(Q38313087)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16714764%20AND%20SRC:MED&resulttype=core&format=json

28 January 2020

title

The biochemical role of the heat shock protein 90 chaperone complex in establishing human telomerase activity (English)

1 reference

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28 January 2020

0 references

1

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28 January 2020

author name string

Allen T Grady

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16714764%20AND%20SRC:MED&resulttype=core&format=json

28 January 2020

Michael B Jarstfer

series ordinal

3

1 reference

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28 January 2020

language of work or name

English

0 references

publication date

19 May 2006

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16714764%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

28 January 2020

published in

1 reference

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28 January 2020

volume

281

1 reference

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28 January 2020

issue

29

1 reference

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28 January 2020

page(s)

19840-19848

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28 January 2020

cites work

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Isolation of a candidate human telomerase catalytic subunit gene, which reveals complex splicing patterns in different cell types.

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Stable association of hsp90 and p23, but Not hsp70, with active human telomerase

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Role of the heat shock response and molecular chaperones in oncogenesis and cell death

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Quantitation and intracellular localization of the 85K heat shock protein by using monoclonal and polyclonal antibodies

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

21 January 2018

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The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation

21 January 2018

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

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Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90

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The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90.

21 January 2018

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

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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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21 January 2018

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21 January 2018

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Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase

21 January 2018

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Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Human telomerase activation requires two independent interactions between telomerase RNA and telomerase reverse transcriptase

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M511067200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16714764%20AND%20SRC:MED&resulttype=core&format=json

28 January 2020

1 reference