HSP82/YPL240C Literature Guide Help

Other names published for HSP82: HSP90, Hsp90 family chaperone HSP82, YPL240C

HSP82 - Alias (32)

ReferenceOther Genes Addressed
Cunningham CN, et al.  (2012) The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis. Protein Sci 21(8):1162-71
Franzosa EA, et al.  (2011) Heterozygous yeast deletion collection screens reveal essential targets of hsp90. PLoS One 6(11):e28211
Mollapour M, et al.  (2010) Hsp90 phosphorylation, Wee1 and the cell cycle. Cell Cycle 9(12):2310-6
Gong Y, et al.  (2009) An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Mol Syst Biol 5:275
Wandinger SK, et al.  (2008) The hsp90 chaperone machinery. J Biol Chem 283(27):18473-7
Wandinger SK, et al.  (2006) The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. EMBO J 25(2):367-76
Zhao R, et al.  (2005) Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 120(5):715-27
Hatakeyama S, et al.  (2004) Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones. Genes Cells 9(6):533-48
Lan C, et al.  (2004) A novel mode of chaperone action: heme activation of Hap1 by enhanced association of Hsp90 with the repressed Hsp70-Hap1 complex. J Biol Chem 279(26):27607-12
Lingelbach LB and Kaplan KB  (2004) The interaction between Sgt1p and Skp1p is regulated by HSP90 chaperones and is required for proper CBF3 assembly. Mol Cell Biol 24(20):8938-50
Meyer P, et al.  (2004) Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J 23(3):511-9
Rowlands MG, et al.  (2004) High-throughput screening assay for inhibitors of heat-shock protein 90 ATPase activity. Anal Biochem 327(2):176-83
Piper PW, et al.  (2003) Sensitivity to Hsp90-targeting drugs can arise with mutation to the Hsp90 chaperone, cochaperones and plasma membrane ATP binding cassette transporters of yeast. Eur J Biochem 270(23):4689-95
Cox MB and Miller CA 3rd  (2002) The p23 co-chaperone facilitates dioxin receptor signaling in a yeast model system. Toxicol Lett 129(1-2):13-21
Stemmann O, et al.  (2002) Hsp90 enables Ctf13p/Skp1p to nucleate the budding yeast kinetochore. Proc Natl Acad Sci U S A 99(13):8585-90
Abbas-Terki T, et al.  (2001) Hsp104 interacts with Hsp90 cochaperones in respiring yeast. Mol Cell Biol 21(22):7569-75
Hon T, et al.  (2001) The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme. Mol Cell Biol 21(23):7923-32
Freeman BC, et al.  (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
Lindquist S  (2000) But yeast prion offers clues about evolution. Nature 408(6808):17-8
Mayr C, et al.  (2000) Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties. J Biol Chem 275(44):34140-6
Knoblauch R and Garabedian MJ  (1999) Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction. Mol Cell Biol 19(5):3748-59
Caplan AJ  (1997) Yeast molecular chaperones and the mechanism of steroid hormone action. Trends Endocrinol Metab 8(7):271-5
Dey B, et al.  (1996) The Ydj1 molecular chaperone facilitates formation of active p60v-src in yeast. Mol Biol Cell 7(1):91-100
Kimura Y, et al.  (1995) Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science 268(5215):1362-5
Whitelaw ML, et al.  (1995) Heat shock protein hsp90 regulates dioxin receptor function in vivo. Proc Natl Acad Sci U S A 92(10):4437-41
Hsin CY and Castilho-Valavicius BA  (1994) The gene encoding eIF-2 beta in S. cerevisiae maps to chromosome XVI. Braz J Med Biol Res 27(10):2359-64
Bohen SP and Yamamoto KR  (1993) Isolation of Hsp90 mutants by screening for decreased steroid receptor function. Proc Natl Acad Sci U S A 90(23):11424-8
Johnson KS, et al.  (1989) The 86-kilodalton antigen from Schistosoma mansoni is a heat-shock protein homologous to yeast HSP-90. Mol Biochem Parasitol 36(1):19-28
Mottram JC, et al.  (1989) A transcriptional analysis of the Trypanosoma brucei hsp83 gene cluster. Mol Biochem Parasitol 37(1):115-27
Dragon EA, et al.  (1987) The genome of Trypanosoma cruzi contains a constitutively expressed, tandemly arranged multicopy gene homologous to a major heat shock protein. Mol Cell Biol 7(3):1271-5