SSE2/YBR169C Literature Guide Help

Other names published for SSE2: YBR169C

SSE2 - Primary Literature (12)

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
Duennwald ML, et al.  (2012) Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 10(6):e1001346
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
Mandal AK, et al.  (2010) Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system. Mol Biol Cell 21(9):1439-48
Polier S, et al.  (2010) Interaction of the Hsp110 Molecular Chaperones from S. cerevisiae with Substrate Protein. J Mol Biol 401(5):696-707
Dragovic Z, et al.  (2006) Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J 25(11):2519-28
Raviol H, et al.  (2006) Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J 25(11):2510-8
Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
Shaner L, et al.  (2004) The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family. J Biol Chem 279(21):21992-2001
Simoes T, et al.  (2003) Adaptation of Saccharomyces cerevisiae to the herbicide 2,4-dichlorophenoxyacetic acid, mediated by Msn2p- and Msn4p-regulated genes: important role of SPI1. Appl Environ Microbiol 69(7):4019-28
Mukai H, et al.  (1993) Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family. Gene 132(1):57-66