Other names published for HSP104: chaperone ATPase HSP104, YLL026W
HSP104 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
HSP104 - Strains/Constructs (144)
| Reference | Other Genes Addressed |
|---|---|
| D'Angelo F, et al. (2013) A yeast model for amyloid-? aggregation exemplifies the role of membrane trafficking and PICALM in cytotoxicity. Dis Model Mech 6(1):206-16 | |
| Chiva R, et al. (2012) Analysis of low temperature-induced genes (LTIG) in wine yeast during alcoholic fermentation. FEMS Yeast Res 12(7):831-43 | |
| Halfmann R, et al. (2012) Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature 482(7385):363-8 | |
| Helsen CW and Glover JR (2012) Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104). J Biol Chem 287(1):542-56 | |
| Klucevsek KM, et al. (2012) The Paf1 complex subunit Rtf1 buffers cells against the toxic effects of [PSI+] and defects in Rkr1-dependent protein quality control in Saccharomyces cerevisiae. Genetics 191(4):1107-18 | |
| Malinovska L, et al. (2012) Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates. Mol Biol Cell 23(16):3041-56 | |
| Mathur V, et al. (2012) Localization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity. Mol Cell Biol 32(1):139-53 | |
| 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 | |
| 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 | |
| Winkler J, et al. (2012) Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol 198(3):387-404 | |
| Calahan D, et al. (2011) Genetic analysis of desiccation tolerance in Sachharomyces cerevisiae. Genetics 189(2):507-19 | |
| Chang HY, et al. (2011) Genome-wide analysis to identify pathways affecting telomere-initiated senescence in budding yeast. G3 (Bethesda) 1(3):197-208 | |
| Disalvo S, et al. (2011) Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation. Nat Struct Mol Biol 18(4):486-92 | |
| Inoue Y, et al. (2011) Yeast prion protein New1 can break Sup35 amyloid fibrils into fragments in an ATP-dependent manner. Genes Cells 16(5):545-56 | |
| 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 | |
| Kurahashi H, et al. (2011) [PSI(+) ] aggregate enlargement in rnq1 nonprion domain mutants, leading to a loss of prion in yeast. Genes Cells 16(5):576-89 | |
| Liu B, et al. (2011) Segregation of protein aggregates involves actin and the polarity machinery. Cell 147(5):959-61 | |
| Miot M, et al. (2011) Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation. Proc Natl Acad Sci U S A 108(17):6915-20 | |
| Morell M, et al. (2011) Linking amyloid protein aggregation and yeast survival. Mol Biosyst 7(4):1121-8 | |
| Sadeh A, et al. (2011) Fine-tuning of the Msn2/4-mediated yeast stress responses as revealed by systematic deletion of Msn2/4 partners. Mol Biol Cell 22(17):3127-38 | |
| Sweeny EA, et al. (2011) Purification of hsp104, a protein disaggregase.LID - 10.3791/3190 [doi]LID - 3190 [pii] J Vis Exp (55) | |
| Unal E, et al. (2011) Gametogenesis eliminates age-induced cellular damage and resets life span in yeast. Science 332(6037):1554-7 | |
| Ungar L, et al. (2011) Tor complex 1 controls telomere length by affecting the level of Ku. Curr Biol 21(24):2115-20 | |
| Zhou C, et al. (2011) Motility and segregation of hsp104-associated protein aggregates in budding yeast. Cell 147(5):1186-96 | |
| Delitheos B, et al. (2010) Histamine modulates the cellular stress response in yeast. Amino Acids 38(4):1219-26 | |
| Goehler H, et al. (2010) Pathogenic polyglutamine tracts are potent inducers of spontaneous sup35 and rnq1 amyloidogenesis. PLoS One 5(3):e9642 | |
| Lee S, et al. (2010) CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. Proc Natl Acad Sci U S A 107(18):8135-40 | |
| Lee do H and Goldberg AL (2010) Hsp104 is essential for the selective degradation in yeast of polyglutamine expanded ataxin-1 but not most misfolded proteins generally. Biochem Biophys Res Commun 391(1):1056-61 | |
| Ma M and Liu LZ (2010) Quantitative transcription dynamic analysis reveals candidate genes and key regulators for ethanol tolerance in Saccharomyces cerevisiae. BMC Microbiol 10():169 |




