STI1/YOR027W Literature Guide Help

Other names published for STI1: YOR027W

STI1 - Protein-protein Interactions (31)

Results: 1 - 30 of 31 records
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ReferenceOther Genes Addressed
Armstrong H, et al.  (2012) The Co-Chaperone Hch1 Regulates Hsp90 Function Differently than Its Homologue Aha1 and Confers Sensitivity to Yeast to the Hsp90 Inhibitor NVP-AUY922. PLoS One 7(11):e49322
Lee CT, et al.  (2012) Dynamics of the regulation of Hsp90 by the co-chaperone Sti1. EMBO J 31(6):1518-28
Schmid AB, et al.  (2012) The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. EMBO J 31(6):1506-17
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
Mandal AK, et al.  (2010) Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system. Mol Biol Cell 21(9):1439-48
Mollapour M, et al.  (2010) Swe1(Wee1)-Dependent Tyrosine Phosphorylation of Hsp90 Regulates Distinct Facets of Chaperone Function. Mol Cell 37(3):333-343
Ran F, et al.  (2010) Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway. J Biol Chem 285(18):13850-62
Reidy M and Masison DC  (2010) Sti1 Regulation of Hsp70 and Hsp90 Is Critical for Curing of Saccharomyces cerevisiae [PSI+] Prions by Hsp104. Mol Cell Biol 30(14):3542-52
Retzlaff M, et al.  (2010) Asymmetric activation of the hsp90 dimer by its cochaperone aha1. Mol Cell 37(3):344-54
Hainzl O, et al.  (2009) The charged linker region is an important regulator of Hsp90 function. J Biol Chem 284(34):22559-67
Hessling M, et al.  (2009) Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nat Struct Mol Biol 16(3):287-93
Mir SS, et al.  (2009) Ssd1 is required for thermotolerance and Hsp104-mediated protein disaggregation in Saccharomyces cerevisiae. Mol Cell Biol 29(1):187-200
Ran F, et al.  (2008) Hsp90/Hsp70 Chaperone Machine Regulation of the Saccharomyces MAL-Activator As Determined in Vivo Using Noninducible and Constitutive Mutant Alleles. Genetics 179(1):331-43
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
Flom G, et al.  (2006) Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiae. Genetics 172(1):41-51
Flom G, et al.  (2005) Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae. Curr Genet 47(6):368-80
Millson SH, et al.  (2005) A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p). Eukaryot Cell 4(5):849-60
Song Y and Masison DC  (2005) Independent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1). J Biol Chem 280(40):34178-85
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
Richter K, et al.  (2004) The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J Mol Biol 342(5):1403-13
Siligardi G, et al.  (2004) Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle. J Biol Chem 279(50):51989-98
Richter K, et al.  (2003) Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle. J Biol Chem 278(12):10328-33
Wegele H, et al.  (2003) Sti1 is a novel activator of the Ssa proteins. J Biol Chem 278(28):25970-6
Abbas-Terki T, et al.  (2002) The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically. Biol Chem 383(9):1335-42
Abbas-Terki T, et al.  (2001) Hsp104 interacts with Hsp90 cochaperones in respiring yeast. Mol Cell Biol 21(22):7569-75
Belghazi M, et al.  (2001) Analysis of protein sequences and protein complexes by matrix-assisted laser desorption/ionization mass spectrometry. Proteomics 1(8):946-54
Nathan DF, et al.  (1999) Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation. Proc Natl Acad Sci U S A 96(4):1409-14
Prodromou C, et al.  (1999) Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones. EMBO J 18(3):754-62
Johnson BD, et al.  (1998) Hop modulates Hsp70/Hsp90 interactions in protein folding. J Biol Chem 273(6):3679-86
Chang HC, et al.  (1997) In vivo analysis of the Hsp90 cochaperone Sti1 (p60). Mol Cell Biol 17(1):318-25
Results: 1 - 30 of 31 records
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