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Global functional map of the p23 molecular chaperone reveals an extensive cellular network.

Echtenkamp FJ, Zelin E, Oxelmark E, Woo JI, Andrews BJ, Garabedian M, Freeman BC.

Mol Cell. 2011 Jul 22;43(2):229-41. doi: 10.1016/j.molcel.2011.05.029.


p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity.

Forafonov F, Toogun OA, Grad I, Suslova E, Freeman BC, Picard D.

Mol Cell Biol. 2008 May;28(10):3446-56. doi: 10.1128/MCB.02246-07. Epub 2008 Mar 24.


SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins.

Fang Y, Fliss AE, Rao J, Caplan AJ.

Mol Cell Biol. 1998 Jul;18(7):3727-34.


Cooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signaling.

Cox MB, Miller CA 3rd.

Cell Stress Chaperones. 2004 Mar;9(1):4-20.


Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system.

Mandal AK, Gibney PA, Nillegoda NB, Theodoraki MA, Caplan AJ, Morano KA.

Mol Biol Cell. 2010 May 1;21(9):1439-48. doi: 10.1091/mbc.E09-09-0779. Epub 2010 Mar 17.


Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone.

Zhao R, Davey M, Hsu YC, Kaplanek P, Tong A, Parsons AB, Krogan N, Cagney G, Mai D, Greenblatt J, Boone C, Emili A, Houry WA.

Cell. 2005 Mar 11;120(5):715-27.


Hsp104 interacts with Hsp90 cochaperones in respiring yeast.

Abbas-Terki T, Donzé O, Briand PA, Picard D.

Mol Cell Biol. 2001 Nov;21(22):7569-75.


The Hsp90 co-chaperone p23 of Toxoplasma gondii: Identification, functional analysis and dynamic interactome determination.

Echeverria PC, Figueras MJ, Vogler M, Kriehuber T, de Miguel N, Deng B, Dalmasso MC, Matthews DE, Matrajt M, Haslbeck M, Buchner J, Angel SO.

Mol Biochem Parasitol. 2010 Aug;172(2):129-40. doi: 10.1016/j.molbiopara.2010.04.004. Epub 2010 Apr 18.


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

Panaretou B, Siligardi G, Meyer P, Maloney A, Sullivan JK, Singh S, Millson SH, Clarke PA, Naaby-Hansen S, Stein R, Cramer R, Mollapour M, Workman P, Piper PW, Pearl LH, Prodromou C.

Mol Cell. 2002 Dec;10(6):1307-18.


Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex.

Ali MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, Piper PW, Prodromou C, Pearl LH.

Nature. 2006 Apr 20;440(7087):1013-7.


Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle.

Siligardi G, Hu B, Panaretou B, Piper PW, Pearl LH, Prodromou C.

J Biol Chem. 2004 Dec 10;279(50):51989-98. Epub 2004 Oct 2.


Characterization of orchardgrass p23, a flowering plant Hsp90 cohort protein.

Cha JY, Ermawati N, Jung MH, Su'udi M, Kim KY, Kim JY, Han CD, Lee KH, Son D.

Cell Stress Chaperones. 2009 May;14(3):233-43. doi: 10.1007/s12192-008-0077-6. Epub 2008 Sep 18.


Genetic dissection of p23, an Hsp90 cochaperone, reveals a distinct surface involved in estrogen receptor signaling.

Oxelmark E, Knoblauch R, Arnal S, Su LF, Schapira M, Garabedian MJ.

J Biol Chem. 2003 Sep 19;278(38):36547-55. Epub 2003 Jun 30.


The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922.

Armstrong H, Wolmarans A, Mercier R, Mai B, LaPointe P.

PLoS One. 2012;7(11):e49322. doi: 10.1371/journal.pone.0049322. Epub 2012 Nov 14.


The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle.

Richter K, Walter S, Buchner J.

J Mol Biol. 2004 Oct 1;342(5):1403-13.


Cdc37 regulation of the kinome: when to hold 'em and when to fold 'em.

Karnitz LM, Felts SJ.

Sci STKE. 2007 May 8;2007(385):pe22. Review.


Expanding the cellular molecular chaperone network through the ubiquitous cochaperones.

Echtenkamp FJ, Freeman BC.

Biochim Biophys Acta. 2012 Mar;1823(3):668-73. doi: 10.1016/j.bbamcr.2011.08.011. Epub 2011 Aug 24. Review.


The p23 co-chaperone facilitates dioxin receptor signaling in a yeast model system.

Cox MB, Miller CA 3rd.

Toxicol Lett. 2002 Mar 24;129(1-2):13-21.


Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity.

Mollapour M, Tsutsumi S, Truman AW, Xu W, Vaughan CK, Beebe K, Konstantinova A, Vourganti S, Panaretou B, Piper PW, Trepel JB, Prodromou C, Pearl LH, Neckers L.

Mol Cell. 2011 Mar 18;41(6):672-81. doi: 10.1016/j.molcel.2011.02.011.

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