PTGES3

From Wikipedia, the free encyclopedia


Prostaglandin E synthase 3 (cytosolic)
PDB rendering based on 1ejf.
Available structures: 1ejf
Identifiers
Symbol(s) PTGES3; TEBP; P23
External IDs OMIM: 607061 MGI1929282 HomoloGene81751
Orthologs
Human Mouse
Entrez 10728 56351


Refseq NM_006601 (mRNA)
NP_006592 (protein)
NM_019766 (mRNA)
NP_062740 (protein)
Pubmed search [1] [2]

Prostaglandin E synthase 3 (cytosolic), also known as PTGES3, is a human gene.[1]


[edit] References

[edit] Further reading

  • Johnson JL, Beito TG, Krco CJ, Toft DO (1994). "Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes.". Mol. Cell. Biol. 14 (3): 1956–63. PMID 8114727. 
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548. 
  • Dittmar KD, Pratt WB (1997). "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.". J. Biol. Chem. 272 (20): 13047–54. PMID 9148915. 
  • Dittmar KD, Demady DR, Stancato LF, et al. (1997). "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.". J. Biol. Chem. 272 (34): 21213–20. PMID 9261129. 
  • Zou J, Guo Y, Guettouche T, et al. (1998). "Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1.". Cell 94 (4): 471–80. PMID 9727490. 
  • Yoo JY, Hamburger AW (1999). "Interaction of the p23/p198 protein with ErbB-3.". Gene 229 (1-2): 215–21. PMID 10095121. 
  • Knoblauch R, Garabedian MJ (1999). "Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction.". Mol. Cell. Biol. 19 (5): 3748–59. PMID 10207098. 
  • Muñoz MJ, Bejarano ER, Daga RR, Jimenez J (2000). "The identification of Wos2, a p23 homologue that interacts with Wee1 and Cdc2 in the mitotic control of fission yeasts.". Genetics 153 (4): 1561–72. PMID 10581266. 
  • Freeman BC, Felts SJ, Toft DO, Yamamoto KR (2000). "The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies.". Genes Dev. 14 (4): 422–34. PMID 10691735. 
  • Weaver AJ, Sullivan WP, Felts SJ, et al. (2000). "Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone.". J. Biol. Chem. 275 (30): 23045–52. doi:10.1074/jbc.M003410200. PMID 10811660. 
  • Tanioka T, Nakatani Y, Semmyo N, et al. (2000). "Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2 biosynthesis.". J. Biol. Chem. 275 (42): 32775–82. doi:10.1074/jbc.M003504200. PMID 10922363. 
  • Kazlauskas A, Poellinger L, Pongratz I (2001). "The immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptor.". J. Biol. Chem. 275 (52): 41317–24. doi:10.1074/jbc.M007765200. PMID 11013261. 
  • Futatsumori M, Kasai K, Takatsu H, et al. (2001). "Identification and characterization of novel isoforms of COP I subunits.". J. Biochem. 128 (5): 793–801. PMID 11056392. 
  • Kazlauskas A, Sundström S, Poellinger L, Pongratz I (2001). "The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor.". Mol. Cell. Biol. 21 (7): 2594–607. doi:10.1128/MCB.21.7.2594-2607.2001. PMID 11259606. 
  • Forsythe HL, Jarvis JL, Turner JW, et al. (2001). "Stable association of hsp90 and p23, but Not hsp70, with active human telomerase.". J. Biol. Chem. 276 (19): 15571–4. doi:10.1074/jbc.C100055200. PMID 11274138. 
  • Donzé O, Abbas-Terki T, Picard D (2001). "The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR.". EMBO J. 20 (14): 3771–80. doi:10.1093/emboj/20.14.3771. PMID 11447118. 
  • Elder RT, Yu M, Chen M, et al. (2001). "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.". Virology 287 (2): 359–70. doi:10.1006/viro.2001.1007. PMID 11531413. 
  • Hernández MP, Chadli A, Toft DO (2002). "HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor.". J. Biol. Chem. 277 (14): 11873–81. doi:10.1074/jbc.M111445200. PMID 11809754. 
  • McLaughlin SH, Smith HW, Jackson SE (2002). "Stimulation of the weak ATPase activity of human hsp90 by a client protein.". J. Mol. Biol. 315 (4): 787–98. doi:10.1006/jmbi.2001.5245. PMID 11812147. 
  • Cox MB, Miller CA (2002). "The p23 co-chaperone facilitates dioxin receptor signaling in a yeast model system.". Toxicol. Lett. 129 (1-2): 13–21. PMID 11879970.