Crystal structures of the disease-causing D444V mutant and the relevant wild type human dihydrolipoamide dehydrogenase

Author:

Szabo Eszter,Mizsei Reka,Wilk Piotr,Zambo Zsofia,Torocsik Beata,Weiss Manfred S.,Adam-Vizi Vera,Ambrus Attila

Funder

Hungarian Academy of Sciences

Hungarian Scientific Research Fund

Hungarian Brain Research Program

EMBO

Fulbright

Bolyai Fellowships

Young Investigator Research Grants of the Semmelweis University

Gedeon Richter Pharmaceuticals PIc

Publisher

Elsevier BV

Subject

Physiology (medical),Biochemistry

Reference53 articles.

1. Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase);Massey;Biochem. J.,1960

2. Multienzyme complexes;Reed;Acc. Chem. Res.,1974

3. Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase—a family of flavoenzyme transhydrogenases;Williams,1992

4. Kinetic model of dihydrolipoamide dehydrogenase from multiple organisms;Moxley;Biophys. J.,2014

5. The identity of diaphorase and lipoyl dehydrogenase;Massey;Biochim. Biophys. Acta,1960

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