Seeded fibrils of the germline variant of human lambda-III immunoglobulin light chain FOR005 have a similar core as patient fibrils with reduced stability

Erstveröffentlichung
2020
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Wissenschaftlicher Artikel


Authors
Pradhan, Tejaswini
Annamalai, Karthikeyan
Sarkar, Riddhiman
Huhn, Stefanie
Hegenbart, Ute
et al.
Faculties
Fakultät für Naturwissenschaften
Institutions
Institut für Proteinbiochemie
Published in
Journal of Biological Chemistry ; 295 (2020), 52. - S. 18474-18484. - ISSN 0021-9258. - eISSN 1083-351X
Link to publication
https://dx.doi.org/10.1074/jbc.RA120.016006
Keywords
AL amyloidosis · antibody light chain · protein aggregation · fibril seeding · Magic Angle Spinning (MAS) solid-state NMR spectroscopy; amyloid; antibody; protein aggregation; solid state NMR; nuclear magnetic resonance (NMR); PRIMARY SYSTEMIC AMYLOIDOSIS; CHEMICAL-SHIFT ASSIGNMENTS; SOLID-STATE NMR; CLINICAL PRESENTATION; AL AMYLOIDOSIS; B-CELL; A-BETA-42; DIMER; C-13; MUTATIONS
Dewey Decimal Group
DDC 570 / Life sciences
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