Other names published for SIS1: YNL007C
SIS1 LITERATURE TOPICS
- Curated Literature
- Additional Literature
- All Curated References
- Primary Literature
- Reviews
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Additional Information
SIS1 - All Curated References (144)
| Reference | Other 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 |





