HSP42/YDR171W Literature Guide Help

Other names published for HSP42: YDR171W

HSP42 - Primary Literature (22)

ReferenceOther Genes Addressed
Brownridge P, et al.  (2013) Quantitative analysis of chaperone network throughput in budding yeast. Proteomics 13(8):1276-91
Powis K, et al.  (2013) Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked. J Cell Sci 126(Pt 2):473-83
Duennwald ML, et al.  (2012) Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 10(6):e1001346
Liu IC, et al.  (2012) The histone deacetylase Hos2 forms an Hsp42-dependent cytoplasmic granule in quiescent yeast cells. Mol Biol Cell 23(7):1231-42
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
Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
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
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
Melamed D, et al.  (2008) Yeast translational response to high salinity: global analysis reveals regulation at multiple levels. RNA 14(7):1337-51
Ahner A, et al.  (2007) Small heat-shock proteins select deltaF508-CFTR for endoplasmic reticulum-associated degradation. Mol Biol Cell 18(3):806-14
Haitani Y, et al.  (2006) Rsp5 regulates expression of stress proteins via post-translational modification of Hsf1 and Msn4 in Saccharomyces cerevisiae. FEBS Lett 580(14):3433-8
Haslbeck M  (2006) Recombinant expression and in vitro refolding of the yeast small heat shock protein Hsp42. Int J Biol Macromol 38(2):107-14
Ma C, et al.  (2006) Identification and characterization of a stress-inducible and a constitutive small heat-shock protein targeted to the matrix of plant peroxisomes. Plant Physiol 141(1):47-60
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
Kabir MA, et al.  (2005) Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae. Yeast 22(3):219-39
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
Kandror O, et al.  (2004) Yeast adapt to near-freezing temperatures by STRE/Msn2,4-dependent induction of trehalose synthesis and certain molecular chaperones. Mol Cell 13(6):771-81
Simoes T, et al.  (2003) Adaptation of Saccharomyces cerevisiae to the herbicide 2,4-dichlorophenoxyacetic acid, mediated by Msn2p- and Msn4p-regulated genes: important role of SPI1. Appl Environ Microbiol 69(7):4019-28
Trotter EW, et al.  (2002) Misfolded proteins are competent to mediate a subset of the responses to heat shock in Saccharomyces cerevisiae. J Biol Chem 277(47):44817-25
Puig S and Perez-Ortin JE  (2000) Stress response and expression patterns in wine fermentations of yeast genes induced at the diauxic shift. Yeast 16(2):139-48
Gu J, et al.  (1997) Small heat shock protein suppression of Vpr-induced cytoskeletal defects in budding yeast. Mol Cell Biol 17(7):4033-42
Wotton D, et al.  (1996) Multimerization of Hsp42p, a novel heat shock protein of Saccharomyces cerevisiae, is dependent on a conserved carboxyl-terminal sequence. J Biol Chem 271(5):2717-23