How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.

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Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains.

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How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.

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2017 nî lūn-bûn

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2017年の論文

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2017年論文

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2017年論文

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How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.

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How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.

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How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.

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How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.

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David A Agard

http://www.w3.org/2001/XMLSchema#string

Kliment A Verba

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Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition

Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperones

Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles

Protein kinase CK2 in health and disease: CK2: the kinase controlling the Hsp90 chaperone machinery

Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha.

Interaction between Cdc37 and Cdk4 in human cells

p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function

The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)

The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy

Structural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis Mechanism

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799-811

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scholarly article

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10.1016/J.TIBS.2017.07.002

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2017-08-04T00:00:00Z

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28784328

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5621984

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How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.

about

P2860

P2860

How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches.

description

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type

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prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P932