SIS1/YNL007C Literature Guide Help

Other names published for SIS1: YNL007C

SIS1 Literature Curation Summary

Curated References for SIS1: 144

Date of last curation: 2013-05-09

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
Shiber A, et al.  (2013) Ubiquitin conjugation triggers misfolded protein sequestration into quality-control foci when Hsp70 chaperone levels are limiting. Mol Biol Cell ()
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
Yang Z, et al.  (2013) Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability. PLoS Genet 9(1):e1003236
Alberti S  (2012) Molecular mechanisms of spatial protein quality control. Prion 6(5):437-42
Bogumil D, et al.  (2012) Chaperones divide yeast proteins into classes of expression level and evolutionary rate. Genome Biol Evol 4(5):618-25
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
Desantis ME, et al.  (2012) Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients. Cell 151(4):778-93
Duennwald ML, et al.  (2012) Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 10(6):e1001346
Figueras MJ, et al.  (2012) Toxoplasma gondii Sis1-like J-domain protein is a cytosolic chaperone associated to HSP90/HSP70 complex. Int J Biol Macromol 50(3):725-33
Fox TD  (2012) Mitochondrial protein synthesis, import, and assembly. Genetics 192(4):1203-34
Jacobson T, et al.  (2012) Arsenite interferes with protein folding and triggers formation of protein aggregates in yeast. J Cell Sci 125(Pt 21):5073-83
Kiktev DA, et al.  (2012) Regulation of chaperone effects on a yeast prion by cochaperone Sgt2. Mol Cell Biol 32(24):4960-70
Li L and Kowal AS  (2012) Environmental regulation of prions in yeast. PLoS Pathog 8(11):e1002973
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
Mathur V, et al.  (2012) Localization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity. Mol Cell Biol 32(1):139-53
Morano KA, et al.  (2012) The response to heat shock and oxidative stress in Saccharomyces cerevisiae. Genetics 190(4):1157-95
Reidy M, et al.  (2012) Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions. Genetics 192(1):185-93
Saibil HR, et al.  (2012) Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures. Proc Natl Acad Sci U S A 109(37):14906-11
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
Truman AW, et al.  (2012) CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progression. Cell 151(6):1308-18
Verghese J, et al.  (2012) Biology of the Heat Shock Response and Protein Chaperones: Budding Yeast (Saccharomyces cerevisiae) as a Model System. Microbiol Mol Biol Rev 76(2):115-58
Wilson DN and Doudna Cate JH  (2012) The structure and function of the eukaryotic ribosome.LID - 10.1101/cshperspect.a011536 [doi]LID - a011536 [pii] Cold Spring Harb Perspect Biol 4(5)
Winkler J, et al.  (2012) Chaperone networks in protein disaggregation and prion propagation. J Struct Biol 179(2):152-60
Cocklin R, et al.  (2011) New insight into the role of the Cdc34 ubiquitin-conjugating enzyme in cell cycle regulation via Ace2 and Sic1. Genetics 187(3):701-15
Furth N, et al.  (2011) Exposure of bipartite hydrophobic signal triggers nuclear quality control of Ndc10 at the endoplasmic reticulum/nuclear envelope. Mol Biol Cell 22(24):4726-39
Geiler-Samerotte KA, et al.  (2011) Misfolded proteins impose a dosage-dependent fitness cost and trigger a cytosolic unfolded protein response in yeast. Proc Natl Acad Sci U S A 108(2):680-5
Gong Y, et al.  (2011) Bioinformatic approach to identify chaperone pathway relationship from large-scale interaction networks. Methods Mol Biol 787():189-203