Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine (Q28269439)

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English	Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine	scientific article

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instance of

scholarly article

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title

Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine (English)

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main subject

cell biology

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molecular chaperones

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phosphorylation

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based on heuristic

inferred from title

author

Kristin Beebe

series ordinal

7

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Chrisostomos Prodromou

object named as

Chrisostomos Prodromou

series ordinal

3

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Len Neckers

series ordinal

14

object named as

Len Neckers

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Jane B Trepel

series ordinal

11

object named as

Jane B Trepel

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Bradley T Scroggins

series ordinal

5

object named as

Bradley T Scroggins

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author name string

Wanping Xu

series ordinal

1

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Mehdi Mollapour

series ordinal

2

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Suiquan Wang

series ordinal

4

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Zach Palchick

series ordinal

6

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Marco Siderius

series ordinal

8

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Min-Jung Lee

series ordinal

9

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Anthony Couvillon

series ordinal

10

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Yoshihiko Miyata

series ordinal

12

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Robert Matts

series ordinal

13

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language of work or name

English

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publication date

10 August 2012

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published in

Molecular Cell

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volume

47

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issue

3

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page(s)

434-43

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cites work

Immunoaffinity profiling of tyrosine phosphorylation in cancer cells

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Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

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Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase

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HSP90 at the hub of protein homeostasis: emerging mechanistic insights

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Cellular functions regulated by Src family kinases

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7 April 2017

Heat shock protein 90's mechanochemical cycle is dominated by thermal fluctuations

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29 September 2017

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

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29 September 2017

Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis

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29 September 2017

Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37.

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PubMed Central

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29 September 2017

Unliganded and hormone-bound glucocorticoid receptors interact with distinct hydrophobic sites in the Hsp90 C-terminal domain

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PubMed Central

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29 September 2017

Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements

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PubMed Central

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29 September 2017

Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation

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PubMed Central

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29 September 2017

CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37.

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PubMed Central

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29 September 2017

Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery

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PubMed Central

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29 September 2017

Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37.

1 reference

stated in

PubMed Central

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29 September 2017

Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37.

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29 September 2017

The Hsp90-specific inhibitor geldanamycin selectively disrupts kinase-mediated signaling events of T-lymphocyte activation

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29 September 2017

Tyrosine Phosphorylation of a 50K Cellular Polypeptide Associated with the Rous Sarcoma Virus Transforming Protein pp60src

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29 September 2017

Analysis of the CK2-dependent phosphorylation of serine 13 in Cdc37 using a phospho-specific antibody and phospho-affinity gel electrophoresis

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27 November 2018

Functional Dissection of Cdc37: Characterization of Domain Structure and Amino Acid Residues Critical for Protein Kinase Binding

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PubMed Central

reference URL

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27 November 2018

The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/22727666

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Structural models and binding site prediction of the C-terminal domain of human Hsp90: a new target for anticancer drugs

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/22727666

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1016/J.MOLCEL.2012.05.015

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4373806

OpenCitations bibliographic resource ID

4373806

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4373806

PMC publication ID

3418412

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4373806

PubMed publication ID

22727666

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4373806

ResearchGate publication ID

228061733

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