SSA1/YAL005C Literature Guide Help

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

SSA1 - Strains/Constructs (134)

Results: 1 - 30 of 134 records
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ReferenceOther Genes Addressed
Eliyahu E, et al.  (2012) The protein chaperone Ssa1 affects mRNA localization to the mitochondria. FEBS Lett 586(1):64-9
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
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
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
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
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
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
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
Hsieh MT and Chen RH  (2011) Cdc48 and Cofactors Npl4-Ufd1 Are Important for G1 Progression during Heat Stress by Maintaining Cell Wall Integrity in Saccharomyces cerevisiae. PLoS One 6(4):e18988
Jaiswal H, et al.  (2011) The chaperone network connected to human ribosome-associated complex. Mol Cell Biol 31(6):1160-73
Kryndushkin DS, et al.  (2011) Molecular chaperone Hsp104 can promote yeast prion generation. Genetics 188(2):339-48
Morell M, et al.  (2011) Linking amyloid protein aggregation and yeast survival. Mol Biosyst 7(4):1121-8
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
Andreasson C, et al.  (2010) The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110. J Biol Chem 285(16):12445-53
Buck TM, et al.  (2010) The Endoplasmic Reticulum-associated Degradation of the Epithelial Sodium Channel Requires a Unique Complement of Molecular Chaperones. Mol Biol Cell 21(6):1047-58
Delitheos B, et al.  (2010) Histamine modulates the cellular stress response in yeast. Amino Acids 38(4):1219-26
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
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
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
Reidy M and Masison DC  (2010) Sti1 Regulation of Hsp70 and Hsp90 Is Critical for Curing of Saccharomyces cerevisiae [PSI+] Prions by Hsp104. Mol Cell Biol 30(14):3542-52
Tapia H and Morano KA  (2010) Hsp90 nuclear accumulation in quiescence is linked to chaperone function and spore development in yeast. Mol Biol Cell 21(1):63-72
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
Wisen S, et al.  (2010) Binding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40. ACS Chem Biol 5(6):611-22
Results: 1 - 30 of 134 records
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