Regulation and function of the human HSP90AA1 gene (Q28646043)

Europe PubMed Central

title

Regulation and function of the human HSP90AA1 gene (English)

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part of the series

Gene Wiki Review Series

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author

Kristin Beebe

2

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Len Neckers

3

object named as

Len Neckers

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author name string

Abbey D Zuehlke

1

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Thomas Prince

Selective targeting of the stress chaperome as a therapeutic strategy

4

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language of work or name

English

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publication date

1 October 2015

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published in

Gene

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volume

570

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page(s)

8-16

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issue

1

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cites work

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Nucleotide sequence and regulation of a human 90-kDa heat shock protein gene

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17 March 2017

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17 March 2017

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High constitutive expression of heat shock protein 90α in human acute leukemia cells

17 March 2017

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HSP90 at the hub of protein homeostasis: emerging mechanistic insights

17 March 2017

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7 April 2017

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Spermatogenesis arrest caused by conditional deletion of Hsp90α in adult mice

3 June 2018

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3 June 2018

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3 June 2018

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Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment

3 June 2018

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Post-translational modifications of Hsp90 and their contributions to chaperone regulation

3 June 2018

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Increased expression of co-chaperone HOP with HSP90 and HSC70 and complex formation in human colonic carcinoma

3 June 2018

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Secretion of extracellular hsp90alpha via exosomes increases cancer cell motility: a role for plasminogen activation

3 June 2018

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Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket

3 June 2018

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Inhibition of apoptosome formation by suppression of Hsp90beta phosphorylation in tyrosine kinase-induced leukemias

3 June 2018

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Drug-mediated targeted disruption of multiple protein activities through functional inhibition of the Hsp90 chaperone complex

3 June 2018

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3 June 2018

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3 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4519370

A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket

3 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4519370

Phylogenetic analysis of the 90 kD heat shock family of protein sequences and an examination of the relationship among animals, plants, and fungi species

3 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4519370

Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer.

3 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4519370

Opposite effect of Hsp90α and Hsp90β on eNOS ability to produce nitric oxide or superoxide anion in human embryonic kidney cells.

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4519370

Hsp90alpha chaperones large C-terminally extended proteolytic intermediates in the MHC class I antigen processing pathway

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4519370

Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies

27 November 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4519370

The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues

27 November 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/26071189

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1016/J.GENE.2015.06.018

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4373749

OpenCitations bibliographic resource ID

4373749

1 reference