Other names published for SSE1: LPG3, MSI3, YPL106C
SSE1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Other Features
- Strains/Constructs
- Techniques and Reagents
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
SSE1 - Strains/Constructs (51)
| Reference | Other 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 | |
| Khosrow-Khavar F, et al. (2012) The yeast ubr1 ubiquitin ligase participates in a prominent pathway that targets cytosolic thermosensitive mutants for degradation. G3 (Bethesda) 2(5):619-28 | |
| Fell GL, et al. (2011) Identification of yeast genes involved in k homeostasis: loss of membrane traffic genes affects k uptake. G3 (Bethesda) 1(1):43-56 | |
| Franzosa EA, et al. (2011) Heterozygous yeast deletion collection screens reveal essential targets of hsp90. PLoS One 6(11):e28211 | |
| 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 | |
| Jaiswal H, et al. (2011) The chaperone network connected to human ribosome-associated complex. Mol Cell Biol 31(6):1160-73 | |
| Konopka CA, et al. (2011) A yeast model for polyalanine-expansion aggregation and toxicity. Mol Biol Cell 22(12):1971-84 | |
| Kryndushkin DS, et al. (2011) Molecular chaperone Hsp104 can promote yeast prion generation. Genetics 188(2):339-48 | |
| 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 | |
| Sun Z, et al. (2011) Molecular Determinants and Genetic Modifiers of Aggregation and Toxicity for the ALS Disease Protein FUS/TLS. PLoS Biol 9(4):e1000614 | |
| Ungar L, et al. (2011) Tor complex 1 controls telomere length by affecting the level of Ku. Curr Biol 21(24):2115-20 | |
| 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 | |
| Koplin A, et al. (2010) A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes. J Cell Biol 189(1):57-68 | |
| Mandal AK, et al. (2010) Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone system. Mol Biol Cell 21(9):1439-48 | |
| Martineau CN, et al. (2010) Swa2p-dependent clathrin dynamics is critical for Flo11p processing and 'Mat' formation in the yeast Saccharomyces cerevisiae. FEBS Lett 584(6):1149-55 | |
| Polier S, et al. (2010) Interaction of the Hsp110 Molecular Chaperones from S. cerevisiae with Substrate Protein. J Mol Biol 401(5):696-707 | |
| Prasad R, et al. (2010) A nucleus-based quality control mechanism for cytosolic proteins. Mol Biol Cell 21(13):2117-27 | |
| 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 | |
| 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) Hsp110 Is a Nucleotide-activated Exchange Factor for Hsp70. J Biol Chem 283(14):8877-84 | |
| 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 | |
| Goeckeler JL, et al. (2008) The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding. FEBS Lett 582(16):2393-6 | |
| Polier S, et al. (2008) Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell 133(6):1068-79 | |
| Sadlish H, et al. (2008) Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS ONE 3(3):e1763 | |
| Shaner L, et al. (2008) The Hsp110 protein chaperone Sse1 is required for yeast cell wall integrity and morphogenesis. Curr Genet 54(1):1-11 | |
| Ando A, et al. (2007) Identification and classification of genes required for tolerance to freeze-thaw stress revealed by genome-wide screening of Saccharomyces cerevisiae deletion strains. FEMS Yeast Res 7(2):244-53 | |
| Fan Q, et al. (2007) The Role of Sse1 in the de Novo Formation and Variant Determination of the [PSI+] Prion. Genetics 177(3):1583-93 | |
| Gasser B, et al. (2007) Transcriptomics-based identification of novel factors enhancing heterologous protein secretion in yeasts. Appl Environ Microbiol 73(20):6499-507 | |
| Kryndushkin D and Wickner RB (2007) Nucleotide Exchange Factors for Hsp70s Are Required for [URE3] Prion Propagation in Saccharomyces cerevisiae. Mol Biol Cell 18(6):2149-54 |




