Phosphorylated and unphosphorylated serine 13 of CDC37 stabilize distinct interactions between its client and HSP90 binding domains.
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Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinaseMulti-kinase inhibitors can associate with heat shock proteins through their NH2-termini by which they suppress chaperone functionStructural and functional basis of protein phosphatase 5 substrate specificity.Effect of glycosides of Cistanche on the expression of mitochondrial precursor protein and keratin type II cytoskeletal 6A in a rat model of vascular dementia.Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37.Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System.
P2860
Phosphorylated and unphosphorylated serine 13 of CDC37 stabilize distinct interactions between its client and HSP90 binding domains.
description
2015 nî lūn-bûn
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2015年の論文
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2015年論文
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2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
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2015年論文
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2015年论文
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2015年论文
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2015年论文
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name
Phosphorylated and unphosphory ...... ent and HSP90 binding domains.
@en
type
label
Phosphorylated and unphosphory ...... ent and HSP90 binding domains.
@en
prefLabel
Phosphorylated and unphosphory ...... ent and HSP90 binding domains.
@en
P2860
P356
P1433
P1476
Phosphorylated and unphosphory ...... ent and HSP90 binding domains.
@en
P2093
Ralf Landgraf
Wenjun Liu
P2860
P304
P356
10.1021/BI501129G
P407
P577
2015-02-11T00:00:00Z