المؤلفون: Xinrui Gui, Shuang Feng, Zilong Li, Yanyan Li, Bernd Reif, Bingyang Shi, Zheng Niu

المصدر: Journal of Biological Chemistry. 299:102926

مصطلحات موضوعية: Cell Biology, Molecular Biology, Biochemistry

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_________::1a68c867cbde27ad198c6850439a660aTest
https://doi.org/10.1016/j.jbc.2023.102926Test

المؤلفون: Saba Suladze, Ayyalusamy Ramamoorthy, Christopher L. Souders, Zhou Deng, Bernd Reif, Toshio Ando, Bikash R. Sahoo, Christopher J. Martyniuk, Hunter Linton, Magdalena I. Ivanova, Takahiro Nakayama

المصدر: J Mol Biol

مصطلحات موضوعية: endocrine system, Amyloid, Maleic acid, Molecular Conformation, Amylin, macromolecular substances, Article, Fluorescence, Styrene, Styrenes, chemistry.chemical_compound, Protein Aggregates, Fibril formation, Structural Biology, Amphiphile, Spectroscopy, Fourier Transform Infrared, Copolymer, Animals, Humans, Computer Simulation, Molecular Biology, Zebrafish, Chemistry, Maleates, In vitro, Islet Amyloid Polypeptide, Diabetes Mellitus, Type 2, Biophysics, Hydrophobic and Hydrophilic Interactions

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15dc511ad520f1f1fdf4f8f556198f8fTest
https://europepmc.org/articles/PMC8752516Test/

المؤلفون: Michaela Aichler, Zheng Niu, Behrooz Hooshyar Yousefi, Hans-Jürgen Wester, Riddhiman Sarkar, Bernd Reif

المصدر: Chembiochem

مصطلحات موضوعية: Amyloid, positron emission tomography, 010402 general chemistry, Fibril, 01 natural sciences, Biochemistry, magic angle spinning solid-state NMR spectroscopy, chemistry.chemical_compound, Alzheimer Disease, Magic angle spinning, Molecule, Bovine serum albumin, Nuclear Magnetic Resonance, Biomolecular, Molecular Biology, Fluorescent Dyes, deuteration, Carbon Isotopes, amyloid-beta fibrils, Aniline Compounds, Binding Sites, Molecular Structure, Full Paper, biology, 010405 organic chemistry, Organic Chemistry, imaging tracer, Nuclear magnetic resonance spectroscopy, Full Papers, Alzheimer's disease, Small molecule, ddc, 0104 chemical sciences, Thiazoles, Solid-state nuclear magnetic resonance, chemistry, Positron-Emission Tomography, Biophysics, biology.protein, Molecular Medicine, Thioflavin

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de63a1af3e745fa651bc3ffae51d211cTest
https://doi.org/10.1002/cbic.202000143Test

المؤلفون: Matthias J. Brandl, Tejaswini Pradhan, Johannes Buchner, Gina Feind, Carolin Berner, Benedikt Weber, Bernd Reif, Maria Daniela Pulido Cendales, Martin Zacharias

المصدر: Journal of Biological Chemistry. 293:17107-17118

مصطلحات موضوعية: Protein Conformation, alpha-Helical, 0301 basic medicine, Amino Acid Motifs, Lysine, Immunoglobulin domain, Protein aggregation, Biochemistry, 03 medical and health sciences, chemistry.chemical_compound, Molecular dynamics, Protein Domains, Humans, Transition Temperature, Molecular Biology, Protein secondary structure, biology, Cell Biology, 030104 developmental biology, Monomer, chemistry, Immunoglobulin G, Protein Structure and Folding, Biophysics, biology.protein, Protein Conformation, beta-Strand, lipids (amino acids, peptides, and proteins), Protein folding, Immunoglobulin Domains, Antibody

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee4e744f62fedfcd0ca5690c5830597fTest
https://doi.org/10.1074/jbc.ra118.005475Test

المؤلفون: Stefanie Huhn, Marcus Fändrich, Bernd Reif, Ute Hegenbart, Riddhiman Sarkar, Tejaswini Pradhan, Stefan Schönland, Karthikeyan Annamalai

المصدر: The Journal of Biological Chemistry
J. Biol. Chem. 295, 18474-18484 (2020)

مصطلحات موضوعية: 0301 basic medicine, Models, Molecular, Amyloid, nuclear magnetic resonance (NMR), Sequence Homology, macromolecular substances, Protein aggregation, Fibril, Immunoglobulin light chain, Biochemistry, protein aggregation, 03 medical and health sciences, antibody, medicine, Humans, AL amyloidosis · antibody light chain · protein aggregation · fibril seeding · Magic Angle Spinning (MAS) solid-state NMR spectroscopy, Immunoglobulin Light-chain Amyloidosis, Amino Acid Sequence, Molecular Biology, Nuclear Magnetic Resonance, Biomolecular, solid state NMR, 030102 biochemistry & molecular biology, Chemistry, C-terminus, Amyloidosis, Point mutation, Cell Biology, Al Amyloidosis ·, Antibody Light Chain ·, Protein Aggregation ·, Fibril Seeding ·, Magic Angle Spinning (mas) Solid-state Nmr Spectroscopy, Antibody, Protein Aggregation, Solid State Nmr, Nuclear Magnetic Resonance (nmr), medicine.disease, 030104 developmental biology, Mutation, Protein Structure and Folding, Biophysics, Immunoglobulin Light Chains, Protein Conformation, beta-Strand, Salt bridge

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08beffb6b520e8806d11c3f5402b7a4cTest
https://pubmed.ncbi.nlm.nih.gov/33093170Test

المؤلفون: Philipp W. N. Schmid, Bernd Reif, Beate Rockel, Sam Asami, Juri Rappsilber, Martin Haslbeck, Carsten Peters, Martin Zacharias, Evgeny V. Mymrikov, Juan Zou, Maria Stavropoulou, Christoph J. O. Kaiser, Sevil Weinkauf, Johannes Buchner, Vinay Dahiya

المصدر: Kaiser, C J O, Peters, C, Schmid, P W N, Stavropoulou, M, Zou, J, Dahiya, V, Mymrikov, E V, Rockel, B, Asami, S, Haslbeck, M, Rappsilber, J, Reif, B, Zacharias, M, Buchner, J & Weinkauf, S 2019, ' The structure and oxidation of the eye lens chaperone αA-crystallin ', Nature Structural and Molecular Biology, vol. 26, no. 12, pp. 1141-1150 . https://doi.org/10.1038/s41594-019-0332-9Test
Nat. Struct. Mol. Biol. 26, 1141-1150 (2019)
Nature structural & molecular biology

مصطلحات موضوعية: Models, Molecular, Molecular model, Protein Conformation, Oligomer, alpha-Crystallin A Chain, Article, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Protein structure, Structural Biology, Crystallin, Heat shock protein, Lens, Crystalline, Humans, Molecular Biology, 030304 developmental biology, Protein Unfolding, 0303 health sciences, biology, Cryoelectron Microscopy, Nuclear magnetic resonance spectroscopy, eye diseases, chemistry, Chaperone (protein), Intramolecular force, biology.protein, Biophysics, sense organs, Protein Multimerization, Oxidation-Reduction, 030217 neurology & neurosurgery

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c4a3bc49d8b425998f5e56665a53e3fTest
https://www.pure.ed.ac.uk/ws/files/131168653/TheStructureAndOxidationOfTheEyesLensChaperone.pdfTest

المؤلفون: Andras Franko, Annette Feuchtinger, Helmut Fuchs, Bernd Reif, Hans-Ulrich Häring, Dirk Janik, Birgit Rathkolb, Annett Böddrich, Andreas Peter, Michaela Aichler, Andrés Camargo, Martin Hrabě de Angelis, Erich E. Wanker, Diana C. Rodriguez Camargo, Divita Garg, Frauke Neff

المصدر: Scientific Reports
Sci. Rep. 8:1116 (2018)
Scientific Reports, Vol 8, Iss 1, Pp 1-12 (2018)

مصطلحات موضوعية: 0301 basic medicine, Genetically modified mouse, Models, Molecular, Amyloid, Molecular Conformation, lcsh:Medicine, Mice, Transgenic, macromolecular substances, Epigallocatechin gallate, Fibril, complex mixtures, Article, Catechin, 03 medical and health sciences, chemistry.chemical_compound, Mice, In vivo, mental disorders, medicine, Animals, Humans, lcsh:Science, Pancreas, geography, Multidisciplinary, geography.geographical_feature_category, 030102 biochemistry & molecular biology, Pancreatic islets, lcsh:R, food and beverages, Amyloidosis, Islet, Molecular biology, In vitro, Islet Amyloid Polypeptide, 030104 developmental biology, medicine.anatomical_structure, Neuroprotective Agents, chemistry, lcsh:Q, Function and Dysfunction of the Nervous System, Biomarkers, Protein Binding

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44f517b968dc34ff8cd71111b568fd06Test
http://edoc.mdc-berlin.de/17048/1/17048oa.pdfTest

المؤلفون: Johannes Buchner, Manuel Hora, Carlo Camilloni, Pamina Kazman, Christoph Göbl, Bernd Reif, Benedikt Weber

المصدر: J. Mol. Biol. 430, 4925-4940 (2018)

مصطلحات موضوعية: Models, Molecular, 0301 basic medicine, Amyloid, Protein Conformation, Proteolysis, Arginine, Immunoglobulin light chain, Fibril, Antibody Folding, Protein Stability, Light Chain Linker, Intramolecular Interactions, Protein Aggregation, Pathological, 03 medical and health sciences, Residue (chemistry), Amyloid disease, Protein Domains, Structural Biology, medicine, Humans, Nuclear Magnetic Resonance, Biomolecular, Molecular Biology, Binding Sites, 030102 biochemistry & molecular biology, medicine.diagnostic_test, Chemistry, 030104 developmental biology, Residual dipolar coupling, Mutation, Biophysics, Immunoglobulin Light Chains, Linker

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8a266856d366d146ff587a41c6b5124Test
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=54713Test

المؤلفون: Muralidhar Dasari, Erich E. Wanker, Bernd Reif, Jan Bieschke, Juan Miguel López del Amo, Gerlinde Grelle, Uwe Fink

المصدر: Journal of Molecular Biology. 421:517-524

مصطلحات موضوعية: Protein Denaturation, Magnetic Resonance Spectroscopy, Amyloid, Protein Conformation, Peptide, complex mixtures, Catechin, Protein structure, Alzheimer Disease, Structural Biology, medicine, Magic angle spinning, Humans, Molecular Biology, chemistry.chemical_classification, Amyloid beta-Peptides, Chemistry, Neurotoxicity, P3 peptide, food and beverages, Nuclear magnetic resonance spectroscopy, medicine.disease, Neuroprotective Agents, Biochemistry, Biophysics, Salt bridge, Protein Multimerization

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9372618fa176649cba486529fcfad13Test
https://doi.org/10.1016/j.jmb.2012.01.013Test

المؤلفون: Maria Stavropoulou, Carsten Peters, Andi Mainz, Jirka Peschek, Johannes Buchner, Katrin C. Back, Bernd Reif, Sevil Weinkauf, Elke Prade, Benjamin Bardiaux, Sam Asami

المساهمون: Department of Chemistry [Munich], Technische Universität Munchen - Université Technique de Munich [Munich, Allemagne] (TUM), Leibniz Forschungsinstitut für Molekulare Pharmakolgie = Leibniz Institute for Molecular Pharmacology [Berlin, Allemagne] (FMP), Leibniz Association, Bioinformatique structurale - Structural Bioinformatics, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Helmholtz-Zentrum München (HZM), This work was performed in the framework of the SFB-1035 (project B07 to B.R. and project A06 to J.B. and S.W., German Research Foundation (DFG)). We acknowledge support from the Helmholtz-Gemeinschaft and the DFG (grant Re1435 to B.R.). We are grateful to the Center for Integrated Protein Science Munich for financial support. J.P. acknowledges support from the Studienstiftung des deutschen Volkes., We are grateful to H. Oschkinat, S. Markovic and J. Muenckemer for stimulating discussions on the project. We also thank M. Ringling, H. Stephanowitz and A. Nieuwkoop for technical support with the EM, MS and fast MAS NMR experiments, respectively., Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Helmholtz Zentrum München = German Research Center for Environmental Health

المصدر: Nature Structural and Molecular Biology
Nature Structural and Molecular Biology, Nature Publishing Group, 2015, pp.898-905. ⟨10.1038/nsmb.3108⟩
Nature Structural and Molecular Biology, 2015, pp.898-905. ⟨10.1038/nsmb.3108⟩

مصطلحات موضوعية: Models, Molecular, Amyloid, Magnetic Resonance Spectroscopy, Protein Conformation, MESH: alpha-Crystallin B Chain, Peptide, Plasma protein binding, Protein aggregation, Models, Biological, 03 medical and health sciences, Protein structure, MESH: Protein Conformation, Structural Biology, Humans, MESH: Protein Binding, Molecular Biology, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, MESH: Amyloid, MESH: Humans, biology, MESH: Magnetic Resonance Spectroscopy, αb crystallin, 030302 biochemistry & molecular biology, An amyloid, MESH: Models, Biological, alpha-Crystallin B Chain, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Interaction studies, chemistry, Biochemistry, Chaperone (protein), Chaperone αB-crystallin, Structural plasticity, Amorphous, biology.protein, Biophysics, MESH: Models, Molecular, Protein Binding

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::378e5d41025faab2460349f7e2e1bb5cTest
https://hal-pasteur.archives-ouvertes.fr/pasteur-01400959Test