The interplay of Hrd3 and the molecular chaperone system ensures efficient degradation of malfolded secretory proteins.
about
DNAJs: more than substrate delivery to HSPADirect and essential function for Hrd3 in ER-associated degradation.Proteolytic regulation of metabolic enzymes by E3 ubiquitin ligase complexes: lessons from yeast.Glycosylation-directed quality control of protein folding.Kingdom Chromista and its eight phyla: a new synthesis emphasising periplastid protein targeting, cytoskeletal and periplastid evolution, and ancient divergences.
P2860
The interplay of Hrd3 and the molecular chaperone system ensures efficient degradation of malfolded secretory proteins.
description
2014 nî lūn-bûn
@nan
2014 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
The interplay of Hrd3 and the ...... malfolded secretory proteins.
@ast
The interplay of Hrd3 and the ...... malfolded secretory proteins.
@en
The interplay of Hrd3 and the ...... malfolded secretory proteins.
@nl
type
label
The interplay of Hrd3 and the ...... malfolded secretory proteins.
@ast
The interplay of Hrd3 and the ...... malfolded secretory proteins.
@en
The interplay of Hrd3 and the ...... malfolded secretory proteins.
@nl
prefLabel
The interplay of Hrd3 and the ...... malfolded secretory proteins.
@ast
The interplay of Hrd3 and the ...... malfolded secretory proteins.
@en
The interplay of Hrd3 and the ...... malfolded secretory proteins.
@nl
P2093
P2860
P356
P1476
The interplay of Hrd3 and the ...... f malfolded secretory proteins
@en
P2093
Franziska Sommermeyer
Maren Berger
Markus Aebi
Martin Mehnert
Robert Gauss
Sathish Kumar Lakshmipathy
Thomas Sommer
P2860
P304
P356
10.1091/MBC.E14-07-1202
P577
2014-11-26T00:00:00Z