HSP90 recognizes the N-terminus of huntingtin involved in regulation of huntingtin aggregation by USP19.

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When nature's robots go rogue: exploring protein homeostasis dysfunction and the implications for understanding human aging disease pathologies.Proteostasis in Huntington's disease: disease mechanisms and therapeutic opportunities.

P2860

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HSP90 recognizes the N-terminus of huntingtin involved in regulation of huntingtin aggregation by USP19.

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http://www.wikidata.org/entity/Q47107288

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

HSP90 recognizes the N-terminu ...... ntingtin aggregation by USP19.

@en

HSP90 recognizes the N-terminu ...... ntingtin aggregation by USP19.

@nl

type

Item

label

HSP90 recognizes the N-terminu ...... ntingtin aggregation by USP19.

@en

HSP90 recognizes the N-terminu ...... ntingtin aggregation by USP19.

@nl

prefLabel

HSP90 recognizes the N-terminu ...... ntingtin aggregation by USP19.

@en

HSP90 recognizes the N-terminu ...... ntingtin aggregation by USP19.

@nl

P1476

HSP90 recognizes the N-terminu ...... untingtin aggregation by USP19

@en

P2093

Hong-Wei Yue

http://www.w3.org/2001/XMLSchema#string

Hong-Yu Hu

http://www.w3.org/2001/XMLSchema#string

Jun-Ye Hong

http://www.w3.org/2001/XMLSchema#string

Lei-Lei Jiang

http://www.w3.org/2001/XMLSchema#string

Wei Xue

http://www.w3.org/2001/XMLSchema#string

Wen-Tian He

http://www.w3.org/2001/XMLSchema#string

P2860

Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition

Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family

Interaction with synphilin-1 promotes inclusion formation of alpha-synuclein: mechanistic insights and pathological implication

TDP-35 sequesters TDP-43 into cytoplasmic inclusions through binding with RNA

Hsp90-Tau complex reveals molecular basis for specificity in chaperone action

Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases

Huntington's disease: underlying molecular mechanisms and emerging concepts

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

Secondary Structure of Huntingtin Amino-Terminal Region

Beta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residues

P2888

s41598-017-13711-7

P304

14797

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P31

scholarly article

P356

10.1038/S41598-017-13711-7

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English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Yongguang Gao

P577

2017-11-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

29093475

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P932

5666004

http://www.w3.org/2001/XMLSchema#string

HSP90 recognizes the N-terminus of huntingtin involved in regulation of huntingtin aggregation by USP19.

about

P2860

P2860

HSP90 recognizes the N-terminus of huntingtin involved in regulation of huntingtin aggregation by USP19.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932