HSP82/YPL240C Literature Guide Help

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

HSP82 - Non-Fungal Related Genes/Proteins (66)

Results: 1 - 30 of 66 records
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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
Dengjel J, et al.  (2012) Identification of autophagosome-associated proteins and regulators by quantitative proteomic analysis and genetic screens. Mol Cell Proteomics 11(3):M111.014035
Lee CT, et al.  (2012) Dynamics of the regulation of Hsp90 by the co-chaperone Sti1. EMBO J 31(6):1518-28
Mendonca YA and Ramos CH  (2012) Cloning, purification and characterization of a 90kDa heat shock protein from Citrus sinensis (sweet orange). Plant Physiol Biochem 50(1):87-94
Morra G, et al.  (2012) Corresponding Functional Dynamics across the Hsp90 Chaperone Family: Insights from a Multiscale Analysis of MD Simulations. PLoS Comput Biol 8(3):e1002433
Cox MB and Johnson JL  (2011) The role of p23, Hop, immunophilins, and other co-chaperones in regulating Hsp90 function. Methods Mol Biol 787():45-66
Hietpas RT, et al.  (2011) Experimental illumination of a fitness landscape. Proc Natl Acad Sci U S A 108(19):7896-901
Krukenberg KA, et al.  (2011) Conformational dynamics of the molecular chaperone Hsp90. Q Rev Biophys 44(2):229-55
Li J, et al.  (2011) Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. Nat Struct Mol Biol 18(1):61-6
Mollapour M, et al.  (2011) Threonine 22 phosphorylation attenuates hsp90 interaction with cochaperones and affects its chaperone activity. Mol Cell 41(6):672-81
Vallee F, et al.  (2011) Tricyclic series of heat shock protein 90 (Hsp90) inhibitors part I: discovery of tricyclic imidazo[4,5-c]pyridines as potent inhibitors of the Hsp90 molecular chaperone. J Med Chem 54(20):7206-19
Millson SH, et al.  (2010) A simple yeast-based system for analyzing inhibitor resistance in the human cancer drug targets Hsp90alpha/beta. Biochem Pharmacol 79(11):1581-8
Mollapour M, et al.  (2010) Hsp90 phosphorylation, Wee1 and the cell cycle. Cell Cycle 9(12):2310-6
Mollapour M, et al.  (2010) Swe1(Wee1)-Dependent Tyrosine Phosphorylation of Hsp90 Regulates Distinct Facets of Chaperone Function. Mol Cell 37(3):333-343
Rowlands M, et al.  (2010) Detection of the ATPase Activity of the Molecular Chaperones Hsp90 and Hsp72 Using the TranscreenerTM ADP Assay Kit. J Biomol Screen 15(3):279-86
Song H, et al.  (2010) Expression of five AtHsp90 genes in Saccharomyces cerevisiae reveals functional differences of AtHsp90s under abiotic stresses. J Plant Physiol 167(14):1172-1178
Xu X, et al.  (2010) Functional characterization of AtHsp90.3 in Saccharomyces cerevisiae and Arabidopsis thaliana under heat stress. Biotechnol Lett 32(7):979-87
Immormino RM, et al.  (2009) Different poses for ligand and chaperone in inhibitor-bound Hsp90 and GRP94: implications for paralog-specific drug design. J Mol Biol 388(5):1033-42
Krukenberg KA, et al.  (2009) Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide. Protein Sci 18(9):1815-27
Krukenberg KA, et al.  (2009) pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation. J Mol Biol 390(2):278-91
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
Vaughan CK, et al.  (2009) A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s. FEBS J 276(1):199-209
Anandatheerthavarada HK, et al.  (2008) An unusual TOM20/TOM22 bypass mechanism for the mitochondrial targeting of cytochrome P450 proteins containing N-terminal chimeric signals. J Biol Chem 283(28):19769-80
Krukenberg KA, et al.  (2008) Multiple Conformations of E. coli Hsp90 in Solution: Insights into the Conformational Dynamics of Hsp90. Structure 16(5):755-65
Millson SH, et al.  (2008) Chaperone ligand-discrimination by the TPR-domain protein Tah1. Biochem J 413(2):261-8
Sawarkar R, et al.  (2008) Heat shock protein 90 regulates development in Dictyostelium discoideum. J Mol Biol 383(1):24-35
Vaughan CK, et al.  (2008) Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37. Mol Cell 31(6):886-95
Zhang M, et al.  (2008) Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes. EMBO J 27(20):2789-98
Kumar R, et al.  (2007) Three-dimensional structure of heat shock protein 90 from Plasmodium falciparum: molecular modelling approach to rational drug design against malaria. J Biosci 32(3):531-6
Results: 1 - 30 of 66 records
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