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Literature DB >> 21898227

Detecting HSP90 phosphorylation.

Abstract

Heat-shock protein 90 (HSP90) is an essential molecular chaperone in eukaryotes. It is important for chaperoning proteins that are important determinants of multistep carcinogenesis. HSP90's ATPase activity is associated with its chaperone function. Co-chaperones as well as posttranslational modifications (phosphorylation, acetylation, and S-nitrosylation) are important for regulating its ATPase activity. Yeast can be used to express and purify HSP90 and also detect its phosphorylation by pan-phosphoserine or phosphothreonine antibodies.

Entities: Chemical Disease Gene Species

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Year: 2011 PMID： 21898227 PMCID： PMC7380563 DOI： 10.1007/978-1-61779-295-3_5

Source DB: PubMed Journal: Methods Mol Biol ISSN： 1064-3745

43 in total

Review 1. Structure and mechanism of the Hsp90 molecular chaperone machinery.

Authors: Laurence H Pearl; Chrisostomos Prodromou
Journal: Annu Rev Biochem Date: 2006 Impact factor: 23.643

Review 2. Hsp90 and developmental networks.

Authors: Suzannah Rutherford; Jennifer R Knapp; Peter Csermely
Journal: Adv Exp Med Biol Date: 2007 Impact factor: 2.622

3. Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1.

Authors: Jill L Johnson; Agnieszka Halas; Gary Flom
Journal: Mol Cell Biol Date: 2006-11-13 Impact factor: 4.272

Review 4. The Hsp90 capacitor, developmental remodeling, and evolution: the robustness of gene networks and the curious evolvability of metamorphosis.

Authors: Suzannah Rutherford; Yoshikazu Hirate; Billie J Swalla
Journal: Crit Rev Biochem Mol Biol Date: 2007 Sep-Oct Impact factor: 8.250

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

Authors: C Prodromou; S M Roe; R O'Brien; J E Ladbury; P W Piper; L H Pearl
Journal: Cell Date: 1997-07-11 Impact factor: 41.582

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

Authors: C E Stebbins; A A Russo; C Schneider; N Rosen; F U Hartl; N P Pavletich
Journal: Cell Date: 1997-04-18 Impact factor: 41.582

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

Authors: J P Grenert; W P Sullivan; P Fadden; T A Haystead; J Clark; E Mimnaugh; H Krutzsch; H J Ochel; T W Schulte; E Sausville; L M Neckers; D O Toft
Journal: J Biol Chem Date: 1997-09-19 Impact factor: 5.157

8. Expressed in the yeast Saccharomyces cerevisiae, human ERK5 is a client of the Hsp90 chaperone that complements loss of the Slt2p (Mpk1p) cell integrity stress-activated protein kinase.

Authors: Andrew W Truman; Stefan H Millson; James M Nuttall; Victoria King; Mehdi Mollapour; Chrisostomos Prodromou; Laurence H Pearl; Peter W Piper
Journal: Eukaryot Cell Date: 2006-09-01

Detecting HSP90 phosphorylation.

Review 1. Structure and mechanism of the Hsp90 molecular chaperone machinery.

Review 2. Hsp90 and developmental networks.

3. Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1.

Review 4. The Hsp90 capacitor, developmental remodeling, and evolution: the robustness of gene networks and the curious evolvability of metamorphosis.

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

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

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

8. Expressed in the yeast Saccharomyces cerevisiae, human ERK5 is a client of the Hsp90 chaperone that complements loss of the Slt2p (Mpk1p) cell integrity stress-activated protein kinase.

9. Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase.

10. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis.

Review 1. Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity.

2. The dynamic interactome of human Aha1 upon Y223 phosphorylation.