Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.

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SCFFBXO17 E3 ligase modulates inflammation by regulating proteasomal degradation of glycogen synthase kinase-3β in lung epithelia.

P2860

Q38712145-0016BECA-80ED-4EE8-AE8A-7480C29DD38D

P2860

Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.

Item

http://www.wikidata.org/entity/Q36074198

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2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.

@ast

Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.

@en

type

Item

label

Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.

@ast

Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.

@en

prefLabel

Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.

@ast

Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.

@en

P1476

Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.

@en

P2093

Eden L Reichard

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

Giavanna G Chirico

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

Katelyn E Bard

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

Nicholas D Nassif

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

Nickolas E Millas

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

William J Dewey

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

P2860

Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate

Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for Cul3, targets Keap1 for degradation by a proteasome-independent pathway

Variably modulated gating of the 26S proteasome by ATP and polyubiquitin

Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex.

Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome

Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation

Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11

Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation

Protein production by auto-induction in high density shaking cultures

Multiple associated proteins regulate proteasome structure and function.

P304

18547-18561

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

P31

scholarly article

P356

10.1074/JBC.M116.720151

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

P407

English

P433

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

P478

291

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

P50

Daniel A Kraut

P577

2016-07-12T00:00:00Z

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

P698

27405762

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

P921

protein ubiquitination

P932

5000099

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

Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.

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P2860

P2860

Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.

description

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type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932