(Q24303612)

GOA release 2020-03-11

Hsp90 protein binding

1 reference

GOA release 2020-03-11

June-Tai Wu

5

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Minoru Yoshida

object named as

Minoru Yoshida

7

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author name string

Jeffrey J Kovacs

1

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Patrick J M Murphy

2

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Stéphanie Gaillard

3

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Xuan Zhao

4

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Christopher V Nicchitta

6

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David O Toft

8

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William B Pratt

9

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Tso-Pang Yao

Hsp90: chaperoning signal transduction

10

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language of work or name

English

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publication date

27 May 2005

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published in

Molecular Cell

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volume

18

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page(s)

601-7

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issue

5

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cites work

1 reference

https://api.crossref.org/works/10.1016%2FJ.MOLCEL.2005.04.021

7 January 2021

Functional domains of the human glucocorticoid receptor

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Four different clones of mouse anti-acetyllysine monoclonal antibodies having different recognition properties share a common immunoglobulin framework structure

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7 January 2021

The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress

1 reference

https://api.crossref.org/works/10.1016%2FJ.MOLCEL.2005.04.021

7 January 2021

Active maintenance of mHDA2/mHDAC6 histone-deacetylase in the cytoplasm

1 reference

https://api.crossref.org/works/10.1016%2FJ.MOLCEL.2005.04.021

7 January 2021

Hsp90 inhibitors as novel cancer chemotherapeutic agents

1 reference

https://api.crossref.org/works/10.1016%2FJ.MOLCEL.2005.04.021

7 January 2021

HDAC6 is a microtubule-associated deacetylase

1 reference

https://api.crossref.org/works/10.1016%2FJ.MOLCEL.2005.04.021

7 January 2021

A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors

1 reference

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Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation

1 reference

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7 January 2021

Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90

1 reference

https://api.crossref.org/works/10.1016%2FJ.MOLCEL.2005.04.021

7 January 2021

Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70.

1 reference

https://api.crossref.org/works/10.1016%2FJ.MOLCEL.2005.04.021

7 January 2021

Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90

1 reference

https://api.crossref.org/works/10.1016%2FJ.MOLCEL.2005.04.021

7 January 2021

The Hsp90 Cochaperone p23 Is the Limiting Component of the Multiprotein Hsp90/Hsp70-based Chaperone System in Vivo Where It Acts to Stabilize the Client Protein·Hsp90 Complex

1 reference

https://api.crossref.org/works/10.1016%2FJ.MOLCEL.2005.04.021

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In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation

1 reference

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HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo

1 reference

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Modulation of p53, ErbB1, ErbB2, and Raf-1 expression in lung cancer cells by depsipeptide FR901228

1 reference

https://api.crossref.org/works/10.1016%2FJ.MOLCEL.2005.04.021

7 January 2021

Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery

1 reference

https://api.crossref.org/works/10.1016%2FJ.MOLCEL.2005.04.021

7 January 2021