SSE2/YBR169C Literature Guide Help

Other names published for SSE2: YBR169C

SSE2 - All Curated References (68)

Results: 1 - 30 of 68 records
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ReferenceOther Genes Addressed
Bajwa PK, et al.  (2013) Transcriptional profiling of Saccharomyces cerevisiae T2 cells upon exposure to hardwood spent sulphite liquor: comparison to acetic acid, furfural and hydroxymethylfurfural. Antonie Van Leeuwenhoek ()
Bravim F, et al.  (2013) High hydrostatic pressure activates gene expression that leads to ethanol production enhancement in a Saccharomyces cerevisiae distillery strain. Appl Microbiol Biotechnol 97(5):2093-107
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
Lancaster DL, et al.  (2013) Chaperone proteins select and maintain [PIN+] prion conformations in Saccharomyces cerevisiae. J Biol Chem 288(2):1266-76
Bogumil D, et al.  (2012) Chaperones divide yeast proteins into classes of expression level and evolutionary rate. Genome Biol Evol 4(5):618-25
Duennwald ML, et al.  (2012) Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 10(6):e1001346
Makhnevych T, et al.  (2012) Hsp110 is required for spindle length control. J Cell Biol 198(4):623-36
Morano KA, et al.  (2012) The response to heat shock and oxidative stress in Saccharomyces cerevisiae. Genetics 190(4):1157-95
Muralidharan V, et al.  (2012) Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers. Nat Commun 3():1310
Truman AW, et al.  (2012) CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progression. Cell 151(6):1308-18
Verghese J, et al.  (2012) Biology of the Heat Shock Response and Protein Chaperones: Budding Yeast (Saccharomyces cerevisiae) as a Model System. Microbiol Mol Biol Rev 76(2):115-58
Vizoso-Vazquez A, et al.  (2012) Ixr1p and the control of the Saccharomyces cerevisiae hypoxic response. Appl Microbiol Biotechnol 94(1):173-84
Winkler J, et al.  (2012) Chaperone networks in protein disaggregation and prion propagation. J Struct Biol 179(2):152-60
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
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
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
Rampelt H, et al.  (2011) Nucleotide exchange factors for Hsp70 chaperones. Methods Mol Biol 787():83-91
Costanzo M, et al.  (2010) The genetic landscape of a cell. Science 327(5964):425-31
Grassl J, et al.  (2010) Analysis of the budding yeast pH 4-7 proteome in meiosis. Proteomics 10(3):506-19
Kim JH, et al.  (2010) Oxidative stress studies in yeast with a frataxin mutant: a proteomics perspective. J Proteome Res 9(2):730-6
Mandal AK, et al.  (2010) Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system. Mol Biol Cell 21(9):1439-48
Mira NP, et al.  (2010) Genomic Expression Program Involving the Haa1p-Regulon in Saccharomyces cerevisiae Response to Acetic Acid. OMICS 14(5):587-601
Noree C, et al.  (2010) Identification of novel filament-forming proteins in Saccharomyces cerevisiae and Drosophila melanogaster. J Cell Biol 190(4):541-51
Polier S, et al.  (2010) Interaction of the Hsp110 Molecular Chaperones from S. cerevisiae with Substrate Protein. J Mol Biol 401(5):696-707
Gong Y, et al.  (2009) An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Mol Syst Biol 5:275
Andreasson C, et al.  (2008) Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity. Proc Natl Acad Sci U S A 105(43):16519-24
Kabani M and Martineau CN  (2008) Multiple hsp70 isoforms in the eukaryotic cytosol: mere redundancy or functional specificity? Curr Genomics 9(5):338-248
Perrett S and Jones GW  (2008) Insights into the mechanism of prion propagation. Curr Opin Struct Biol 18(1):52-9
Polier S, et al.  (2008) Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell 133(6):1068-79
Results: 1 - 30 of 68 records
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