1. References

2. Further reading

The protein encoded by this gene is also known as p23 which functions as a chaperone which is required for proper functioning of the glucocorticoid and other steroid receptors.^[2]

References

Further reading

• {{cite journal |vauthors=Johnson JL, Beito TG, Krco CJ, Toft DO |title=Characterization of a novel 23-kilodalton protein of inactive progesterone receptor complexes |journal=Mol. Cell. Biol. |volume=14 |issue= 3 |pages= 1956–63 |year= 1994 |pmid= 8114727 |doi= 10.1128/MCB.14.3.1956| pmc=358554 }}
• {{cite journal |vauthors=Wu T, Wu H, Wang J, Wang J |title=Expression and cellular localization of cyclooxygenases and prostaglandin E synthases in the hemorrhagic brain. |journal=J Neuroinflammation |volume=8 |pages= 22 |year= 2011 |pmid= 21385433 |doi=10.1186/1742-2094-8-22 | pmc=3062590 }}
• {{cite journal |vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
• {{cite journal |vauthors=Dittmar KD, Pratt WB |title=Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation |journal=J. Biol. Chem. |volume=272 |issue= 20 |pages= 13047–13054 |year= 1997 |pmid= 9148915 |doi=10.1074/jbc.272.20.13047 }}
• {{cite journal | author=Dittmar KD |title=Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70 |journal=J. Biol. Chem. |volume=272 |issue= 34 |pages= 21213–21220 |year= 1997 |pmid= 9261129 |doi=10.1074/jbc.272.34.21213 |name-list-format=vanc| author2=Demady DR | author3=Stancato LF | display-authors=3 | last4=Krishna | first4=P | last5=Pratt | first5=WB }}
• {{cite journal | author=Zou J |title=Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1 |journal=Cell |volume=94 |issue= 4 |pages= 471–480 |year= 1998 |pmid= 9727490 |doi=10.1016/S0092-8674(00)81588-3 |name-list-format=vanc| author2=Guo Y | author3=Guettouche T | display-authors=3 | last4=Smith | first4=David F | last5=Voellmy | first5=Richard }}
• {{cite journal |vauthors=Yoo JY, Hamburger AW |title=Interaction of the p23/p198 protein with ErbB-3 |journal=Gene |volume=229 |issue= 1–2 |pages= 215–221 |year= 1999 |pmid= 10095121 |doi=10.1016/S0378-1119(98)00604-0 }}
• {{cite journal |vauthors=Knoblauch R, Garabedian MJ |title=Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction |journal=Mol. Cell. Biol. |volume=19 |issue= 5 |pages= 3748–59 |year= 1999 |pmid= 10207098 |doi= 10.1128/MCB.19.5.3748| pmc=84199 }}
• {{cite journal |vauthors=Muñoz MJ, Bejarano ER, Daga RR, Jimenez J |title=The identification of Wos2, a p23 homologue that interacts with Wee1 and Cdc2 in the mitotic control of fission yeasts |journal=Genetics |volume=153 |issue= 4 |pages= 1561–72 |year= 2000 |pmid= 10581266 |doi= | pmc=1460861 }}
• {{cite journal |vauthors=Freeman BC, Felts SJ, Toft DO, Yamamoto KR |title=The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies |journal=Genes Dev. |volume=14 |issue= 4 |pages= 422–34 |year= 2000 |pmid= 10691735 |doi= | pmc=316379 }}
• {{cite journal | author=Weaver AJ |title=Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 23045–23052 |year= 2000 |pmid= 10811660 |doi= 10.1074/jbc.M003410200 |name-list-format=vanc| author2=Sullivan WP | author3=Felts SJ | display-authors=3 | last4=Owen | first4=BA | last5=Toft | first5=DO }}
• {{cite journal | author=Tanioka T |title=Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2 biosynthesis |journal=J. Biol. Chem. |volume=275 |issue= 42 |pages= 32775–32782 |year= 2000 |pmid= 10922363 |doi= 10.1074/jbc.M003504200 |name-list-format=vanc| author2=Nakatani Y | author3=Semmyo N | display-authors=3 | last4=Murakami | first4=M | last5=Kudo | first5=I }}
• {{cite journal |vauthors=Kazlauskas A, Poellinger L, Pongratz I |title=The immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptor |journal=J. Biol. Chem. |volume=275 |issue= 52 |pages= 41317–41324 |year= 2001 |pmid= 11013261 |doi= 10.1074/jbc.M007765200 }}
• {{cite journal | author=Futatsumori M |title=Identification and characterization of novel isoforms of COP I subunits |journal=J. Biochem. |volume=128 |issue= 5 |pages= 793–801 |year= 2001 |pmid= 11056392 |doi= 10.1093/oxfordjournals.jbchem.a022817|name-list-format=vanc| author2=Kasai K | author3=Takatsu H | display-authors=3 | last4=Shin | first4=HW | last5=Nakayama | first5=K }}
• {{cite journal |vauthors=Kazlauskas A, Sundström S, Poellinger L, Pongratz I |title=The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor |journal=Mol. Cell. Biol. |volume=21 |issue= 7 |pages= 2594–2607 |year= 2001 |pmid= 11259606 |doi= 10.1128/MCB.21.7.2594-2607.2001 | pmc=86890 }}
• {{cite journal | author=Forsythe HL |title=Stable association of hsp90 and p23, but Not hsp70, with active human telomerase |journal=J. Biol. Chem. |volume=276 |issue= 19 |pages= 15571–15574 |year= 2001 |pmid= 11274138 |doi= 10.1074/jbc.C100055200 |name-list-format=vanc| author2=Jarvis JL | author3=Turner JW | display-authors=3 | last4=Elmore | first4=LW | last5=Holt | first5=SE }}
• {{cite journal |vauthors=Donzé O, Abbas-Terki T, Picard D |title=The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR |journal=EMBO J. |volume=20 |issue= 14 |pages= 3771–3780 |year= 2001 |pmid= 11447118 |doi= 10.1093/emboj/20.14.3771 | pmc=125551 }}
• {{cite journal | author=Elder RT |title=HIV-1 Vpr induces cell cycle G2 arrest in fission yeast (Schizosaccharomyces pombe) through a pathway involving regulatory and catalytic subunits of PP2A and acting on both Wee1 and Cdc25 |journal=Virology |volume=287 |issue= 2 |pages= 359–370 |year= 2001 |pmid= 11531413 |doi= 10.1006/viro.2001.1007 |name-list-format=vanc| author2=Yu M | author3=Chen M | display-authors=3 | last4=Zhu | first4=X | last5=Yanagida | first5=M | last6=Zhao | first6=Y }}
• {{cite journal |vauthors=Hernández MP, Chadli A, Toft DO |title=HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 11873–11881 |year= 2002 |pmid= 11809754 |doi= 10.1074/jbc.M111445200 }}
• {{cite journal |vauthors=McLaughlin SH, Smith HW, Jackson SE |title=Stimulation of the weak ATPase activity of human hsp90 by a client protein |journal=J. Mol. Biol. |volume=315 |issue= 4 |pages= 787–798 |year= 2002 |pmid= 11812147 |doi= 10.1006/jmbi.2001.5245 }}
• {{cite journal |vauthors=Cox MB, Miller CA |title=The p23 co-chaperone facilitates dioxin receptor signaling in a yeast model system |journal=Toxicol. Lett. |volume=129 |issue= 1–2 |pages= 13–21 |year= 2002 |pmid= 11879970 |doi=10.1016/S0378-4274(01)00465-9 }}

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