HSP26/YBR072W Literature Guide Help

Other names published for HSP26: YBR072W

HSP26 - Protein Physical Properties (20)

ReferenceOther Genes Addressed
Benesch JL, et al.  (2010) The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated. Chem Biol 17(9):1008-17
Chen J, et al.  (2010) Regions outside the alpha-crystallin domain of the small heat shock protein Hsp26 are required for its dimerization. J Mol Biol 398(1):122-31
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
Franzmann TM, et al.  (2008) Activation of the chaperone hsp26 is controlled by the rearrangement of its thermosensor domain. Mol Cell 29(2):207-16
Mirzaei H and Regnier F  (2008) Protein:protein aggregation induced by protein oxidation. J Chromatogr B Analyt Technol Biomed Life Sci 873(1):8-14
de Godoy LM, et al.  (2008) Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast. Nature 455(7217):1251-4
Ferreira RM, et al.  (2006) Purification and characterization of the chaperone-like Hsp26 from Saccharomyces cerevisiae. Protein Expr Purif 47(2):384-92
Franzmann TM  (2006) Matrix-assisted refolding of oligomeric small heat-shock protein Hsp26. Int J Biol Macromol 39(1-3):104-10
Gomes RA, et al.  (2006) Yeast protein glycation in vivo by methylglyoxal. FEBS J 273(23):5273-87
Cashikar AG, et al.  (2005) A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J Biol Chem 280(25):23869-75
Franzmann TM, et al.  (2005) The activation mechanism of Hsp26 does not require dissociation of the oligomer. J Mol Biol 350(5):1083-93
Haslbeck M, et al.  (2004) Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. EMBO J 23(3):638-49
Stromer T, et al.  (2004) Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: the N-terminal domail is important for oligomer assembly and the binding of unfolding proteins. J Biol Chem 279(12):11222-8
White HE, et al.  (2004) Recognition and separation of single particles with size variation by statistical analysis of their images. J Mol Biol 336(2):453-60
Salusjarvi L, et al.  (2003) Proteome analysis of recombinant xylose-fermenting Saccharomyces cerevisiae. Yeast 20(4):295-314
Stromer T, et al.  (2003) Analysis of the interaction of small heat shock proteins with unfolding proteins. J Biol Chem 278(20):18015-21
Norbeck J and Blomberg A  (1997) Two-dimensional electrophoretic separation of yeast proteins using a non-linear wide range (pH 3-10) immobilized pH gradient in the first dimension; reproducibility and evidence for isoelectric focusing of alkaline (pI > 7) proteins. Yeast 13(16):1519-34
Silva JT, et al.  (1994) On the hsp26 of Saccharomyces cerevisiae. Biochem Mol Biol Int 33(2):211-20
Bentley NJ, et al.  (1992) The small heat-shock protein Hsp26 of Saccharomyces cerevisiae assembles into a high molecular weight aggregate. Yeast 8(2):95-106
Rossi JM and Lindquist S  (1989) The intracellular location of yeast heat-shock protein 26 varies with metabolism. J Cell Biol 108(2):425-39