Structural alterations by five disease-causing mutations in the low-pH conformation of human dihydrolipoamide dehydrogenase (hLADH) analyzed by molecular dynamics - Implications in functional loss and modulation of reactive oxygen species generation by pathogenic hLADH forms

Biochemistry and Biophysics Reports

Volumn 2, Issue , 2015, Pages 50-56

  Ambrus, Attila ^a   Mizsei, Reka ^a   Adam Vizi, Vera ^a  

^a SEMMELWEIS UNIVERSITY   (Hungary)

Author keywords

Lipoamide dehydrogenase; Molecular dynamics; Mutation; Reactive oxygen species

Indexed keywords

DIHYDROLIPOAMIDE DEHYDROGENASE; REACTIVE OXYGEN METABOLITE;

ARTICLE; CONTROLLED STUDY; ENZYME CONFORMATION; MOLECULAR DYNAMICS; MOLECULAR PATHOLOGY; MUTANT; MUTATION; PH; STRUCTURE ANALYSIS; WILD TYPE;

EID: 84937053471     PISSN: None     EISSN: 24055808     Source Type: Journal    
DOI: 10.1016/j.bbrep.2015.04.006     Document Type: Article

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