HSC82/YMR186W Literature Guide Help

Other names published for HSC82: HSP90, Hsp90 family chaperone HSC82, YMR186W

HSC82 - Protein Sequence Features (26)

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
Pursell NW, et al.  (2012) Solubility-promoting function of Hsp90 contributes to client maturation and robust cell growth. Eukaryot Cell 11(8):1033-41
Schmid AB, et al.  (2012) The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. EMBO J 31(6):1506-17
Mollapour M, et al.  (2011) Casein kinase 2 phosphorylation of Hsp90 threonine 22 modulates chaperone function and drug sensitivity. Oncotarget 2(5):407-17
Street TO, et al.  (2011) Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone. Mol Cell 42(1):96-105
Marino SM, et al.  (2010) Characterization of Surface-Exposed Reactive Cysteine Residues in Saccharomyces cerevisiae. Biochemistry 49(35):7709-21
Mollapour M, et al.  (2010) Hsp90 phosphorylation, Wee1 and the cell cycle. Cell Cycle 9(12):2310-6
Wayne N, et al.  (2010) Modular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo. J Biol Chem 285(1):234-41
Kota P, et al.  (2009) Identification of a consensus motif in substrates bound by a Type I Hsp40. Proc Natl Acad Sci U S A 106(27):11073-8
Nilapwar S, et al.  (2009) Structural-thermodynamic relationships of interactions in the N-terminal ATP-binding domain of Hsp90. J Mol Biol 392(4):923-36
Retzlaff M, et al.  (2009) Hsp90 is regulated by a switch point in the C-terminal domain. EMBO Rep 10(10):1147-53
Tsutsumi S, et al.  (2009) Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain. Nat Struct Mol Biol 16(11):1141-7
Millson SH, et al.  (2008) Chaperone ligand-discrimination by the TPR-domain protein Tah1. Biochem J 413(2):261-8
Johnson JL, et al.  (2007) Nucleotide-dependent interaction of Saccharomyces cerevisiae Hsp90 with the cochaperone proteins Sti1, Cpr6, and Sba1. Mol Cell Biol 27(2):768-76
Scroggins BT, et al.  (2007) An acetylation site in the middle domain of Hsp90 regulates chaperone function. Mol Cell 25(1):151-9
Proisy N, et al.  (2006) Inhibition of Hsp90 with synthetic macrolactones: synthesis and structural and biological evaluation of ring and conformational analogs of radicicol. Chem Biol 13(11):1203-15
Kishimoto J, et al.  (2005) Identification of the pentapeptide constituting a dominant epitope common to all eukaryotic heat shock protein 90 molecular chaperones. Cell Stress Chaperones 10(4):296-311
Jones G, et al.  (2004) Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding. Mol Cell Biol 24(9):3928-37
Kawano T, et al.  (2004) A comprehensive study on the immunological reactivity of the Hsp90 molecular chaperone. J Biochem 136(5):711-22
Lotz GP, et al.  (2003) Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J Biol Chem 278(19):17228-35
Lee HC, et al.  (2002) The molecular chaperone Hsp90 mediates heme activation of the yeast transcriptional activator Hap1. J Biol Chem 277(9):7430-7
Marino-Ramirez L and Hu JC  (2002) Isolation and mapping of self-assembling protein domains encoded by the Saccharomyces cerevisiae genome using lambda repressor fusions. Yeast 19(7):641-50
Matsumoto S, et al.  (2002) Interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 molecular chaperone. J Biol Chem 277(38):34959-66
Abbas-Terki T, et al.  (2001) Hsp104 interacts with Hsp90 cochaperones in respiring yeast. Mol Cell Biol 21(22):7569-75
Scheibel T, et al.  (1998) Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence. Proc Natl Acad Sci U S A 95(4):1495-9
Kimura Y, et al.  (1994) Temperature-sensitive mutants of hsp82 of the budding yeast Saccharomyces cerevisiae. Mol Gen Genet 242(5):517-27