The lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity.
about
Selective activators of protein phosphatase 5 target the auto-inhibitory mechanism.The balanced regulation of Hsc70 by DNJ-13 and UNC-23 is required for muscle functionality.Two-Dimensional Gel Electrophoresis-Based Proteomic Analysis Reveals N-terminal Truncation of the Hsc70 Protein in Cotton Fibers In VivoNovel Entropically Driven Conformation-specific Interactions with Tomm34 Protein Modulate Hsp70 Protein Folding and ATPase Activities.Target profiling of 4-hydroxyderricin in S. aureus reveals seryl-tRNA synthetase binding and inhibition by covalent modification.
P2860
The lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity.
description
2012 nî lūn-bûn
@nan
2012 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մարտին 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
The lid domain of Caenorhabdit ...... and protein folding activity.
@ast
The lid domain of Caenorhabdit ...... and protein folding activity.
@en
The lid domain of Caenorhabdit ...... and protein folding activity.
@nl
type
label
The lid domain of Caenorhabdit ...... and protein folding activity.
@ast
The lid domain of Caenorhabdit ...... and protein folding activity.
@en
The lid domain of Caenorhabdit ...... and protein folding activity.
@nl
prefLabel
The lid domain of Caenorhabdit ...... and protein folding activity.
@ast
The lid domain of Caenorhabdit ...... and protein folding activity.
@en
The lid domain of Caenorhabdit ...... and protein folding activity.
@nl
P2860
P50
P1433
P1476
The lid domain of Caenorhabdit ...... g and protein folding activity
@en
P2093
Andreas M Gaiser
P2860
P304
P356
10.1371/JOURNAL.PONE.0033980
P407
P577
2012-03-29T00:00:00Z