MDJ1/YFL016C Literature Guide Help

Other names published for MDJ1: YFL016C

MDJ1 - Primary Literature (26)

ReferenceOther Genes Addressed
Brownridge P, et al.  (2013) Quantitative analysis of chaperone network throughput in budding yeast. Proteomics 13(8):1276-91
Sukhai MA, et al.  (2013) Lysosomal disruption preferentially targets acute myeloid leukemia cells and progenitors. J Clin Invest 123(1):315-28
Blamowska M, et al.  (2012) Biogenesis of the mitochondrial Hsp70 chaperone. J Cell Biol 199(1):125-35
Goswami AV, et al.  (2012) Enhanced J-protein interaction and compromised protein stability of mtHsp70 variants lead to mitochondrial dysfunction in Parkinson's disease. Hum Mol Genet 21(15):3317-32
Iosefson O, et al.  (2012) Reactivation of protein aggregates by mortalin and Tid1--the human mitochondrial Hsp70 chaperone system. Cell Stress Chaperones 17(1):57-66
Schilke BA, et al.  (2012) Genetic analysis of complex interactions among components of the mitochondrial import motor and translocon in Saccharomyces cerevisiae. Genetics 190(4):1341-53
Suzuki T, et al.  (2012) Lactic-acid stress causes vacuolar fragmentation and impairs intracellular amino-acid homeostasis in Saccharomyces cerevisiae. J Biosci Bioeng 113(4):421-30
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
Fontanesi F, et al.  (2010) Mss51 and ssc1 facilitate translational regulation of cytochrome C oxidase biogenesis. Mol Cell Biol 30(1):245-59
Mapa K, et al.  (2010) The conformational dynamics of the mitochondrial Hsp70 chaperone. Mol Cell 38(1):89-100
Cajo GC, et al.  (2006) The role of the DIF motif of the DnaJ (Hsp40) co-chaperone in the regulation of the DnaK (Hsp70) chaperone cycle. J Biol Chem 281(18):12436-44
Lu B, et al.  (2006) Tid1 isoforms are mitochondrial DnaJ-like chaperones with unique carboxyl termini that determine cytosolic fate. J Biol Chem 281(19):13150-8
Burri L, et al.  (2004) Zim17, a novel zinc finger protein essential for protein import into mitochondria. J Biol Chem 279(48):50243-9
Christensen CA, et al.  (2002) Mitochondrial GFA2 is required for synergid cell death in Arabidopsis. Plant Cell 14(9):2215-32
Tachibana T, et al.  (2002) A novel non-conventional heat shock element regulates expression of MDJ1 encoding a DnaJ homolog in Saccharomyces cerevisiae. J Biol Chem 277(25):22140-6
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
Lisse T and Schwarz E  (2000) Functional specificity of the mitochondrial DnaJ protein, Mdj1p, in Saccharomyces cerevisiae. Mol Gen Genet 263(3):527-34
Duchniewicz M, et al.  (1999) Dual role of the mitochondrial chaperone Mdj1p in inheritance of mitochondrial DNA in yeast. Mol Cell Biol 19(12):8201-10
Kubo Y, et al.  (1999) Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system. J Mol Biol 286(2):447-64
Deloche O, et al.  (1997) Purification and biochemical properties of Saccharomyces cerevisiae Mdj1p, the mitochondrial DnaJ homologue. J Biol Chem 272(45):28539-44
Horst M, et al.  (1997) Sequential action of two hsp70 complexes during protein import into mitochondria. EMBO J 16(8):1842-9
Westermann B and Neupert W  (1997) Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast Saccharomyces cerevisiae. J Mol Biol 272(4):477-83
Prip-Buus C, et al.  (1996) Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation. FEBS Lett 380(1-2):142-6
Westermann B, et al.  (1996) Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins. Mol Cell Biol 16(12):7063-71
Rowley N, et al.  (1994) Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77(2):249-59
Wagner I, et al.  (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J 13(21):5135-45