HSP104/YLL026W Literature Guide Help

Other names published for HSP104: chaperone ATPase HSP104, YLL026W

HSP104 - Cellular Location (19)

ReferenceOther Genes Addressed
Jacobson T, et al.  (2012) Arsenite interferes with protein folding and triggers formation of protein aggregates in yeast. J Cell Sci 125(Pt 21):5073-83
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
Spokoini R, et al.  (2012) Confinement to organelle-associated inclusion structures mediates asymmetric inheritance of aggregated protein in budding yeast. Cell Rep 2(4):738-47
Winkler J, et al.  (2012) Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol 198(3):387-404
Liu B, et al.  (2011) Segregation of protein aggregates involves actin and the polarity machinery. Cell 147(5):959-61
Specht S, et al.  (2011) Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae. J Cell Biol 195(4):617-29
Unal E, et al.  (2011) Gametogenesis eliminates age-induced cellular damage and resets life span in yeast. Science 332(6037):1554-7
Zhou C, et al.  (2011) Motility and segregation of hsp104-associated protein aggregates in budding yeast. Cell 147(5):1186-96
Noree C, et al.  (2010) Identification of novel filament-forming proteins in Saccharomyces cerevisiae and Drosophila melanogaster. J Cell Biol 190(4):541-51
Mir SS, et al.  (2009) Ssd1 is required for thermotolerance and Hsp104-mediated protein disaggregation in Saccharomyces cerevisiae. Mol Cell Biol 29(1):187-200
Izawa S, et al.  (2008) Heat shock and ethanol stress provoke distinctly different responses in 3'-processing and nuclear export of HSP mRNA in Saccharomyces cerevisiae. Biochem J 414(1):111-9
Kaganovich D, et al.  (2008) Misfolded proteins partition between two distinct quality control compartments. Nature 454(7208):1088-95
Tkach JM and Glover JR  (2008) Nucleocytoplasmic Trafficking of the Molecular Chaperone Hsp104 in Unstressed and Heat-Shocked Cells. Traffic 9(1):39-56
Dieppois G, et al.  (2006) Cotranscriptional recruitment to the mRNA export receptor mex67p contributes to nuclear pore anchoring of activated genes. Mol Cell Biol 26(21):7858-70
Tkach JM and Glover JR  (2004) Amino acid substitutions in the C-terminal AAA+ module of Hsp104 prevent substrate recognition by disrupting oligomerization and cause high temperature inactivation. J Biol Chem 279(34):35692-701
Cao F, et al.  (2001) Nuclear aggregation of huntingtin is not prevented by deletion of chaperone Hsp104. Biochim Biophys Acta 1537(2):158-66
Hanninen AL, et al.  (1999) The cytoplasmic chaperone hsp104 is required for conformational repair of heat-denatured proteins in the yeast endoplasmic reticulum. Mol Biol Cell 10(11):3623-32
Kawai R, et al.  (1999) Direct evidence for the intracellular localization of Hsp104 in Saccharomyces cerevisiae by immunoelectron microscopy. Cell Stress Chaperones 4(1):46-53
Fujita K, et al.  (1998) Hsp104 responds to heat and oxidative stress with different intracellular localization in Saccharomyces cerevisiae. Biochem Biophys Res Commun 248(3):542-7