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The Grp170 nucleotide exchange factor executes a key role during ERAD of cellular misfolded clients

publicat în: Molecular Biology of the Cell

Data de publicare: 2016-03-30

Citează articole 43

Dată

Title

Autori

2015-04-15

The nucleotide exchange factors Grp170 and Sil1 induce cholera toxin release from BiP to enable retrotranslocation
2015-04-10

BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions

Matthias J Feige
2015-02-04

A nucleotide exchange factor promotes endoplasmic reticulum-to-cytosol membrane penetration of the nonenveloped virus simian virus 40.
2014-09-11

Key steps in ERAD of luminal ER proteins reconstituted with purified components

Tom Rapoport, Alexander Stein, Pedro Carvalho
2014-07-23

The co-chaperone and reductase ERdj5 facilitates rod opsin biogenesis and quality control

Takao Iwawaki, Paul Chapple, Michael E. Cheetham
2014-04-01

Cleaning up in the endoplasmic reticulum: ubiquitin in charge

John C Christianson
2014-03-01

Quality control: ER-associated degradation: protein quality control and beyond

Ombretta Foresti, Pedro Carvalho
2013-12-10

The large Hsp70 Grp170 binds to unfolded protein substrates in vivo with a regulation distinct from conventional Hsp70s
2013-05-03

The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channel
2013-01-30

The ERdj5-Sel1L complex facilitates cholera toxin retrotranslocation
2013-09-01

The mammalian endoplasmic reticulum-associated degradation system
2013-08-21

Glycosylation-independent ERAD pathway serves as a backup system under ER stress
2012-12-01

Cleaning up: ER-associated degradation to the rescue
2012-03-09

ERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family protein that interacts with ER-associated degradation machinery

Erik Lee Snapp
2012-01

Defining human ERAD networks through an integrative mapping strategy

James Olzmann
2011-11-25

Road to ruin: targeting proteins for degradation in the endoplasmic reticulum

Hidde Ploegh
2011-11-03

Protein quality control in the ER: balancing the ubiquitin checkbook

Hidde Ploegh
2011-08-15

Structural and functional interactions between the cholera toxin A1 subunit and ERdj3/HEDJ, a chaperone of the endoplasmic reticulum
2011-02-18

Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5

Kazuhiro Nagata
2011-08-20

SEL1L is required for endoplasmic reticulum-associated degradation of misfolded luminal proteins but not transmembrane proteins in chicken DT40 cell line
2010-11-12

Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p

Tom Rapoport, Pedro Carvalho
2010-08-01

The HSP70 chaperone machinery: J proteins as drivers of functional specificity

Harm H Kampinga
2010-01-01

Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates
2009-11-13

Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo.
2009-04-03

Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans

Koichi Kato, Kazuhiro Nagata
2009-03-01

The ubiquitylation machinery of the endoplasmic reticulum
2008-11-05

Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3

David Ron
2008-11-05

Regulated release of ERdj3 from unfolded proteins by BiP
2008-07-25

Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP

Tatsuya Moriyama, Ikuo Wada, Kazuhiro Nagata
2008-06

ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C
2008-03

OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
2007-09-10

The heat shock protein 70 molecular chaperone network in the pancreatic endoplasmic reticulum - a quantitative approach

Articol - wd:Q36896318

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