Role of domain interactions in the aggregation of full-length immunoglobulin light chains.
antibody light-chain domains
light-chain amyloidosis
protein aggregation
proteinopathy
solution NMR spectroscopy
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
15 01 2019
15 01 2019
Historique:
pubmed:
2
1
2019
medline:
14
3
2019
entrez:
2
1
2019
Statut:
ppublish
Résumé
Amyloid light-chain (LC) amyloidosis is a protein misfolding disease in which the aggregation of an overexpressed antibody LC from a clonal plasma cell leads to organ toxicity and patient death if left untreated. While the overall dimeric architecture of LC molecules is established, with each LC composed of variable (V
Identifiants
pubmed: 30598439
pii: 1817538116
doi: 10.1073/pnas.1817538116
pmc: PMC6338840
doi:
Substances chimiques
Immunoglobulin Light Chains
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
854-863Subventions
Organisme : NIDDK NIH HHS
ID : R01 DK046335
Pays : United States
Organisme : NIDDK NIH HHS
ID : R37 DK046335
Pays : United States
Organisme : Canadian Institutes of Health Research
Pays : International
Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
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