Other names published for SSA2: YG102, Hsp70 family chaperone SSA2, YLL024C
SSA2 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
- Other Topics
- Additional Information
SSA2 - Additional Literature (179)
| Reference | Other 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 | |
| Reidy M, et al. (2013) Schizosaccharomyces pombe Disaggregation Machinery Chaperones Support Saccharomyces cerevisiae Growth and Prion Propagation. Eukaryot Cell 12(5):739-45 | |
| Shiber A, et al. (2013) Ubiquitin conjugation triggers misfolded protein sequestration into quality-control foci when Hsp70 chaperone levels are limiting. Mol Biol Cell () | |
| Shrestha A, et al. (2013) The role of Yca1 in proteostasis. Yca1 regulates the composition of the insoluble proteome. J Proteomics 81():24-30 | |
| Bogumil D, et al. (2012) Chaperones divide yeast proteins into classes of expression level and evolutionary rate. Genome Biol Evol 4(5):618-25 | |
| Dos Santos SC, et al. (2012) Quantitative- and phospho-proteomic analysis of the yeast response to the tyrosine kinase inhibitor imatinib to pharmacoproteomics-guided drug line extension. OMICS 16(10):537-51 | |
| Eliyahu E, et al. (2012) The protein chaperone Ssa1 affects mRNA localization to the mitochondria. FEBS Lett 586(1):64-9 | |
| Jun H, et al. (2012) Comparative proteome analysis of Saccharomyces cerevisiae: A global overview of in vivo targets of the yeast activator protein 1. BMC Genomics 13(1):230 | |
| Kiktev DA, et al. (2012) Regulation of chaperone effects on a yeast prion by cochaperone Sgt2. Mol Cell Biol 32(24):4960-70 | |
| Nagaraj N, et al. (2012) System-wide perturbation analysis with nearly complete coverage of the yeast proteome by single-shot ultra HPLC runs on a bench top Orbitrap. Mol Cell Proteomics 11(3):M111.013722 | |
| Page B and Drouin G (2012) Stronger purifying selection against gene conversions in a pathogenic Saccharomyces cerevisiae strain. Genome 55(12):835-43 | |
| Prasad R, et al. (2012) Biosynthetic mode can determine the mechanism of protein quality control. Biochem Biophys Res Commun 425(3):689-95 | |
| 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 | |
| Tamarit J, et al. (2012) Analysis of oxidative stress-induced protein carbonylation using fluorescent hydrazides. J Proteomics 75(12):3778-88 | |
| Truman AW, et al. (2012) CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progression. Cell 151(6):1308-18 | |
| Wang Y, et al. (2012) The yeast Hsp70 Ssa1 is a sensor for activation of the heat shock response by thiol-reactive compounds. Mol Biol Cell 23(17):3290-8 | |
| Winkler J, et al. (2012) Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol 198(3):387-404 | |
| Alabrudzinska M, et al. (2011) Dipoid-Specific Genome Stability Genes of S. cerevisiae: Genomic Screen Reveals Haploidization as an Escape from Persisting DNA Rearrangement Stress. PLoS One 6(6):e21124 | |
| Becerra M, et al. (2011) Comparative transcriptome analysis of yeast strains carrying slt2, rlm1, and pop2 deletions. Genome 54(2):99-109 | |
| Bell SL, et al. (2011) Expression of a Malarial Hsp70 Improves Defects in Chaperone-Dependent Activities in ssa1 Mutant Yeast. PLoS One 6(5):e20047 | |
| Boender LG, et al. (2011) Extreme calorie restriction and energy source starvation in Saccharomyces cerevisiae represent distinct physiological states. Biochim Biophys Acta 1813(12):2133-44 | |
| Davidson GS, et al. (2011) The proteomics of quiescent and nonquiescent cell differentiation in yeast stationary-phase cultures. Mol Biol Cell 22(7):988-98 | |
| Fang NN, et al. (2011) Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins. Nat Cell Biol 13(11):1344-52 | |
| 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 | |
| Helbig AO, et al. (2011) The diversity of protein turnover and abundance under nitrogen-limited steady-state conditions in Saccharomyces cerevisiae. Mol Biosyst 7(12):3316-26 | |
| Jaiswal H, et al. (2011) The chaperone network connected to human ribosome-associated complex. Mol Cell Biol 31(6):1160-73 | |
| Sanada M, et al. (2011) ROS production and apoptosis induction by formation of Gts1p-mediated protein aggregates. Biosci Biotechnol Biochem 75(8):1546-53 | |
| 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 | |
| Esposito AM and Kinzy TG (2010) The Eukaryotic Translation Elongation Factor 1B{gamma} Has a Non-guanine Nucleotide Exchange Factor Role in Protein Metabolism. J Biol Chem 285(49):37995-8004 |





