HSP10/YOR020C Literature Guide Help

Other names published for HSP10: CPN10, YOR020C

HSP10 - Additional Literature (28)

ReferenceOther Genes Addressed
Bogumil D, et al.  (2012) Chaperones divide yeast proteins into classes of expression level and evolutionary rate. Genome Biol Evol 4(5):618-25
Cap M, et al.  (2012) Cell differentiation within a yeast colony: metabolic and regulatory parallels with a tumor-affected organism. Mol Cell 46(4):436-48
Hodgins-Davis A, et al.  (2012) Abundant gene-by-environment interactions in gene expression reaction norms to copper within Saccharomyces cerevisiae. Genome Biol Evol 4(11):1061-79
Boender LG, et al.  (2011) Extreme calorie restriction and energy source starvation in Saccharomyces cerevisiae represent distinct physiological states. Biochim Biophys Acta 1813(12):2133-44
Valentine SJ, et al.  (2011) Using ion mobility data to improve peptide identification: intrinsic amino acid size parameters. J Proteome Res 10(5):2318-29
Morris RT, et al.  (2010) Ceres: software for the integrated analysis of transcription factor binding sites and nucleosome positions in Saccharomyces cerevisiae. Bioinformatics 26(2):168-74
Lin FM, et al.  (2009) Comparative proteomic analysis of tolerance and adaptation of ethanologenic Saccharomyces cerevisiae to furfural, a lignocellulosic inhibitory compound. Appl Environ Microbiol 75(11):3765-76
Miyakawa I, et al.  (2009) Mitochondrial nucleoids from the yeast Candida parapsilosis: expansion of the repertoire of proteins associated with mitochondrial DNA. Microbiology 155(Pt 5):1558-68
Daigle BJ Jr and Altman RB  (2008) M-BISON: microarray-based integration of data sources using networks. BMC Bioinformatics 9:214
Shen Y, et al.  (2008) Mass spectrometry analysis of proteome-wide proteolytic post-translational degradation of proteins. Anal Chem 80(15):5819-28
Wu WS and Li WH  (2008) Identifying gene regulatory modules of heat shock response in yeast. BMC Genomics 9:439
Miura T, et al.  (2006) Systematic analysis of HSP gene expression and effects on cell growth and survival at high hydrostatic pressure in Saccharomyces cerevisiae. Extremophiles 10(4):279-84
Nosek J, et al.  (2006) Mitochondrial chromosome structure: an insight from analysis of complete yeast genomes. FEMS Yeast Res 6(3):356-70
Reinders J, et al.  (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J Proteome Res 5(7):1543-54
Zahedi RP, et al.  (2006) Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol Biol Cell 17(3):1436-50
Millson SH, et al.  (2005) A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p). Eukaryot Cell 4(5):849-60
Stribinskis V, et al.  (2005) Rpm2p, a component of yeast mitochondrial RNase P, acts as a transcriptional activator in the nucleus. Mol Cell Biol 25(15):6546-58
Suzuki M, et al.  (2005) Single protein production in living cells facilitated by an mRNA interferase. Mol Cell 18(2):253-61
Ichimura T, et al.  (2004) Transcriptomic and proteomic analysis of a 14-3-3 gene-deficient yeast. Biochemistry 43(20):6149-58
Schade B, et al.  (2004) Cold adaptation in budding yeast. Mol Biol Cell 15(12):5492-502
Sickmann A, et al.  (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc Natl Acad Sci U S A 100(23):13207-12
Fang YC and Cheng M  (2002) The effect of C-terminal mutations of HSP60 on protein folding. J Biomed Sci 9(3):223-33
Martin CC, et al.  (2002) Expression and genomic organization of the zebrafish chaperonin gene complex. Genome 45(5):804-11
Landry SJ, et al.  (1999) Chaperonin function depends on structure and disorder in co-chaperonin mobile loops. Pac Symp Biocomput ():520-31
Dubaquie Y, et al.  (1998) Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10. EMBO J 17(20):5868-76
Kawata Y, et al.  (1998) Purification and characterization of chaperonins 60 and 10 from Methylobacillus glycogenes. Cell Stress Chaperones 3(3):200-7
Bramhall EA, et al.  (1997) Identification of amino acid residues at nucleotide-binding sites of chaperonin GroEL/GroES and cpn10 by photoaffinity labeling with 2-azido-adenosine 5'-triphosphate. Eur J Biochem 244(2):627-34
Monzini N, et al.  (1994) Identification and cloning of human chaperonin 10 homologue. Biochim Biophys Acta 1218(3):478-80