Isoform-Specific Phosphorylation in Human Hsp90β Affects Interaction with Clients and the Cochaperone Cdc37.
about
Detecting Posttranslational Modifications of Hsp90.Identification of Hsp90 inhibitors with anti-Plasmodium activity.Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation.A switch point in the molecular chaperone Hsp90 responding to client interaction.Dissecting Structure-Encoded Determinants of Allosteric Cross-Talk between Post-Translational Modification Sites in the Hsp90 Chaperones.
P2860
Isoform-Specific Phosphorylation in Human Hsp90β Affects Interaction with Clients and the Cochaperone Cdc37.
description
2017 nî lūn-bûn
@nan
2017年の論文
@ja
2017年論文
@yue
2017年論文
@zh-hant
2017年論文
@zh-hk
2017年論文
@zh-mo
2017年論文
@zh-tw
2017年论文
@wuu
2017年论文
@zh
2017年论文
@zh-cn
name
Isoform-Specific Phosphorylati ...... nts and the Cochaperone Cdc37.
@en
Isoform-Specific Phosphorylati ...... nts and the Cochaperone Cdc37.
@nl
type
label
Isoform-Specific Phosphorylati ...... nts and the Cochaperone Cdc37.
@en
Isoform-Specific Phosphorylati ...... nts and the Cochaperone Cdc37.
@nl
prefLabel
Isoform-Specific Phosphorylati ...... nts and the Cochaperone Cdc37.
@en
Isoform-Specific Phosphorylati ...... nts and the Cochaperone Cdc37.
@nl
P2093
P1476
Isoform-Specific Phosphorylati ...... ents and the Cochaperone Cdc37
@en
P2093
Laura Le Breton
Minh T N Nguyen
Robert A Knieß
Soumya Daturpalli
Xiangyu Ke
Xuemei Chen
P304
P356
10.1016/J.JMB.2017.01.011
P407
P577
2017-01-19T00:00:00Z