The co-chaperone Cdc37 regulates the rabies virus phosphoprotein stability by targeting to Hsp90AA1 machinery.

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Rabies Virus Infection Induces Microtubule Depolymerization to Facilitate Viral RNA Synthesis by Upregulating HDAC6.Identification and characterization of host cell proteins interacting with Scylla serrata reovirus non-structural protein p35.Hsp90 interacts with multiple dengue virus 2 proteins.

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The co-chaperone Cdc37 regulates the rabies virus phosphoprotein stability by targeting to Hsp90AA1 machinery.

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http://www.wikidata.org/entity/Q36959539

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

@zh-hk

2016年論文

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2016年論文

@zh-tw

2016年论文

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2016年论文

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2016年论文

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name

The co-chaperone Cdc37 regulat ...... rgeting to Hsp90AA1 machinery.

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type

Item

label

The co-chaperone Cdc37 regulat ...... rgeting to Hsp90AA1 machinery.

@en

prefLabel

The co-chaperone Cdc37 regulat ...... rgeting to Hsp90AA1 machinery.

@en

P1476

The co-chaperone Cdc37 regulat ...... rgeting to Hsp90AA1 machinery.

@en

P2093

Dandan Wang

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

Fei Liu

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

Jie Zan

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

Jiyong Zhou

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

Juan Liu

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

Senlin Ji

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

Yan Yan

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

Yunbin Xu

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

P2860

Hsp90 regulates p50(cdc37) function during the biogenesis of the activeconformation of the heme-regulated eIF2 alpha kinase

Hsp90: a specialized but essential protein-folding tool

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

Circovirus transport proceeds via direct interaction of the cytoplasmic dynein IC1 subunit with the viral capsid protein

Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4

Interaction of the rabies virus P protein with the LC8 dynein light chain

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

The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

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

Structure of the vesicular stomatitis virus nucleocapsid in complex with the nucleocapsid-binding domain of the small polymerase cofactor, P

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srep27123

P304

27123

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scholarly article

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10.1038/SREP27123

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English

P478

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

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2016-06-02T00:00:00Z

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1047765346

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27251758

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P921

Amorru

molecular chaperones

P932

4890047

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

The co-chaperone Cdc37 regulates the rabies virus phosphoprotein stability by targeting to Hsp90AA1 machinery.

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P2860

P2860

The co-chaperone Cdc37 regulates the rabies virus phosphoprotein stability by targeting to Hsp90AA1 machinery.

description

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type

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P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P577

P6179

P698

P921

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P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P577

P6179

P698

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P932