Molecular interaction between the chaperone Hsc70 and the N-terminal flank of huntingtin exon 1 modulates aggregation
about
The struggle by Caenorhabditis elegans to maintain proteostasis during aging and diseaseAn Intein-based Strategy for the Production of Tag-free Huntingtin Exon 1 Proteins Enables New Insights into the Polyglutamine Dependence of Httex1 Aggregation and Fibril FormationFibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine coreSequestration of cellular interacting partners by protein aggregates: implication in a loss-of-function pathology.Folding Landscape of Mutant Huntingtin Exon1: Diffusible Multimers, Oligomers and Fibrils, and No Detectable Monomer.The emerging role of the first 17 amino acids of huntingtin in Huntington's diseaseα-Synuclein and huntingtin exon 1 amyloid fibrils bind laterally to the cellular membrane.Axonal transport and secretion of fibrillar forms of α-synuclein, Aβ42 peptide and HTTExon 1Nanoscale studies link amyloid maturity with polyglutamine diseases onset.Chaperones in Polyglutamine Aggregation: Beyond the Q-Stretch.DnaJ/Hsc70 chaperone complexes control the extracellular release of neurodegenerative-associated proteins.Endocytic vesicle rupture is a conserved mechanism of cellular invasion by amyloid proteins.Inhibition of polyglutamine aggregation by SIMILAR huntingtin N-terminal sequences: Prospective molecules for preclinical evaluation in Huntington's disease.Binding, internalization and fate of Huntingtin Exon1 fibrillar assemblies in mitotic and nonmitotic neuroblastoma cells.Proteins Containing Expanded Polyglutamine Tracts and Neurodegenerative Disease.Rapid α-oligomer formation mediated by the Aβ C terminus initiates an amyloid assembly pathway.Glyceraldehyde 3-phosphate dehydrogenase augments the intercellular transmission and toxicity of polyglutamine aggregates in a cell model of Huntington disease.HSP90 recognizes the N-terminus of huntingtin involved in regulation of huntingtin aggregation by USP19.Complete suppression of Htt fibrilization and disaggregation of Htt fibrils by a trimeric chaperone complex.
P2860
Q28069294-059B3753-C6BE-4EE8-A1D6-BD983A34FE48Q30385936-671CFD17-DE3B-4365-9857-5E07AB765054Q33761247-900D6A4A-B435-4329-9D88-9410E40F3BFBQ34519909-847E9810-5069-4854-B1A0-8FB0A4C9C9E1Q36043574-0F728CD6-3030-4112-9174-F50CE6131AFCQ36110838-768074A1-F91F-45FF-9FA5-BE0F5B410102Q36499643-5A9237BF-15C1-49D1-AEA2-175A6C262EB0Q36680329-61083952-B693-4940-ACD5-BE0B34846893Q37157361-0F18713D-EF67-4F46-83C0-6365EB78DFD3Q37716781-9AD8A5A9-C78C-43C5-8637-EAE5058A7CCEQ38766640-5B986AB4-C508-4F42-9B5C-F1DB23916301Q38773604-B30F04BE-CBCD-41FF-B88B-7ACCD0311102Q38838617-28273006-EADC-4510-BB92-7CC1BD62AB7EQ38860098-B7D1E63A-792D-47CA-8107-56E314269D93Q39124557-3A3A43B7-F89C-4182-BA8C-1B5E0CE7B8DAQ41230841-810C01A5-7AB6-459C-B6C9-2551971B7A58Q45291908-0E202BDA-94DA-4D20-A28E-19606DD60501Q47107288-A4BF4A30-36B3-44FD-AE98-79101A6D2042Q47322329-5C944096-246D-4A4B-9D10-E793E78D36CA
P2860
Molecular interaction between the chaperone Hsc70 and the N-terminal flank of huntingtin exon 1 modulates aggregation
description
2014 nî lūn-bûn
@nan
2014 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Molecular interaction between ...... n exon 1 modulates aggregation
@ast
Molecular interaction between ...... n exon 1 modulates aggregation
@en
type
label
Molecular interaction between ...... n exon 1 modulates aggregation
@ast
Molecular interaction between ...... n exon 1 modulates aggregation
@en
prefLabel
Molecular interaction between ...... n exon 1 modulates aggregation
@ast
Molecular interaction between ...... n exon 1 modulates aggregation
@en
P2093
P2860
P356
P1476
Molecular interaction between ...... n exon 1 modulates aggregation
@en
P2093
Gemma Ruiz-Arlandis
Luc Bousset
Ronald Melki
P2860
P304
P356
10.1074/JBC.M114.603332
P407
P577
2014-12-10T00:00:00Z