HSP104/YLL026W Literature Guide Help

Other names published for HSP104: chaperone ATPase HSP104, YLL026W

HSP104 - Protein Processing/Modification/Regulation (26)

ReferenceOther Genes Addressed
Felberbaum R, et al.  (2012) Desumoylation of the endoplasmic reticulum membrane VAP family protein Scs2 by Ulp1 and SUMO regulation of the inositol synthesis pathway. Mol Cell Biol 32(1):64-75
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
Kiktev DA, et al.  (2012) Regulation of chaperone effects on a yeast prion by cochaperone Sgt2. Mol Cell Biol 32(24):4960-70
Park YN, et al.  (2012) Differences in the Curing of [PSI(+)] Prion by Various Methods of Hsp104 Inactivation. PLoS One 7(6):e37692
Frey AG and Eide DJ  (2011) Roles of Two Activation Domains in Zap1 in the Response to Zinc Deficiency in Saccharomyces cerevisiae. J Biol Chem 286(8):6844-54
Geiler-Samerotte KA, et al.  (2011) Misfolded proteins impose a dosage-dependent fitness cost and trigger a cytosolic unfolded protein response in yeast. Proc Natl Acad Sci U S A 108(2):680-5
Jimenez-Marti E, et al.  (2011) Molecular response of Saccharomyces cerevisiae wine and laboratory strains to high sugar stress conditions. Int J Food Microbiol 145(1):211-20
Kim IS, et al.  (2011) Adaptive stress response to menadione-induced oxidative stress in Saccharomyces cerevisiae KNU5377. J Microbiol 49(5):816-23
Newnam GP, et al.  (2011) Destabilization and recovery of a yeast prion after mild heat shock. J Mol Biol 408(3):432-48
Helbig AO, et al.  (2010) Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levels. BMC Genomics 11(1):685
Kim IS, et al.  (2010) A cyclophilin A CPR1 overexpression enhances stress acquisition in Saccharomyces cerevisiae. Mol Cells 29(6):567-74
Lee RE, et al.  (2010) Metacaspase Yca1 is required for clearance of insoluble protein aggregates. Proc Natl Acad Sci U S A 107(30):13348-53
Cheng JS, et al.  (2009) Inoculation-density-dependent responses and pathway shifts in Saccharomyces cerevisiae. Proteomics 9(20):4704-13
Cheng JS, et al.  (2009) Proteomic insights into adaptive responses of Saccharomyces cerevisiae to the repeated vacuum fermentation. Appl Microbiol Biotechnol 83(5):909-23
Lin YY, et al.  (2009) Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis. Cell 136(6):1073-84
Dalley JA, et al.  (2008) Access to ribosomal protein Rpl25p by the signal recognition particle is required for efficient cotranslational translocation. Mol Biol Cell 19(7):2876-84
Seo HY, et al.  (2008) Proteomic Analysis of Recombinant Saccharomyces cerevisiae Upon Iron Deficiency Induced via Human H-Ferritin Production. J Microbiol Biotechnol 18(8):1368-76
Tkach JM and Glover JR  (2008) Nucleocytoplasmic Trafficking of the Molecular Chaperone Hsp104 in Unstressed and Heat-Shocked Cells. Traffic 9(1):39-56
Vianna CR, et al.  (2008) Saccharomyces cerevisiae strains from traditional fermentations of Brazilian cachaca: trehalose metabolism, heat and ethanol resistance. Antonie Van Leeuwenhoek 93(1-2):205-17
Aron R, et al.  (2007) J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation. EMBO J 26(16):3794-803
Loovers HM, et al.  (2007) Importance of the hsp70 ATPase domain in yeast prion propagation. Genetics 175(2):621-30
Makrantoni V, et al.  (2005) Rapid enrichment and analysis of yeast phosphoproteins using affinity chromatography, 2D-PAGE and peptide mass fingerprinting. Yeast 22(5):401-14
Kryndushkin DS, et al.  (2003) Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J Biol Chem 278(49):49636-43
Jung G, et al.  (2002) Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance. Proc Natl Acad Sci U S A 99(15):9936-41
Jung G and Masison DC  (2001) Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions. Curr Microbiol 43(1):7-10
Zhou P, et al.  (1999) The yeast non-Mendelian factor [ETA+] is a variant of [PSI+], a prion-like form of release factor eRF3. EMBO J 18(5):1182-91