Symmetry breaking during homodimeric assembly activates an E3 ubiquitin ligase - Wikidata - awgldk - TriplyDB

Symmetry breaking during homodimeric assembly activates an E3 ubiquitin ligase

Symmetry breaking during homodimeric assembly activates an E3 ubiquitin ligase

http://www.wikidata.org/entity/Q29994698

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Chaperone-directed ubiquitylation maintains proteostasis at the expense of longevity.

P2860

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P2860

Symmetry breaking during homodimeric assembly activates an E3 ubiquitin ligase

http://www.wikidata.org/entity/Q29994698

description

2017 nî lūn-bûn

@nan

2017 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2017 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2017年の論文

@ja

2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

@zh-tw

2017年论文

@wuu

name

Symmetry breaking during homodimeric assembly activates an E3 ubiquitin ligase

@ast

Symmetry breaking during homodimeric assembly activates an E3 ubiquitin ligase

@en

type

label

Symmetry breaking during homodimeric assembly activates an E3 ubiquitin ligase

@ast

Symmetry breaking during homodimeric assembly activates an E3 ubiquitin ligase

@en

prefLabel

Symmetry breaking during homodimeric assembly activates an E3 ubiquitin ligase

@ast

Symmetry breaking during homodimeric assembly activates an E3 ubiquitin ligase

@en

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S41598-017-01880-4

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Scientific Reports

P1476

Symmetry breaking during homodimeric assembly activates an E3 ubiquitin ligase

@en

P2093

Brandon L Garcia

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

Carlos J Camacho

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

Jeffrey L Brodsky

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

Patrick G Needham

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

Samuel K Estabrooks

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

Saurav Misra

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

Susan K Whitaker

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

Zhaofeng Ye

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

P2860

Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex

Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology

Hikeshi, a nuclear import carrier for Hsp70s, protects cells from heat shock-induced nuclear damage

CHIP-dependent termination of MEKK2 regulates temporal ERK activation required for proper hyperosmotic response

FastContact: a free energy scoring tool for protein-protein complex structures

Cell signaling by receptor tyrosine kinases

The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3

CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation

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s41598-017-01880-4

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1789

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scholarly article

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10.1038/S41598-017-01880-4

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1

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7

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2017-05-11T00:00:00Z

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1085347341

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28496195

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5431976

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