Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains - Test2 - elhamkhani - TriplyDB

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

http://www.wikidata.org/entity/Q27674961

about

Cleaning up in the endoplasmic reticulum: ubiquitin in charge A single MIU motif of MINDY-1 recognizes K48-linked polyubiquitin chains Efficient and generalized processing of multidimensional NUS NMR data: the NESTA algorithm and comparison of regularization terms.The ubiquitin-associated domain of cellular inhibitor of apoptosis proteins facilitates ubiquitylation gp78 elongates of polyubiquitin chains from the distal end through the cooperation of its G2BR and CUE domains Structural characterization of the late competence protein ComFB from Bacillus subtilis.Comparison of native and non-native ubiquitin oligomers reveals analogous structures and reactivities.A ubiquitin-dependent signalling axis specific for ALKBH-mediated DNA dealkylation repair.

P2860

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P2860

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

http://www.wikidata.org/entity/Q27674961

description

2012 nî lūn-bûn

@nan

2012 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

@ast

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

@en

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

@nl

type

label

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

@ast

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

@en

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

@nl

prefLabel

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

@ast

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

@en

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

@nl

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P356

J.STR.2012.09.020

P1433

P1476

Promiscuous interactions of gp78 E3 ligase CUE domain with polyubiquitin chains

@en

P2093

Aaren King

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

Allan M Weissman

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

Jess Li

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

Ranabir Das

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

Sergey Tarasov

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

Shan Liu

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

Tao Huang

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

Yinghua Chen

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

P2860

E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages

A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate

Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase

Recognition of the polyubiquitin proteolytic signal

Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction

The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site

Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series

Mechanism of ubiquitin recognition by the CUE domain of Vps9p

Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding

Allosteric Activation of E2-RING Finger-Mediated Ubiquitylation by a Structurally Defined Specific E2-Binding Region of gp78

P304

2138-2150

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

P31

scholarly article

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10.1016/J.STR.2012.09.020

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P433

12

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P478

20

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P50

P577

2012-11-01T00:00:00Z

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232811731

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P698

23123110

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

P921

structural biology

P932

3518592

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