CPR7/YJR032W Literature Guide Help

Other names published for CPR7: peptidylprolyl isomerase CPR7, YJR032W

CPR7 - Genetic Interactions (21)

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
Kiktev DA, et al.  (2012) Regulation of chaperone effects on a yeast prion by cochaperone Sgt2. Mol Cell Biol 32(24):4960-70
Singh-Babak SD, et al.  (2012) A novel calcineurin-independent activity of cyclosporin A in Saccharomyces cerevisiae. Mol Biosyst 8(10):2575-84
Zuehlke AD and Johnson JL  (2012) Chaperoning the chaperone: a role for the co-chaperone Cpr7 in modulating Hsp90 function in Saccharomyces cerevisiae. Genetics 191(3):805-14
Boettner DR, et al.  (2011) Clathrin light chain directs endocytosis by influencing the binding of the yeast Hip1R homologue, Sla2, to F-actin. Mol Biol Cell 22(19):3699-714
Moosavi B, et al.  (2010) Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI(+)] prion but not for prion propagation. Yeast 27(3):167-79
Lian HY, et al.  (2007) Hsp40 Interacts Directly with the Native State of the Yeast Prion Protein Ure2 and Inhibits Formation of Amyloid-like Fibrils. J Biol Chem 282(16):11931-40
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
Audhya A, et al.  (2004) Genome-wide lethality screen identifies new PI4,5P2 effectors that regulate the actin cytoskeleton. EMBO J 23(19):3747-57
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
Lee P, et al.  (2004) Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase. Mol Biol Cell 15(4):1785-92
Tong AH, et al.  (2004) Global mapping of the yeast genetic interaction network. Science 303(5659):808-13
Bali M, et al.  (2003) The Hsp90 molecular chaperone complex regulates maltose induction and stability of the Saccharomyces MAL gene transcription activator Mal63p. J Biol Chem 278(48):47441-8
Tesic M, et al.  (2003) Functional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae. J Biol Chem 278(35):32692-701
Tong AH, et al.  (2001) Systematic genetic analysis with ordered arrays of yeast deletion mutants. Science 294(5550):2364-8
Dolinski KJ, et al.  (1998) CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90. Mol Cell Biol 18(12):7344-52
Duina AA, et al.  (1998) Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response. J Biol Chem 273(30):18974-8
Marsh JA, et al.  (1998) Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cells. Mol Cell Biol 18(12):7353-9
Dolinski K, et al.  (1997) All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 94(24):13093-8
Duina AA, et al.  (1996) A cyclophilin function in Hsp90-dependent signal transduction. Science 274(5293):1713-5
Zagulski M, et al.  (1995) The sequence of 24.3 kb from chromosome X reveals five complete open reading frames, all of which correspond to new genes, and a tandem insertion of a Ty1 transposon. Yeast 11(12):1179-86