The BRICHOS domain, amyloid fibril formation, and their relationship.
about
Transient dynamics of Aβ contribute to toxicity in Alzheimer's diseasePotentiation of neurotoxicity in double-mutant mice with Pink1 ablation and A53T-SNCA overexpression.Itm2a, a target gene of GATA-3, plays a minimal role in regulating the development and function of T cellsSpecific chaperones and regulatory domains in control of amyloid formation.The chaperone domain BRICHOS prevents CNS toxicity of amyloid-β peptide in Drosophila melanogasterA molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomersRNA-seq analysis of lung adenocarcinomas reveals different gene expression profiles between smoking and nonsmoking patients.The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation.Current and future treatment of amyloid diseases.The activities of amyloids from a structural perspective.Transthyretin and BRICHOS: The Paradox of Amyloidogenic Proteins with Anti-Amyloidogenic Activity for Aβ in the Central Nervous System.Antagonistic evolution of an antibiotic and its molecular chaperone: how to maintain a vital ectosymbiosis in a highly fluctuating habitat.Pseudocatalytic Antiaggregation Activity of Antibodies: Immunoglobulins can Influence α-Synuclein Aggregation at Substoichiometric Concentrations.Modulating the Effects of the Bacterial Chaperonin GroEL on Fibrillogenic Polypeptides through Modification of Domain Hinge Architecture.BRICHOS domain of Bri2 inhibits islet amyloid polypeptide (IAPP) fibril formation and toxicity in human beta cells.Caenorhabditis elegans BRICHOS Domain-Containing Protein C09F5.1 Maintains Thermotolerance and Decreases Cytotoxicity of Aβ42 by Activating the UPR.
P2860
Q26827421-D13ED535-D33D-4568-9A89-48B15A0EC5FFQ27301199-206A9796-633E-49C8-8055-B84ECFA58B9BQ28506017-9D30D205-56F0-4FB9-ABE3-16D0074B3102Q30378979-53BEB557-6BCE-403E-88C1-F2D17D397EE0Q33677217-332242C3-3697-4B4E-9CFB-CC8556B79042Q36129561-B5B8E3F5-7FE1-4C78-BAC7-47A158FFADFBQ36359897-F58F5B22-152B-4531-A92F-FF152F0E666AQ38240692-D4627C99-CD37-40DC-A3F5-80FC163A74AAQ38831388-645FD50D-DC06-4948-B9FA-D59D62C5D295Q39004351-7319C7A2-923F-4E8C-824E-0FDD9723FDEAQ39209937-9E4D1AA8-55FA-4329-9A9B-904C3D8345E9Q40227488-91067704-562D-4045-B885-94CBC36A861CQ48251459-E93068F8-C15A-4699-A6FE-8AE7BD2A468EQ51138141-20CE529E-F805-496B-95D1-FD7F339698E7Q51744166-F0A38672-107F-4739-B78C-331FD8FD38CBQ55261151-AD155CB0-6C20-48A1-9863-E1E16F818316
P2860
The BRICHOS domain, amyloid fibril formation, and their relationship.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年学术文章
@wuu
2013年学术文章
@zh-cn
2013年学术文章
@zh-hans
2013年学术文章
@zh-my
2013年学术文章
@zh-sg
2013年學術文章
@yue
2013年學術文章
@zh
2013年學術文章
@zh-hant
name
The BRICHOS domain, amyloid fibril formation, and their relationship.
@en
The BRICHOS domain, amyloid fibril formation, and their relationship.
@nl
type
label
The BRICHOS domain, amyloid fibril formation, and their relationship.
@en
The BRICHOS domain, amyloid fibril formation, and their relationship.
@nl
prefLabel
The BRICHOS domain, amyloid fibril formation, and their relationship.
@en
The BRICHOS domain, amyloid fibril formation, and their relationship.
@nl
P50
P356
P1433
P1476
The BRICHOS domain, amyloid fibril formation, and their relationship.
@en
P304
P356
10.1021/BI400908X
P407
P577
2013-10-17T00:00:00Z