SIS1/YNL007C Literature Guide Help

Other names published for SIS1: YNL007C

SIS1 - Function/Process (32)

Results: 1 - 30 of 32 records
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ReferenceOther Genes Addressed
Duennwald ML, et al.  (2012) Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 10(6):e1001346
Malinovska L, et al.  (2012) Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates. Mol Biol Cell 23(16):3041-56
Reidy M, et al.  (2012) Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions. Genetics 192(1):185-93
Hines JK, et al.  (2011) Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements. Prion 5(4):238-44
Kryndushkin DS, et al.  (2011) Molecular chaperone Hsp104 can promote yeast prion generation. Genetics 188(2):339-48
Morell M, et al.  (2011) Linking amyloid protein aggregation and yeast survival. Mol Biosyst 7(4):1121-8
Shorter J  (2011) The Mammalian disaggregase machinery: hsp110 synergizes with hsp70 and hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS One 6(10):e26319
Walter GM, et al.  (2011) Ordered assembly of heat shock proteins, Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probes. J Biol Chem 286(47):40486-93
Higurashi T, et al.  (2008) Specificity of the J-protein Sis1 in the propagation of 3 yeast prions. Proc Natl Acad Sci U S A 105(43):16596-601
Needham PG and Masison DC  (2008) Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities. Arch Biochem Biophys 478(2):167-74
Shorter J and Lindquist S  (2008) Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. EMBO J 27(20):2712-24
Tipton KA, et al.  (2008) In Vivo Monitoring of the Prion Replication Cycle Reveals a Critical Role for Sis1 in Delivering Substrates to Hsp104. Mol Cell 32(4):584-591
Tutar L and Tutar Y  (2008) Ydj1 but not Sis1 stabilizes Hsp70 protein under prolonged stress in vitro. Biopolymers 89(3):171-4
Aron R, et al.  (2007) J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation. EMBO J 26(16):3794-803
Krzewska J and Melki R  (2006) Molecular chaperones and the assembly of the prion Sup35p, an in vitro study. EMBO J 25(4):822-33
Raviol H, et al.  (2006) Human and yeast Hsp110 chaperones exhibit functional differences. FEBS Lett 580(1):168-74
Fan CY, et al.  (2004) Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function. Mol Biol Cell 15(2):761-73
Lopez N, et al.  (2003) Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ+]. Mol Biol Cell 14(3):1172-81
Kryndushkin DS, et al.  (2002) Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions. J Biol Chem 277(26):23702-8
Qian X, et al.  (2002) Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1. Biochem J 361(Pt 1):27-34
Horton LE, et al.  (2001) The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes. J Biol Chem 276(17):14426-33
Johnson JL and Craig EA  (2001) An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae. J Cell Biol 152(4):851-6
Qian X, et al.  (2001) Cloning, expression, purification and preliminary X-ray crystallographic studies of yeast Hsp40 Sis1 complexed with Hsp70 Ssa1 C-terminal lid domain. Acta Crystallogr D Biol Crystallogr 57(Pt 5):748-50
Sondheimer N, et al.  (2001) The role of Sis1 in the maintenance of the [RNQ+] prion. EMBO J 20(10):2435-42
Krobitsch S and Lindquist S  (2000) Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc Natl Acad Sci U S A 97(4):1589-94
Lisse T and Schwarz E  (2000) Functional specificity of the mitochondrial DnaJ protein, Mdj1p, in Saccharomyces cerevisiae. Mol Gen Genet 263(3):527-34
Sha B, et al.  (2000) The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1. Structure 8(8):799-807
Sha B and Cyr D  (1999) Purification, crystallization and preliminary X-ray crystallographic studies of S. cerevisiae Hsp40 Sis1. Acta Crystallogr D Biol Crystallogr 55(Pt 6):1234-6
Yan W and Craig EA  (1999) The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1. Mol Cell Biol 19(11):7751-8
Lu Z and Cyr DM  (1998) Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1. J Biol Chem 273(43):27824-30
Results: 1 - 30 of 32 records
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