Structural and functional characterization of hMEX-3C Ring finger domain as an E3 ubiquitin ligase

about

Structural and functional characterization of hMEX-3C Ring finger domain as an E3 ubiquitin ligase

Item

http://www.wikidata.org/entity/Q58725200

description

im September 2018 veröffentlichter wissenschaftlicher Artikel

@de

wetenschappelijk artikel

@nl

наукова стаття, опублікована у вересні 2018

@uk

name

Structural and functional char ...... main as an E3 ubiquitin ligase

@en

Structural and functional char ...... main as an E3 ubiquitin ligase

@nl

type

Item

label

Structural and functional char ...... main as an E3 ubiquitin ligase

@en

Structural and functional char ...... main as an E3 ubiquitin ligase

@nl

prefLabel

Structural and functional char ...... main as an E3 ubiquitin ligase

@en

Structural and functional char ...... main as an E3 ubiquitin ligase

@nl

P1476

Structural and functional char ...... main as an E3 ubiquitin ligase

@en

P2093

Guodong Xie

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

Jihui Wu

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

Nshogoza Gilbert

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

Qingguo Gong

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

Sayed Ala Moududee

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

Yajun Tang

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

Yiyang Jiang

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

Yunyu Shi

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

Zheng Xu

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

P2860

RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination

The RNA-binding E3 ubiquitin ligase MEX-3C links ubiquitination with MHC-I mRNA degradation

Structure of a RING E3 trapped in action reveals ligation mechanism for the ubiquitin-like protein NEDD8

Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b

Identification and characterization of human Mex-3 proteins, a novel family of evolutionarily conserved RNA-binding proteins differentially localized to processing bodies

Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans

Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis

BIRC7–E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer

Activation of a primed RING E3-E2-ubiquitin complex by non-covalent ubiquitin

Mechanisms underlying ubiquitination

P304

1661-1669

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

P31

scholarly article

P356

10.1002/PRO.3473

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

P407

English

P433

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

P478

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

P577

2018-09-01T00:00:00Z

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

P698

30095198

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

P921

molecular biology

P932

6194269

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