SSA2/YLL024C Literature Guide Help

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

SSA2 - Strains/Constructs (81)

Results: 1 - 30 of 81 records
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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
Eliyahu E, et al.  (2012) The protein chaperone Ssa1 affects mRNA localization to the mitochondria. FEBS Lett 586(1):64-9
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
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
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
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
Jaiswal H, et al.  (2011) The chaperone network connected to human ribosome-associated complex. Mol Cell Biol 31(6):1160-73
Laxman S and Tu BP  (2011) Multiple TORC1-Associated Proteins Regulate Nitrogen Starvation-Dependent Cellular Differentiation in Saccharomyces cerevisiae. PLoS One 6(10):e26081
Sanada M, et al.  (2011) Inhibition of heat tolerance and nuclear import of gts1p by ssa1p and ssa2p. Biosci Biotechnol Biochem 75(2):323-30
Sharma D and Masison DC  (2011) Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p. Proc Natl Acad Sci U S A 108(33):13665-70
Heck JW, et al.  (2010) Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1. Proc Natl Acad Sci U S A 107(3):1106-11
Juretschke J, et al.  (2010) The Hsp70 chaperone Ssa1 is essential for catabolite induced degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase. Biochem Biophys Res Commun 397(3):447-52
Moosavi B, et al.  (2010) Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI(+)] prion but not for prion propagation. Yeast 27(3):167-79
Prasad R, et al.  (2010) A nucleus-based quality control mechanism for cytosolic proteins. Mol Biol Cell 21(13):2117-27
Ran F, et al.  (2010) Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway. J Biol Chem 285(18):13850-62
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
Mathur V, et al.  (2009) Ssa1 overexpression and [PIN(+)] variants cure [PSI(+)] by dilution of aggregates. J Mol Biol 390(2):155-67
Singh LR and Kruger WD  (2009) Functional Rescue of Mutant Human Cystathionine {beta}-Synthase by Manipulation of Hsp26 and Hsp70 Levels in Saccharomyces cerevisiae. J Biol Chem 284(7):4238-45
Wang RY, et al.  (2009) A key role for heat shock protein 70 in the localization and insertion of tombusvirus replication proteins to intracellular membranes. J Virol 83(7):3276-87
Wang RY, et al.  (2009) A temperature sensitive mutant of heat shock protein 70 reveals an essential role during the early steps of tombusvirus replication. Virology 394(1):28-38
Baranes-Bacher K, et al.  (2008) New interacting partners of the F-box protein Ufo1 of yeast. Yeast 25(10):733-43
Floer M, et al.  (2008) HSP90/70 chaperones are required for rapid nucleosome removal upon induction of the GAL genes of yeast. Proc Natl Acad Sci U S A 105(8):2975-80
Sharma D and Masison DC  (2008) Functionally redundant isoforms of a yeast hsp70 chaperone subfamily have different antiprion effects. Genetics 179(3):1301-11
Han S, et al.  (2007) Cytoplasmic Hsp70 promotes ubiquitination for endoplasmic reticulum-associated degradation of a misfolded mutant of the yeast plasma membrane ATPase, PMA1. J Biol Chem 282(36):26140-9
Liou ST, et al.  (2007) SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae. Cell Stress Chaperones 12(1):59-70
Loovers HM, et al.  (2007) Importance of the hsp70 ATPase domain in yeast prion propagation. Genetics 175(2):621-30
Martineau CN, et al.  (2007) Flo11p-independent control of "mat" formation by hsp70 molecular chaperones and nucleotide exchange factors in yeast. Genetics 177(3):1679-89
Matsumoto R, et al.  (2007) Exploring Novel Function of Yeast Ssa1/2p by Quantitative Profiling Proteomics Using NanoESI-LC-MS/MS. J Proteome Res 6(9):3465-3474
Results: 1 - 30 of 81 records
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