SSA1/YAL005C Literature Guide Help

Other names published for SSA1: YG100, Hsp70 family ATPase SSA1, YAL005C

SSA1 - Primary Literature (156)

ReferenceOther Genes Addressed
Brownridge P, et al.  (2013) Quantitative analysis of chaperone network throughput in budding yeast. Proteomics 13(8):1276-91
Eremenko E, et al.  (2013) Aggregation of Human S100A8 and S100A9 Amyloidogenic Proteins Perturbs Proteostasis in a Yeast Model. PLoS One 8(3):e58218
Guerriero CJ, et al.  (2013) Hsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligase. J Biol Chem ()
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
Xu L, et al.  (2013) Using Steered Molecular Dynamics to Predict and Assess Hsp70 Substrate-Binding Domain Mutants that Alter Prion Propagation. PLoS Comput Biol 9(1):e1002896
Xu LQ, et al.  (2013) Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2. Philos Trans R Soc Lond B Biol Sci 368(1617):20110410
Beltrao P, et al.  (2012) Systematic functional prioritization of protein posttranslational modifications. Cell 150(2):413-25
Duennwald ML, et al.  (2012) Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 10(6):e1001346
Eliyahu E, et al.  (2012) The protein chaperone Ssa1 affects mRNA localization to the mitochondria. FEBS Lett 586(1):64-9
Kiktev DA, et al.  (2012) Regulation of chaperone effects on a yeast prion by cochaperone Sgt2. Mol Cell Biol 32(24):4960-70
Makhnevych T, et al.  (2012) Hsp110 is required for spindle length control. J Cell Biol 198(4):623-36
Nowicki L, et al.  (2012) Role of a conserved aspartic acid in nucleotide binding domain 1 (NBD1) of Hsp100 chaperones in their activities. Cell Stress Chaperones 17(3):361-73
Park YN, et al.  (2012) Differences in the Curing of [PSI(+)] Prion by Various Methods of Hsp104 Inactivation. PLoS One 7(6):e37692
Redeker V, et al.  (2012) Identification of protein interfaces between a-synuclein, the principal component of Lewy bodies in Parkinson disease, and the molecular chaperones human Hsc70 and the yeast Ssa1p. J Biol Chem 287(39):32630-9
Schmid AB, et al.  (2012) The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. EMBO J 31(6):1506-17
Shim JS, et al.  (2012) Selective inhibition of HER2-positive breast cancer cells by the HIV protease inhibitor nelfinavir. J Natl Cancer Inst 104(20):1576-90
Stewart-Ornstein J, et al.  (2012) Cellular Noise Regulons Underlie Fluctuations in Saccharomyces cerevisiae. Mol Cell 45(4):483-93
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
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
Braconi D, et al.  (2011) Surfome analysis of a wild-type wine Saccharomyces cerevisiae strain. Food Microbiol 28(6):1220-30
Burtner CR, et al.  (2011) A genomic analysis of chronological longevity factors in budding yeast. Cell Cycle 10(9):1385-96
Hines JK, et al.  (2011) [SWI], the Prion Formed by the Chromatin Remodeling Factor Swi1, Is Highly Sensitive to Alterations in Hsp70 Chaperone System Activity. PLoS Genet 7(2):e1001309
Newnam GP, et al.  (2011) Destabilization and recovery of a yeast prion after mild heat shock. J Mol Biol 408(3):432-48
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
Shorter J  (2011) The Mammalian disaggregase machinery: hsp110 synergizes with hsp70 and hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS One 6(10):e26319
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
Nillegoda NB, et al.  (2010) Ubr1 and ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins. Mol Biol Cell 21(13):2102-16