SSA2/YLL024C Literature Guide Help

Other names published for SSA2: YG102, Hsp70 family chaperone SSA2, YLL024C

SSA2 - Additional Literature (179)

ReferenceOther 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