Chuang, David Te-Chao - UT Southwestern Medical Center

个人简介

Graduate School National Taiwan University - Taiwan (1964) Graduate School Utah State University (1970)

研究领域

Chaperone-mediated biogenesis of mitochondrial multi-enzyme complexes. Molecular genetic and biochemical basis of maple syrup urine disease. Structure and protein-protein interactions of mitochondrial multienzyme complexes.

近期论文

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Brunetti-Pierri, N., Lanpher, B., Erez, A., Ananieva, E.A., Islam, M., C. Marini, J.C., Sun, Q., Yu, C., Hegde. M., Li, J., Wynn, R.M., Chuang, D.T., Hutson, S., and Lee, B. Phenylbutyrate Therapy for Maple Sryup Urine Disease. Human Molecular Genetics, in press. Islam, M. M., Nautiyal, M., Wynn, R.M., Mobley, J. A., Chuang, D. T., and Hutson, S.M. Branched-chain amino acid metabolon: interaction of glutamate dehydrogenase with the mitochondrial branched-chain aminotransferase (BCATm). J. Biol. Chem. 285, 265-276, 2010 Li, J., Kato, M., and Chuang, D. T. Pivotal role of the C-terminal DW-motif in mediating inhibition of pyruvate dehydrogenase kinase 2 by dichloroacetate. J. Biol. Chem. 284, 34458-34467, 2009 Georgiou, T., Chuang, J. L., Wynn, R. M., Stylianidou, G., Korson, M., Chuang, D. T., and Drousiotou, A. Maple syrup urine disease in Cypriot families: identification of three novel mutations and biochemical characterization of the p.Thr211Met mutation in the E1alpha subunit. Genet. Test Mol. Biomarkers. 13, 657-664, 2009 Brautigam, C. A., Wynn, R. M., Chuang, J. L., and Chuang, D. T. Subunit and catalytic-component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex. J. Biol. Chem. In press. Kato, M., Wynn, R. M., Chuang, J. L., Tso, S.-C., Machius, M., Li, J. and Chuang, D. T. Structural Basis for Inactivation of the Human Pyruvate Dehydrogenase Complex by Phosphorylation: Role of Disordered Phosphorylation Loops. Structure, 16, 1849-59, 2008 Faculty of 1000 Biology: evaluations for this article Wynn, R. M., Kato, M., Chuang, J. L., Tso, S.-C., Li, J. and Chuang, D. T. Pyruvate dehydrogenase kinase-4 structures reveal a metastable open conformation fostering robust core-free basal activity. J Biol Chem. 283, 25305-25315, 2008 Faculty of 1000 Biology: evaluations for this article Ludtke, S. J., Baker, M.L., Chen, D.-H., Song, J.-L., Chuang, D.T. and Chiu, W. De Novo Backbone Trace of GroEL from Single Particle Electron Cryomicroscopy. Structure 16, 441-448, 2008 Faculty of 1000 Biology: evaluations for this article Kato, M., Li, J., Chuang, J. L. and Chuang, D. T. Distinct Structural Mechanisms for Inhibition of Pyruvate Dehydrogenase Kinase Isoforms by AZD7545, Dichloroacetate and Radicicol. Structure 15, 992-1004, 2007 Li, J., Machius, M., Chuang, J. L., Wynn, R. M. and Chuang, D. T. The two active sites in human branched-chain α-ketoacid dehydrogenase operate independently without an obligatory alternating-site mechanism. J Biol Chem. 282, 11904-13, 2007 Islam, M. M., Wallin, R., Wynn, R. M. Conway, M., Fujii, H., Mobley, J. A., Chuang, D. T. and Hutson, S. M. A novel branched-chain amino acid metabolon: Protein-protein interactions in a supramolecular complex. J Biol Chem. 282, 11893-903, 2007 Kato, M., Wynn, R. M., Chuang, J. L., Brautigam, C. A., Custorio, M. and Chuang, D. T. A synchronized substrate-gating mechanism revealed by cubic-core structure of the bovine branched-chain α-ketoacid dehydrogenase complex. EMBO J. 25, 5983-5994, 2006 Chen, D.-H., Song, J.-L., Chuang, D. T., Chiu, W. and Ludtke, S. J. An Expanded Conformation of Single-Ring GroEL-GroES Complex Encapsulates an 86 kDa Substrate. Structure, 14, 1711-1722, 2006 Chang, C. F., Chou, H. T., Lin, Y. J., Lee, S. J., Chuang, J. L., Chuang, D. T. and Huang, T. H. Structure of the subunit binding domain and dynamics of the di-domain region from the core of human branched-chain α-ketoacid dehydrogenase complex. J. Biol. Chem. 281, 28345-353, 2006 Tso, C.-S., Kato, M., Chuang, J. L. and Chuang, D. T. Structural determinants for cross-talk between pyruvate dehydrogenase kinase 3 and lipoyl domain 2 of the human pyruvate dehydrogenase complex. J. Biol. Chem. 281, 27197–204, 2006 Brautigam, C. A., Wynn, R. M., Chuang, J. L., Machius, M., Tomchick, D. R. and Chuang, D. T. Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex. Structure 14, 611-21. Machius, M., Wynn, R. M., Chuang, J. L., Li, J., Kluger, R., Yu, D., Tomchick, D. R., Brautigam, C. A. and Chuang, D. T. A versatile conformational switch regulates reactivity in human branched-chain α-ketoacid dehydrogenase. Structure 14, 287-298. Chuang, D. T., Chuang, J. L. and Wynn, R. M. Lessons from genetic disorders of branched-chain amino acid metabolism. J Nutr 136, 243S-9S. Brautigam, C. A., Chuang, J. L., Tomchick, D. R., Machius, M. and Chuang, D. T. Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations. J. Mol. Biol. 350, 543-552, 2005 Kato, M., Chuang, J. L., Tso, C.-S., Wynn, R. M. and Chuang, D. T. Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex. EMBO J. 24, 1763-1774, 2005 Faculty of 1000 Biology: evaluations for this article