HSP78/YDR258C Literature Guide Help

Other names published for HSP78: chaperone ATPase HSP78, YDR258C

HSP78 - Primary Literature (20)

ReferenceOther Genes Addressed
Brownridge P, et al.  (2013) Quantitative analysis of chaperone network throughput in budding yeast. Proteomics 13(8):1276-91
Blamowska M, et al.  (2012) Biogenesis of the mitochondrial Hsp70 chaperone. J Cell Biol 199(1):125-35
Sakurai H and Ota A  (2011) Regulation of chaperone gene expression by heat shock transcription factor in Saccharomyces cerevisiae: importance in normal cell growth, stress resistance, and longevity. FEBS Lett 585(17):2744-8
Martinez-Pastor M, et al.  (2010) Adaptive changes of the yeast mitochondrial proteome in response to salt stress. OMICS 14(5):541-52
Sarry JE, et al.  (2007) Analysis of the vacuolar luminal proteome of Saccharomyces cerevisiae. FEBS J 274(16):4287-305
Leidhold C, et al.  (2006) Structure and function of Hsp78, the mitochondrial ClpB homolog. J Struct Biol 156(1):149-64
Lewandowska A, et al.  (2006) Hsp78 chaperone functions in restoration of mitochondrial network following heat stress. Biochim Biophys Acta 1763(2):141-51
von Janowsky B, et al.  (2006) The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress. J Mol Biol 357(3):793-807
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
Germaniuk A, et al.  (2002) A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J Biol Chem 277(31):27801-8
Rottgers K, et al.  (2002) The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix. J Biol Chem 277(48):45829-37
Donalies UE and Stahl U  (2001) Phase-specific gene expression in Saccharomyces cerevisiae, using maltose as carbon source under oxygen-limiting conditions. Curr Genet 39(3):150-5
Krzewska J, et al.  (2001) Importance of two ATP-binding sites for oligomerization, ATPase activity and chaperone function of mitochondrial Hsp78 protein. J Mol Biol 314(4):901-10
Krzewska J, et al.  (2001) Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding. FEBS Lett 489(1):92-6
Riou C, et al.  (1997) Stationary-phase gene expression in Saccharomyces cerevisiae during wine fermentation. Yeast 13(10):903-15
Rospert S, et al.  (1996) Hsp60-independent protein folding in the matrix of yeast mitochondria. EMBO J 15(4):764-74
Schmitt M, et al.  (1996) The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. J Cell Biol 134(6):1375-86
Moczko M, et al.  (1995) The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function. J Mol Biol 254(4):538-43
Schmitt M, et al.  (1995) Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J 14(14):3434-44
Leonhardt SA, et al.  (1993) HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol Cell Biol 13(10):6304-13