SBA1/YKL117W Literature Guide Help

Other names published for SBA1: YKL117W

SBA1 - Primary Literature (23)

ReferenceOther Genes Addressed
Lancaster DL, et al.  (2013) Chaperone proteins select and maintain [PIN+] prion conformations in Saccharomyces cerevisiae. J Biol Chem 288(2):1266-76
Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
Zelin E, et al.  (2012) The p23 molecular chaperone and GCN5 acetylase jointly modulate protein-DNA dynamics and open chromatin status. Mol Cell 48(3):459-70
Echtenkamp FJ, et al.  (2011) Global Functional Map of the p23 Molecular Chaperone Reveals an Extensive Cellular Network. Mol Cell 43(2):229-41
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
Tapia H and Morano KA  (2010) Hsp90 nuclear accumulation in quiescence is linked to chaperone function and spore development in yeast. Mol Biol Cell 21(1):63-72
Cha JY, et al.  (2009) Characterization of orchardgrass p23, a flowering plant Hsp90 cohort protein. Cell Stress Chaperones 14(3):233-43
Godin KS, et al.  (2009) The box H/ACA snoRNP assembly factor Shq1p is a chaperone protein homologous to Hsp90 cochaperones that binds to the Cbf5p enzyme. J Mol Biol 390(2):231-44
Forafonov F, et al.  (2008) p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity. Mol Cell Biol 28(10):3446-56
Toogun OA, et al.  (2007) The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociation. Proc Natl Acad Sci U S A 104(14):5765-70
Ali MM, et al.  (2006) Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440(7087):1013-7
Cox MB and Miller CA 3rd  (2004) Cooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signaling. Cell Stress Chaperones 9(1):4-20
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
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
Donze O, et al.  (2001) The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR. EMBO J 20(14):3771-80
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
Young JC and Hartl FU  (2000) Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. EMBO J 19(21):5930-40
Donze O and Picard D  (1999) Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2 [corrected]. Mol Cell Biol 19(12):8422-32
Knoblauch R and Garabedian MJ  (1999) Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction. Mol Cell Biol 19(5):3748-59
Ouspenski II, et al.  (1999) New yeast genes important for chromosome integrity and segregation identified by dosage effects on genome stability. Nucleic Acids Res 27(15):3001-8
Bohen SP  (1998) Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins. Mol Cell Biol 18(6):3330-9
Fang Y, et al.  (1998) SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins. Mol Cell Biol 18(7):3727-34
Dujon B, et al.  (1994) Complete DNA sequence of yeast chromosome XI. Nature 369(6479):371-8