Disruption of the CD Loop by Enzymatic Cleavage Promotes the Formation of Toxic Transthyretin Oligomers through a Common Transthyretin Misfolding Pathway.
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
30 06 2020
30 06 2020
Historique:
pubmed:
6
6
2020
medline:
25
2
2021
entrez:
6
6
2020
Statut:
ppublish
Résumé
Amyloid formation of full-length TTR involves dissociation of the native tetramers into misfolded monomers that self-assemble into amyloid. In addition to the full-length TTR, C-terminal fragments including residues 49-127 were also observed
Identifiants
pubmed: 32500705
doi: 10.1021/acs.biochem.0c00079
pmc: PMC7339286
mid: NIHMS1605923
doi:
Substances chimiques
Amyloidogenic Proteins
0
Prealbumin
0
Trypsin
EC 3.4.21.4
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
2319-2327Subventions
Organisme : NIGMS NIH HHS
ID : P41 GM132079
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK046335
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS097490
Pays : United States
Organisme : NIH HHS
ID : S10 OD023513
Pays : United States
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