Crystal structure of 6aJL2-R24G light chain variable domain: Does crystal packing explain amyloid fibril formation?
Abstract
Light chain amyloidosis is one of the most common systemic amyloidosis, characterized by the deposition of immunoglobulin light variable domain as insoluble amyloid fibrils in vital organs, leading to the death of patients. Germline λ6a is closely related with this disease and has been reported that 25% of proteins encoded by this germline have a change at position 24 where an Arg is replaced by a Gly (R24G). This germline variant reduces...
Paper Details
Title
Crystal structure of 6aJL2-R24G light chain variable domain: Does crystal packing explain amyloid fibril formation?
Published Date
Dec 1, 2019
Volume
20
Pages
100682 - 100682
Citation AnalysisPro
You’ll need to upgrade your plan to Pro
Looking to understand the true influence of a researcher’s work across journals & affiliations?
- Scinapse’s Top 10 Citation Journals & Affiliations graph reveals the quality and authenticity of citations received by a paper.
- Discover whether citations have been inflated due to self-citations, or if citations include institutional bias.
Notes
History