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

Authors

Pradhan, Tejaswini

Annamalai, Karthikeyan

Sarkar, Riddhiman

Huhn, Stefanie

Hegenbart, Ute

et al.

Wissenschaftlicher Artikel

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

Faculties

Fakultät für Naturwissenschaften

Institutions

Institut für Proteinbiochemie

Subject headings

[Free subject headings]: AL amyloidosis &#183 | antibody light chain &#183 | protein aggregation &#183 | fibril seeding &#183 | 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
[DDC subject group]: DDC 570 / Life sciences

Metadata

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