pathway states that are instead detected by native gel electrophoresis at low ionic strength. NMR studies revealed how NaCl modulates the self‐assembling mechanism of MNEI, switching the process from soluble oligomeric forms to fibrils. Comparative analysis demonstrated that the presence of NaCl induces local differences in the protein dynamics and surface accessibility, without altering the native fold. We identified the regions most affected by the presence of NaCl, which control the aggregation process, and represent hot spots on the protein surface for the rational design of new mutants with controlled aggregation propensity. [ABSTRACT FROM AUTHOR]

Published
2020
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46. Backbone and side-chain proton NMR assignment in fully protonated proteins: microcrystals, sedimented assemblies, and amyloid fibrils

Author

Stanek, Jan, Andreas, Loren, Jaudzems, Kristaps, Cala, Diane, Lalli, Daniela, Bertarello, Andrea, Schubeis, Tobias, Akopjana, Inara, Kotelovica, Svetlana, Tars, Kaspars, Pica, Andrea, Leone, Serena, Picone, Delia, Xu, Zhi-Qiang, Dixon, Nicholas, Martinez, Denis, Berbon, Melanie, El Mammeri, Nadia, Noubhani, Abdelmajid, Saupe, Sven, Habenstein, Birgit, Loquet, Antoine, Pintacuda, Guido, Biological Solid-State NMR Methods - Méthodes de RMN à l'état solide en biologie, Institut des Sciences Analytiques (ISA), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Biomed Res & Study Ctr, Latvian Biomed Res & Study Ctr, Dept Mol Biol, University of Latvia (LU), Dipartimento di Scienze Chimiche, University of Naples Federico II = Università degli studi di Napoli Federico II, School of Chemistry [Wollongong], University of Wollongong [Australia], Chimie et Biologie des Membranes et des Nanoobjets (CBMN), Université de Bordeaux (UB)-École Nationale d'Ingénieurs des Travaux Agricoles - Bordeaux (ENITAB)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut de biochimie et génétique cellulaires (IBGC), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Fondation pour la Chimie des Substances Naturelles, IR-RMN FR3050, Fondazione con il Sud (grant 2011- PDR-19), European Project: 648974,H2020,ERC-2014-CoG,P-MEM-NMR(2015), European Project: 639020,H2020,ERC-2014-STG,Weakinteract(2015), European Project: 624918,EC:FP7:PEOPLE,FP7-PEOPLE-2013-IIF,MEM-MAS(2014), European Project: 661799,H2020,H2020-MSCA-IF-2014,COMPLEX-fastMAS-NMR(2016), European Project: 661175,H2020,H2020-MSCA-IF-2014,virus-DNP-NMR(2015), European Project: 317127,EC:FP7:PEOPLE,FP7-PEOPLE-2012-ITN,PNMR(2013), Institut de Chimie du CNRS (INC)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), and Università degli studi di Napoli Federico II

Subjects
[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, magic-angle spinning, proton detection, solid-state NMR spectroscopy, resonance assignment
Abstract

International audience; Wir beschreiben die sensitive Messung von alpha-Protonen in voll protonierten Proteinen durch Festkörper-NMR mit Rotation um den magischen Winkel (MAS) von 100-111 kHz. Die exzellente Auflösung in der Cα-Hα-Ebene wird für 5 Proteine gezeigt, darunter Mikrokristalle, ein sedimentierter Komplex, ein Kapsid und Amyloidfibrillen. Ausgehend davon wurde ein Satz 3D-Spektren für die sequenzspezifische Zuordnung der Rückgrat- und der aliphatischen Seitenketten-Resonanzen entwickelt. Dabei wurden nur 500 μg Probe verwendet. Diese Entwicklungen beschleunigen strukturelle Untersuchungen von biomolekularen Komplexen, die nur in Submilligramm-Mengen verfügbar sind, ohne die Notwendigkeit einer Deuterierung.; We demonstrate sensitive detection of alpha protons of fully protonated proteins by solid-state NMR with 100-111 kHz magic-angle spinning (MAS). The excellent resolution in the Cα-Hα plane is demonstrated for 5 proteins, including microcrystals, a sedimented complex, a capsid and amyloid fibrils. A set of 3D spectra based on a Cα-Hα detection block was developed and applied for the sequence-specific backbone and aliphatic side-chain resonance assignment using only 500 μg of sample. These developments accelerate structural studies of biomolecular assemblies available in submilligram quantities without the need of protein deuteration.

Published
2016
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48. Frontispiece: NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils

Author

Stanek, Jan, primary, Andreas, Loren B., additional, Jaudzems, Kristaps, additional, Cala, Diane, additional, Lalli, Daniela, additional, Bertarello, Andrea, additional, Schubeis, Tobias, additional, Akopjana, Inara, additional, Kotelovica, Svetlana, additional, Tars, Kaspars, additional, Pica, Andrea, additional, Leone, Serena, additional, Picone, Delia, additional, Xu, Zhi-Qiang, additional, Dixon, Nicholas E., additional, Martinez, Denis, additional, Berbon, Mélanie, additional, El Mammeri, Nadia, additional, Noubhani, Abdelmajid, additional, Saupe, Sven, additional, Habenstein, Birgit, additional, Loquet, Antoine, additional, and Pintacuda, Guido, additional

Published
2016
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49. Frontispiz: Zuordnung der Rückgrat- und Seitenketten-Protonen in vollständig protonierten Proteinen durch Festkörper-NMR-Spektroskopie: Mikrokristalle, Sedimente und Amyloidfibrillen

Author

Stanek, Jan, primary, Andreas, Loren B., additional, Jaudzems, Kristaps, additional, Cala, Diane, additional, Lalli, Daniela, additional, Bertarello, Andrea, additional, Schubeis, Tobias, additional, Akopjana, Inara, additional, Kotelovica, Svetlana, additional, Tars, Kaspars, additional, Pica, Andrea, additional, Leone, Serena, additional, Picone, Delia, additional, Xu, Zhi-Qiang, additional, Dixon, Nicholas E., additional, Martinez, Denis, additional, Berbon, Mélanie, additional, Mammeri, Nadia El, additional, Noubhani, Abdelmajid, additional, Saupe, Sven, additional, Habenstein, Birgit, additional, Loquet, Antoine, additional, and Pintacuda, Guido, additional

Published
2016
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50. Zuordnung der Rückgrat- und Seitenketten-Protonen in vollständig protonierten Proteinen durch Festkörper-NMR-Spektroskopie: Mikrokristalle, Sedimente und Amyloidfibrillen

Author

Stanek, Jan, primary, Andreas, Loren B., additional, Jaudzems, Kristaps, additional, Cala, Diane, additional, Lalli, Daniela, additional, Bertarello, Andrea, additional, Schubeis, Tobias, additional, Akopjana, Inara, additional, Kotelovica, Svetlana, additional, Tars, Kaspars, additional, Pica, Andrea, additional, Leone, Serena, additional, Picone, Delia, additional, Xu, Zhi-Qiang, additional, Dixon, Nicholas E., additional, Martinez, Denis, additional, Berbon, Mélanie, additional, Mammeri, Nadia El, additional, Noubhani, Abdelmajid, additional, Saupe, Sven, additional, Habenstein, Birgit, additional, Loquet, Antoine, additional, and Pintacuda, Guido, additional

Published
2016
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