Collagen I Weakly Interacts with the β-Sheets of β
Journal
Journal of the American Chemical Society
ISSN: 1520-5126
Titre abrégé: J Am Chem Soc
Pays: United States
ID NLM: 7503056
Informations de publication
Date de publication:
22 01 2020
22 01 2020
Historique:
pubmed:
26
12
2019
medline:
26
1
2021
entrez:
26
12
2019
Statut:
ppublish
Résumé
Amyloidogenesis is significant in both protein function and pathology. Amyloid formation of folded, globular proteins is commonly initiated by partial or complete unfolding. However, how this unfolding event is triggered for proteins that are otherwise stable in their native environments is not well understood. The accumulation of the immunoglobulin protein β
Identifiants
pubmed: 31875390
doi: 10.1021/jacs.9b10421
pmc: PMC7135851
doi:
Substances chimiques
Amyloid
0
Collagen Type I
0
beta 2-Microglobulin
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
1321-1331Subventions
Organisme : NIGMS NIH HHS
ID : P41 GM066354
Pays : United States
Organisme : Wellcome Trust
ID : 204963
Pays : United Kingdom
Organisme : NIGMS NIH HHS
ID : R01 GM045302
Pays : United States
Organisme : Wellcome Trust
ID : 092896
Pays : United Kingdom
Organisme : NIGMS NIH HHS
ID : P41 GM118302
Pays : United States
Organisme : American Heart Association-American Stroke Association
ID : 17POST33410326
Pays : United States
Organisme : NCRR NIH HHS
ID : C06 RR015495
Pays : United States
Organisme : Wellcome Trust
ID : 204963/Z/16/Z
Pays : United Kingdom
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