المؤلفون: Kai Xue, Riddhiman Sarkar, Carina Motz, Sam Asami, Diana C. Rodriguez Camargo, Venita Decker, Sebastian Wegner, Zdenek Tosner, Bernd Reif

المصدر: Scientific Reports, Vol 7, Iss 1, Pp 1-7 (2017)

مصطلحات موضوعية: Medicine, Science

وصف الملف: electronic resource

العلاقة: https://doaj.org/toc/2045-2322Test

الوصول الحر: https://doaj.org/article/d086e727126b43d6b7851cd83e778236Test

المؤلفون: Diana C Rodriguez Camargo, Kyle J Korshavn, Alexander Jussupow, Kolio Raltchev, David Goricanec, Markus Fleisch, Riddhiman Sarkar, Kai Xue, Michaela Aichler, Gabriele Mettenleiter, Axel Karl Walch, Carlo Camilloni, Franz Hagn, Bernd Reif, Ayyalusamy Ramamoorthy

المصدر: eLife, Vol 6 (2017)

مصطلحات موضوعية: membrane, Amyloid peptide, Structure, NMR, Medicine, Science, Biology (General), QH301-705.5

وصف الملف: electronic resource

العلاقة: https://elifesciences.org/articles/31226Test; https://doaj.org/toc/2050-084XTest

الوصول الحر: https://doaj.org/article/83e9a3672fef478bbca4e26152d644a1Test

المؤلفون: Manuel Hora, Riddhiman Sarkar, Vanessa Morris, Kai Xue, Elke Prade, Emma Harding, Johannes Buchner, Bernd Reif

المصدر: PLoS ONE, Vol 12, Iss 7, p e0181799 (2017)

مصطلحات موضوعية: Medicine, Science

وصف الملف: electronic resource

العلاقة: http://europepmc.org/articles/PMC5528828?pdf=renderTest; https://doaj.org/toc/1932-6203Test

الوصول الحر: https://doaj.org/article/8385323faf984c73a88bfdb03891255dTest

المؤلفون: Jonathan Schönfelder (11217173), Peter Benedikt Pfeiffer (11217176), Tejaswini Pradhan (11217179), Johan Bijzet (478976), Bouke P. C. Hazenberg (8041688), Stefan O. Schönland (8888558), Ute Hegenbart (5538473), Bernd Reif (1262229), Christian Haupt (11217182), Marcus Fändrich (54216)

مصطلحات موضوعية: Biophysics, Biochemistry, Medicine, Cell Biology, Neuroscience, Ecology, Immunology, Developmental Biology, Cancer, Computational Biology, Chemical Sciences not elsewhere classified, Amyloid structure, prion, protein misfolding, proteolytic stability, immunoglobulin light chain, transthyretin, serum amyloid A

العلاقة: https://figshare.com/articles/journal_contribution/Protease_resistance_of_i_ex_vivo_i_amyloid_fibrils_implies_the_proteolytic_selection_of_disease-associated_fibril_morphologies/15090326Test

الإتاحة: https://doi.org/10.6084/m9.figshare.15090326.v1Test

المؤلفون: Bouke P. C. Hazenberg, Stefan Schoenland, Bernd Reif, Tejaswini Pradhan, Christian Haupt, M. Faendrich, J. Schoenfelder, Johan Bijzet, Ute Hegenbart, P. B. Pfeiffer

المساهمون: Translational Immunology Groningen (TRIGR)

المصدر: Amyloid, 28(4), 243-251. Taylor & Francis Ltd

مصطلحات موضوعية: PROTEINS, medicine.medical_treatment, proteolytic stability, macromolecular substances, Fibril, prion, Amyloid disease, Internal Medicine, medicine, Serum amyloid A, protein misfolding, immunoglobulin light chain, GLYCOSAMINOGLYCANS, chemistry.chemical_classification, Protease, biology, Chemistry, serum amyloid A, Amyloid fibril, TRANSTHYRETIN, In vitro, POLYMORPHISM, Amino acid, Transthyretin, Amyloid structure, biology.protein, Biophysics, Protein folding, Ex vivo

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e229dee1268b3cc10a97beb6344d5b95Test
https://doi.org/10.1080/13506129.2021.1960501Test

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

المصدر: Biomol. NMR Assign. 15, 9-16 (2021)
Biomolecular Nmr Assignments

مصطلحات موضوعية: Amyloid, Protein Folding, Complementarity determining region, macromolecular substances, 010402 general chemistry, Fibril, Immunoglobulin light chain, 01 natural sciences, Biochemistry, Article, 03 medical and health sciences, Structural Biology, medicine, AL amyloidosis, Humans, Amino Acid Sequence, Protein secondary structure, Nuclear Magnetic Resonance, Biomolecular, 030304 developmental biology, Solid state NMR, 0303 health sciences, Chemistry, Amyloidosis, Protein primary structure, medicine.disease, ddc, 0104 chemical sciences, Variable light chain fibrils, Biophysics, Immunoglobulin Light Chains, Al Amyloidosis, Variable Light Chain Fibrils, Solid State Nmr

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3ac7968014d16059c2f5e6f14725858Test
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=60078Test

المؤلفون: S. Schoenland, Bernd Reif, Stefanie Huhn, Riddhiman Sarkar, Tejaswini Pradhan, Ute Hegenbart, Karthikeyan Annamalai, M. Faendrich

مصطلحات موضوعية: Mutation, Chemistry, Amyloidosis, Point mutation, macromolecular substances, medicine.disease, Fibril, Immunoglobulin light chain, medicine.disease_cause, law.invention, Protein sequencing, law, Recombinant DNA, Biophysics, medicine, Salt bridge

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_________::c2a3b7706ea96f74df41edf9b84e5249Test
https://doi.org/10.1101/2020.10.02.323303Test

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: Vanessa K. Morris, Christoph Göbl, Laura Liesinger, Harmjan R. Vos, Tobias B. Dansen, Manuel Hora, Paulien E. Polderman, Bernd Reif, Christoph Hartlmueller, Ruth Birner-Gruenberger, Tobias Madl, Marieke Visscher, Hesther de Ruiter, Loes van Dam

المصدر: Redox Biology, Vol 28, Iss, Pp-(2020)
Redox Biology
Redox Biol. 28:101316 (2020)

مصطلحات موضوعية: 0301 basic medicine, Models, Molecular, Cell cycle checkpoint, Redox signaling, Clinical Biochemistry, Protein aggregation, medicine.disease_cause, Biochemistry, Protein Structure, Secondary, law.invention, 0302 clinical medicine, law, Amyloids, Cysteine oxidation, lcsh:QH301-705.5, Cellular Senescence, chemistry.chemical_classification, Protein Aggregation, Redox Signaling, Cysteine Oxidation, Structural Biology, 0303 health sciences, lcsh:R5-920, biology, integumentary system, Chemistry, 030302 biochemistry & molecular biology, Cell Cycle, ddc, biological phenomena, cell phenomena, and immunity, Structural biology, lcsh:Medicine (General), Oxidation-Reduction, Research Paper, Senescence, Amyloid, 03 medical and health sciences, medicine, Humans, Cysteine, neoplasms, Cyclin-Dependent Kinase Inhibitor p16, 030304 developmental biology, Reactive oxygen species, Cyclin-dependent kinase 4, Organic Chemistry, 030104 developmental biology, HEK293 Cells, lcsh:Biology (General), biology.protein, Biophysics, Suppressor, Protein Multimerization, 030217 neurology & neurosurgery, Oxidative stress, Function (biology)

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b0c192bc880623b2c14023c5a1b1886Test
http://www.sciencedirect.com/science/article/pii/S2213231719307918Test

المؤلفون: Aphrodite Kapurniotu, Ana C. Messias, Matthias J. Feige, Zheng Niu, Bernd Reif, Yonatan G. Mideksa, Chen Qian, Li-Mei Yan, Carlo Camilloni, Markus Fleisch, Don C. Lamb, Alexander Jussupow, Elke Prade, Michael Sattler, Kathleen Hille, Eleni Malideli, Riddhiman Sarkar

المصدر: Angewandte Chemie (International Ed. in English)
Adv. Mater. 59, 5820-5830 (2020)
Angew. Chem.-Int. Edit. 59, 2-13 (2020)

مصطلحات موضوعية: Amyloid, Peptide, amyloid formation, Molecular Dynamics Simulation, 010402 general chemistry, 01 natural sciences, Catalysis, Fluorescence spectroscopy, Substrate Specificity, medicine, Molecule, ddc:630, Amino Acid Sequence, Nuclear Magnetic Resonance, Biomolecular, solid-state NMR spectroscopy, Research Articles, Aβ, chemistry.chemical_classification, Amyloid-bildung, Amyloid-inhibitoren, Festkörper-nmr-spektroskopie, Amyloid beta-Peptides, 010405 organic chemistry, Chemistry, Amyloid Formation, Amyloid Inhibitors, A Beta, Solid-state Nmr Spectroscopy, Peptides, General Medicine, General Chemistry, Nuclear magnetic resonance spectroscopy, Peptide Fragments, 0104 chemical sciences, ddc, Islet Amyloid Polypeptide, Mechanism of action, Microscopy, Fluorescence, Biophysics, peptides, Aβ amyloid, medicine.symptom, Function (biology), Research Article

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e5bac7e5a286d7746d16df0f3a9ae13Test
https://pubmed.ncbi.nlm.nih.gov/31863711Test