HSP82/YPL240C Literature Guide Help

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

HSP82 - Protein Sequence Features (54)

Results: 1 - 30 of 54 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
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
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
Franzosa EA, et al.  (2011) Heterozygous yeast deletion collection screens reveal essential targets of hsp90. PLoS One 6(11):e28211
Hagn F, et al.  (2011) Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53.LID - 10.1038/nsmb.2114 [doi] Nat Struct Mol Biol ()
Hietpas RT, et al.  (2011) Experimental illumination of a fitness landscape. Proc Natl Acad Sci U S A 108(19):7896-901
Laskar S, et al.  (2011) HSP90 Controls SIR2 Mediated Gene Silencing. PLoS One 6(8):e23406
Mollapour M, et al.  (2011) Casein kinase 2 phosphorylation of Hsp90 threonine 22 modulates chaperone function and drug sensitivity. Oncotarget 2(5):407-17
Mollapour M, et al.  (2011) Threonine 22 phosphorylation attenuates hsp90 interaction with cochaperones and affects its chaperone activity. Mol Cell 41(6):672-81
Pullen L and Bolon DN  (2011) Enforced N-domain Proximity Stimulates Hsp90 ATPase Activity and Is Compatible with Function in Vivo. J Biol Chem 286(13):11091-8
Street TO, et al.  (2011) Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone. Mol Cell 42(1):96-105
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
Retzlaff M, et al.  (2010) Asymmetric activation of the hsp90 dimer by its cochaperone aha1. Mol Cell 37(3):344-54
Wayne N, et al.  (2010) Modular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo. J Biol Chem 285(1):234-41
Hainzl O, et al.  (2009) The charged linker region is an important regulator of Hsp90 function. J Biol Chem 284(34):22559-67
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
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
Li J, et al.  (2009) Molecular chaperone Hsp70/Hsp90 prepares the mitochondrial outer membrane translocon receptor Tom71 for preprotein loading. J Biol Chem 284(35):23852-9
Millson SH, et al.  (2009) The Hsp90/Cdc37p chaperone system is a determinant of molybdate resistance in Saccharomyces cerevisiae. Yeast 26(6):339-47
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
Prodromou C, et al.  (2009) Structural basis of the radicicol resistance displayed by a fungal hsp90. ACS Chem Biol 4(4):289-97
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
Wayne N and Bolon DN  (2007) Dimerization of Hsp90 Is Required for in Vivo Function: DESIGN AND ANALYSIS OF MONOMERS AND DIMERS. J Biol Chem 282(48):35386-95
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
Results: 1 - 30 of 54 records
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