A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells (Q43577973)

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scientific article published in March 2001

Language	Label	Description	Also known as
English	A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells	scientific article published in March 2001

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells (English)

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Europe PubMed Central

PubMed publication ID

24 November 2017

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author name string

Chiosis G

1

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24 November 2017

Timaul MN

2

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24 November 2017

Lucas B

3

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24 November 2017

Munster PN

4

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24 November 2017

Zheng FF

5

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24 November 2017

Sepp-Lorenzino L

6

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24 November 2017

Rosen N

7

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24 November 2017

publication date

1 March 2001

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24 November 2017

number of pages

11

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Chemistry and Biology

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24 November 2017

8

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24 November 2017

3

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24 November 2017

289-299

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24 November 2017

Hsp90 & Co. - a holding for folding

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https://api.crossref.org/works/10.1016%2FS1074-5521%2801%2900015-1

7 January 2021

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Recent Advances in the Study of hsp90 Structure and Mechanism of Action

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https://api.crossref.org/works/10.1016%2FS1074-5521%2801%2900015-1

7 January 2021

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The Hsp90 complex--a super-chaperone machine as a novel drug target

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https://api.crossref.org/works/10.1016%2FS1074-5521%2801%2900015-1

7 January 2021

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Structure and in vivo function of Hsp90.

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7 January 2021

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The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors

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7 January 2021

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The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase

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7 January 2021

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The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent

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Association of Hsp90 with cellular Src-family kinases in a cell-free system correlates with altered kinase structure and function

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Unusual expression and localization of heat-shock proteins in human tumor cells

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Geldanamycin as a potential anti-cancer agent: its molecular target and biochemical activity

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A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone

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Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

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7 January 2021

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Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

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Antibiotic radicicol binds to the N-terminal domain of Hsp90 and shares important biologic activities with geldanamycin

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Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin

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Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings

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Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation

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Short circuiting stress protein expression via a tyrosine kinase inhibitor, herbimycin A.

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Facile synthesis of a library of 9-alkyl-8-benzyl-9H-purin-6-ylamine derivatives

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Flow cytometric analysis of G1- and G2/M-phase subpopulations in mammalian cell nuclei using side scatter and DNA content measurements

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Identifiers

10.1016/S1074-5521(01)00015-1

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

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