|Title:||Assistant Professor, Biochemistry|
1988 B.S., Wuhan University, China
2001 Ph.D., University of Oklahoma
2002-2003 Postdoctoral Fellow, University of Oklahoma
2003-2004 Postdoctoral Fellow, UT Southwestern Medical Center at Dallas
2004-2009 Postdoctoral Fellow, Brandeis University
Dr. Liu's laboratory primarily employs X-ray crystallography, mechanistic enzymology, and computer simulations to study key protein components involved in bacterial pathogenesis and human metabolic diseases. Current research areas include:
Structural Enzymology of the Quorum-quenching N-Acyl Homoserine Lactone Hydrolases (AHL Lactonases). Focusing on the catalysis, substrate specificity and promiscuous activities of the AHL lactonases, we want to decipher the biological roles played by these metalloenzymes, in particular their roles in quorum-sensing down-regulation and disrupting the quorum-sensing pathways of the competing microorganisms. The obtained knowledge can potentially generate novel methods to combat persistent infections via blocking or disrupting the quorum-sensing pathways of the pathogenic bacteria.
The Virulence Mechanism of Vibrio vulnificus. The hemolytic toxin MARTXVv is an essential virulence factor in V. vulnificus. Through studying the expression, post-translational modification, and the virulence actions of the MARTXVv toxin, we aim to find means that can prevent the deadly blood infection caused by V. vulnificus.
Study of the Key Enzymes in Human Cardiolipin Metabolism. The metabolism of cardiolipin, an "exclusive" mitochondrial lipid, is involved in the pathogenesis of cardiomyopathy and other human metabolic diseases. By studying the catalysis and regulation of the key enzymes in the human cardiolipin synthesis pathways, we hope to elucidate the pathogenic mechanisms at the molecular level and establish potential therapeutic methods for the related metabolic diseases.
Dali Liu, Jessica Momb, Pei W. Thomas, Aaron Moulin, Gregory A. Petsko, Walter Fast, and Dagmar Ringe, "Mechanism of the Quorum-Quenching Lactonase (AiiA) from Bacillus thuringiensis: 1. Product-Bound Structures", (2008) Biochemistry, 47(29): 7706-7714.
Jessica Momb, Canhui Wang, Dali Liu, Pei W. Thomas, Gregory A. Petsko, Hua Guo, Dagmar Ringe and Walter Fast, "Mechanism of the Quorum-Quenching Lactonase (AiiA) from Bacillus thuringiensis: 2. Substrate Modeling and Active Site Mutations", (2008) Biochemistry, 47(29): 7715-7725.
Dali Liu, Pei W. Thomas, Jessica Momb, Quyen Q. Hoang, Gregory A. Petsko, Dagmar Ringe and Walter Fast, "Structure and Specificity of a Quorum-Quenching Lactonase (AiiB) from Agrobacterium tumefaciens", (2007) Biochemistry 46(42): 11789-11799.
Dali Liu, Edwin Pozharski, Bryan W. Lepore, Mengmeng Fu, Richard B. Silverman, Gregory A. Petsko and Dagmar Ringe, "Structural Studies on the Inhibition of E. coli Aspartate Aminotransferase by (S)-4-Amino-4,5-Dihydro-2-Thiophenecarboxylic Acid (SADTA) Reveals 'A Tale of Two Mechanisms'", (2007) Biochemistry 46(37):10517-10527.
Dali Liu, Bryan Lepore, Pei Thomas, Gregory A. Petsko, Walter Fast, and Dagmar Ringe, "Three-Dimensional Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase from Bacillus thuringiensis", (2005) Proc. Natl. Acad. Sci. 16; 102(33): 11882-11887.
William E. Karsten, Dali Liu, Jagannatha Rao, and Paul F. Cook, "A Catalytic Triad Is Responsible for Acid-Base Chemistry in the Ascaris suum NAD-Malic Enzyme", (2005) Biochemistry, 44: 3626-3635.