J
Jian Cao
Researcher at University of California, San Diego
Publications - 15
Citations - 1464
Jian Cao is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Phospholipase & Phospholipase A2. The author has an hindex of 14, co-authored 14 publications receiving 1243 citations. Previous affiliations of Jian Cao include University at Buffalo & University of Maryland Biotechnology Institute.
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Journal ArticleDOI
Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention.
TL;DR: The phospholipase A2 (PLA2) superfamily traces its roots to the identification of lytic actions of snake venom at the end of the 19th century and to the late 1980’s when PLA2-like activities were reported in mammalian cells in contrast to extracellular secreted activities from venom and pancreas.
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Divergence of function in the hot dog fold enzyme superfamily: the bacterial thioesterase YciA.
Zhihao Zhuang,Feng Song,Hong Zhao,Ling Li,Jian Cao,Edward Eisenstein,Osnat Herzberg,Debra Dunaway-Mariano +7 more
TL;DR: It is concluded that YciA is responsible for the efficient, "seemingly" indiscriminant, CoA-regulated hydrolysis of cellular acyl-CoA thioesters in a wide range of bacteria and hypothesize that this activity may support membrane biogenesis.
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Assessing Phospholipase A2 Activity toward Cardiolipin by Mass Spectrometry
TL;DR: It is demonstrated that cardiolipin is a substrate for s PLA2, cPLA2 and iPLA2, but not for Lp-PLA1, and that none of these PLA2s have significant PLA1 activities toward dilyso-cardiolipIn.
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The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis.
TL;DR: The work described in this paper represents the first reported structure-function based analysis of a human hotdog-fold thioesterase and hypothesize that the physiological role of hTHEM2 involves catalysis of the hydrolysis of cytosolic medium-to-long-chain acyl-CoA thioesters.
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Mechanism of 4-chlorobenzoate:coenzyme a ligase catalysis.
TL;DR: A catalytic mechanism is proposed that centers on a small group of key residues (some of which serve in more than one role) and that includes several residues that function in domain alternation that is based on the structure-derived prediction that PP i dissociation must precede the switch from conformation 1 to conformation 2 and therefore CoA binding.