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Jun Li

University of Texas Southwestern Medical Center

18

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650

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Roles of His[superscript 291]-[alpha] and His[superscript 146]-[beta]; in the Reductive Acylation Reaction Catalyzed by Human Branched-chain [alpha]-Ketoacid Dehydrogenase: Refined Phosphorylation Loop Structure in the Active Site

2015 Journal of Biological Chemistry
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Structural and biochemical characterization of human mitochondrial branched-chain α-ketoacid dehydrogenase phosphatase

2012 Journal of Biological Chemistry
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Combined Inhibition of Janus Kinase 1/2 for the Treatment of JAK2V617F-Driven Neoplasms: Selective Effects on Mutant Cells and Improvements in Measures of Disease Severity

2009 Clinical Cancer Research
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Pivotal role of the C-terminal DW-motif in mediating inhibition of pyruvate dehydrogenase kinase 2 by dichloroacetate

2009 Journal of Biological Chemistry
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Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops.

2008 Structure
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Pyruvate Dehydrogenase Kinase-4 Structures Reveal a Metastable Open Conformation Fostering Robust Core-free Basal Activity

2008 Journal of Biological Chemistry
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The Two Active Sites in Human Branched-chain α-Keto Acid Dehydrogenase Operate Independently without an Obligatory Alternating-site Mechanism

2007 Journal of Biological Chemistry
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Distinct Structural Mechanisms for Inhibition of Pyruvate Dehydrogenase Kinase Isoforms by AZD7545, Dichloroacetate, and Radicicol.

2007 Structure
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Erratum: A versatile conformational switch regulates reactivity in human branched-chain α-ketoacid dehydrogenase (Structure DOI:10.1016/j.str.2006. 03.001)

2006 Structure
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A Versatile Conformational Switch Regulates Reactivity in Human Branched-Chain α-Ketoacid Dehydrogenase

2006 Structure
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Citations (45)