HSP104/YLL026W Literature Guide Help

Other names published for HSP104: chaperone ATPase HSP104, YLL026W

HSP104 - Protein Physical Properties (18)

ReferenceOther Genes Addressed
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
Franzmann TM, et al.  (2011) Regulatory circuits of the AAA+ disaggregase Hsp104. J Biol Chem 286(20):17992-8001
Zhou C, et al.  (2011) Motility and segregation of hsp104-associated protein aggregates in budding yeast. Cell 147(5):1186-96
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
Sielaff B and Tsai FT  (2010) The M-Domain Controls Hsp104 Protein Remodeling Activity in an Hsp70/Hsp40-Dependent Manner. J Mol Biol 402(1):30-37
Bardill JP, et al.  (2009) Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prion. Prion 3(3):151-60
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
Wendler P, et al.  (2009) Motor mechanism for protein threading through Hsp104. Mol Cell 34(1):81-92
Lum R, et al.  (2008) Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding. J Biol Chem 283(44):30139-50
Schaupp A, et al.  (2007) Processing of proteins by the molecular chaperone hsp104. J Mol Biol 370(4):674-86
Bosl B, et al.  (2005) Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides. J Biol Chem 280(46):38170-6
Grimminger V, et al.  (2004) The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104. J Biol Chem 279(9):7378-83
Lum R, et al.  (2004) Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J Biol Chem 279(28):29139-46
Cashikar AG, et al.  (2002) Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein. Mol Cell 9(4):751-60
Hattendorf DA and Lindquist SL  (2002) Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding. Proc Natl Acad Sci U S A 99(5):2732-7
Hattendorf DA and Lindquist SL  (2002) Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants. EMBO J 21(1-2):12-21
Cavicchioli R and Watson K  (1986) Loss of heat-shock acquisition of thermotolerance in yeast is not correlated with loss of heat-shock proteins. FEBS Lett 207(1):149-52