المؤلفون: Thomas Heerde, Matthies Rennegarbe, Alexander Biedermann, Dilan Savran, Peter B. Pfeiffer, Manuel Hitzenberger, Julian Baur, Ioana Puscalau-Girtu, Martin Zacharias, Nadine Schwierz, Christian Haupt, Matthias Schmidt, Marcus Fändrich

المصدر: Nature Communications
Nature Communications, Vol 13, Iss 1, Pp 1-8 (2022)

مصطلحات موضوعية: DDC 540 / Chemistry & allied sciences, Amyloid, Prions, Protein Conformation, Science, Genetic Vectors, General Physics and Astronomy, Gene Expression, Mice, Transgenic, macromolecular substances, Molecular Dynamics Simulation, General Biochemistry, Genetics and Molecular Biology, Article, Mice, DDC 570 / Life sciences, Cryoelectron microscopy, ddc:570, Escherichia coli, Animals, Humans, Protein Isoforms, ddc:530, Cloning, Molecular, Serum Amyloid A Protein, Multidisciplinary, Protein Stability, Cryoelectron Microscopy, food and beverages, General Chemistry, Amyloidosis, Molecular conformation, Recombinant Proteins, ddc:540, Proteolysis, Prion, Protein aggregation, Endopeptidase K

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29953e768386712fcd255c923e97f72fTest
http://europepmc.org/articles/PMC8748726Test

المؤلفون: Sara Karimi-Farsijani, Stefanie Huhn, Marcus Fändrich, Lynn Radamaker, Julian David Baur, Giada Andreotti, Paul Walther, Matthias Neumann, Sarah Schreiner, Volker Schmidt, Clarissa Read, Matthias Schmidt, Ute Hegenbart, Christian Haupt, Stefan Schönland, Raoul Motika, Sebastian Wiese, Natalie Berghaus

المصدر: Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)

مصطلحات موضوعية: INVOLVEMENT, Protein Folding, Glycosylation, PREDICTION, Protein Conformation, General Physics and Astronomy, Protein aggregation, Aggregation (Chemistry), Immunoglobulin light-chain amyloidosis, chemistry.chemical_compound, DDC 570 / Life sciences, FIBRILS, Cryoelectron microscopy, Immunoglobulin Light-chain Amyloidosis, Multidisciplinary, Strukturbiologie, Immunglobuline, lipids (amino acids, peptides, and proteins), Structural biology, GERMLINE GENE, Amyloid, Science, Somatic hypermutation, Immunoglobulins, macromolecular substances, Fibril, Immunoglobulin light chain, DEPOSITS, General Biochemistry, Genetics and Molecular Biology, Article, ddc:570, AL amyloidosis, medicine, ddc:610, LAMBDA-III, Immunoglobulin light chains, General Chemistry, Amyloidose, medicine.disease, carbohydrates (lipids), chemistry, Mutation, Biophysics, VISUALIZATION, Cryoelectron tomography, DDC 610 / Medicine & health

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebd3e500479b0af12a5673f1585a4e06Test
https://pubmed.ncbi.nlm.nih.gov/34741031Test

المؤلفون: Stefan Schönland, Matthias Schmidt, Akanksha Bansal, Ute Hegenbart, Marcus Fändrich, Christian Haupt, Julian David Baur, Lynn Radamaker, Stefanie Huhn

المصدر: Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)

مصطلحات موضوعية: Amyloid, Cryo-electron microscopy, Protein Conformation, Science, Sequence (biology), macromolecular substances, Immunoglobulin light chain, Fibril, Article, Protein Aggregates, Variable domain, AL amyloidosis, medicine, Humans, Immunoglobulin Light-chain Amyloidosis, Amino Acid Sequence, Chemistry, Cryoelectron Microscopy, Middle Aged, Amyloid fibril, medicine.disease, Mutation, Biophysics, Fatal disease, Female, Immunoglobulin Light Chains, Protein aggregation, Structural biology

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3e1bec955e12e28b5adc33371c1b5abTest
https://pubmed.ncbi.nlm.nih.gov/33558536Test