LPD1/YFL018C Literature Guide Help

Other names published for LPD1: HPD1, dihydrolipoyl dehydrogenase, YFL018C

LPD1 - Protein Sequence Features (9)

ReferenceOther Genes Addressed
Fomenko DE and Gladyshev VN  (2012) Comparative genomics of thiol oxidoreductases reveals widespread and essential functions of thiol-based redox control of cellular processes. Antioxid Redox Signal 16(3):193-201
Brandes N, et al.  (2011) Using quantitative redox proteomics to dissect the yeast redoxome. J Biol Chem 286(48):41893-903
Marino SM, et al.  (2010) Characterization of Surface-Exposed Reactive Cysteine Residues in Saccharomyces cerevisiae. Biochemistry 49(35):7709-21
Marino SM and Gladyshev VN  (2009) A structure-based approach for detection of thiol oxidoreductases and their catalytic redox-active cysteine residues. PLoS Comput Biol 5(5):e1000383
Toyoda T, et al.  (1997) Crystallization of eukaryotic E3, lipoamide dehydrogenase, from yeast, for exhibiting X-ray diffraction beyond 2.5 A resolution, and preliminary structure analysis. J Biochem 121(1):1-4
Branda SS and Isaya G  (1995) Prediction and identification of new natural substrates of the yeast mitochondrial intermediate peptidase. J Biol Chem 270(45):27366-73
Browning KS, et al.  (1988) Nucleotide sequence for yeast dihydrolipoamide dehydrogenase. Proc Natl Acad Sci U S A 85(6):1831-4
Ross J, et al.  (1988) The nucleotide sequence of the LPD1 gene encoding lipoamide dehydrogenase in Saccharomyces cerevisiae: comparison between eukaryotic and prokaryotic sequences for related enzymes and identification of potential upstream control sites. J Gen Microbiol 134(5):1131-9
Roy DJ and Dawes IW  (1987) Cloning and characterization of the gene encoding lipoamide dehydrogenase in Saccharomyces cerevisiae. J Gen Microbiol 133(4):925-33