SIS1/YNL007C Literature Guide Help

Other names published for SIS1: YNL007C

SIS1 - Primary Literature (49)

Results: 1 - 30 of 49 records
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ReferenceOther Genes Addressed
Brownridge P, et al.  (2013) Quantitative analysis of chaperone network throughput in budding yeast. Proteomics 13(8):1276-91
Powis K, et al.  (2013) Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked. J Cell Sci 126(Pt 2):473-83
Summers DW, et al.  (2013) The Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein. PLoS One 8(1):e52099
Borges JC, et al.  (2012) Identification of regions involved in substrate binding and dimer stabilization within the central domains of yeast Hsp40 Sis1. PLoS One 7(12):e50927
Kiktev DA, et al.  (2012) Regulation of chaperone effects on a yeast prion by cochaperone Sgt2. Mol Cell Biol 32(24):4960-70
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
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
Treusch S and Lindquist S  (2012) An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component. J Cell Biol 197(3):369-79
Hines JK, et al.  (2011) Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements. Prion 5(4):238-44
Hines JK, et al.  (2011) [SWI], the Prion Formed by the Chromatin Remodeling Factor Swi1, Is Highly Sensitive to Alterations in Hsp70 Chaperone System Activity. PLoS Genet 7(2):e1001309
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
Silva JC, et al.  (2011) Central domain deletions affect the SAXS solution structure and function of Yeast Hsp40 proteins Sis1 and Ydj1. BMC Struct Biol 11(1):40
Sahi C, et al.  (2010) Cwc23, an Essential J Protein Critical for Pre-mRNA Splicing with a Dispensable J Domain. Mol Cell Biol 30(1):33-42
Weeks SA, et al.  (2010) A targeted analysis of cellular chaperones reveals contrasting roles for heat shock protein 70 in flock house virus RNA replication. J Virol 84(1):330-9
Douglas PM, et al.  (2009) Reciprocal efficiency of RNQ1 and polyglutamine detoxification in the cytosol and nucleus. Mol Biol Cell 20(19):4162-73
Sharma D, et al.  (2009) Curing of Yeast [URE3] Prion by the Hsp40 Cochaperone Ydj1p Is Mediated by Hsp70. Genetics 181(1):129-37
Douglas PM, et al.  (2008) Chaperone-dependent amyloid assembly protects cells from prion toxicity. Proc Natl Acad Sci U S A 105(20):7206-11
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
Ramos CH, et al.  (2008) Conserved central domains control the quaternary structure of type I and type II Hsp40 molecular chaperones. J Mol Biol 383(1):155-66
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
Sahi C and Craig EA  (2007) Network of general and specialty J protein chaperones of the yeast cytosol. Proc Natl Acad Sci U S A 104(17):7163-8
Li J, et al.  (2006) Crystal structure of yeast Sis1 peptide-binding fragment and Hsp70 Ssa1 C-terminal complex. Biochem J 398(3):353-60
Raviol H, et al.  (2006) Human and yeast Hsp110 chaperones exhibit functional differences. FEBS Lett 580(1):168-74
Aron R, et al.  (2005) In vivo bipartite interaction between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae. Genetics 169(4):1873-82
Gokhale KC, et al.  (2005) Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model. J Biol Chem 280(24):22809-18
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
Results: 1 - 30 of 49 records
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