Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational changes and binding of further cofactors.
about
The architecture of functional modules in the Hsp90 co-chaperone Sti1/HopThe activity of protein phosphatase 5 towards native clients is modulated by the middle- and C-terminal domains of Hsp90Selective activators of protein phosphatase 5 target the auto-inhibitory mechanism.Differential modulation of functional dynamics and allosteric interactions in the Hsp90-cochaperone complexes with p23 and Aha1: a computational study.An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humansDownregulation of the Hsp90 system causes defects in muscle cells of Caenorhabditis elegansThe lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity.Probing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics.Challenging muscle homeostasis uncovers novel chaperone interactions in Caenorhabditis elegansCo-chaperones of Hsp90 in Plasmodium falciparum and their concerted roles in cellular regulation.Alternative approaches to Hsp90 modulation for the treatment of cancer.Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.A two-domain protein triggers heat shock pathway and necrosis pathway both in model plant and nematode.Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites.Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate.
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P2860
Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational changes and binding of further cofactors.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Cdc37-Hsp90 complexes are resp ...... binding of further cofactors.
@en
type
label
Cdc37-Hsp90 complexes are resp ...... binding of further cofactors.
@en
prefLabel
Cdc37-Hsp90 complexes are resp ...... binding of further cofactors.
@en
P2860
P356
P1476
Cdc37-Hsp90 complexes are resp ...... binding of further cofactors.
@en
P2093
Andreas M Gaiser
Anja Kretzschmar
P2860
P304
40921-40932
P356
10.1074/JBC.M110.131086
P407
P577
2010-09-29T00:00:00Z