L
Li Chung Ma
Researcher at Rutgers University
Publications - 20
Citations - 1874
Li Chung Ma is an academic researcher from Rutgers University. The author has contributed to research in topics: Protein structure & Influenza A virus. The author has an hindex of 15, co-authored 20 publications receiving 1753 citations. Previous affiliations of Li Chung Ma include Center for Advanced Biotechnology and Medicine & Structural Genomics Consortium.
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Journal ArticleDOI
Structures of influenza A proteins and insights into antiviral drug targets
Kalyan Das,James M. Aramini,James M. Aramini,Li Chung Ma,Li Chung Ma,Robert M. Krug,Edward Arnold,Edward Arnold +7 more
TL;DR: The structures of domains of the influenza RNA-dependent RNA polymerase and the nonstructural NS1A protein provide opportunities for targeting these proteins to inhibit viral replication.
Journal ArticleDOI
Cold-shock induced high-yield protein production in Escherichia coli.
Guoliang Qing,Li Chung Ma,Li Chung Ma,Ahmad Khorchid,G. V. T. Swapna,G. V. T. Swapna,Tapas K. Mal,Masanori Takayama,Bing Xia,Sangita Phadtare,Haiping Ke,Thomas Acton,Thomas Acton,Gaetano T. Montelione,Gaetano T. Montelione,Gaetano T. Montelione,Mitsuhiko Ikura,Masayori Inouye,Masayori Inouye +18 more
TL;DR: The unique features of the cspA gene are applied to develop a series of expression vectors, termed pCold vectors, that drive the high expression of cloned genes upon induction by cold-shock, and are highly complementary to the widely used pET vectors.
Journal ArticleDOI
Structural basis for suppression of a host antiviral response by influenza A virus.
Kalyan Das,Li Chung Ma,Rong Xiao,Brian M. Radvansky,James M. Aramini,Li Zhao,Jesper Marklund,Rei-Lin Kuo,Karen Y. Twu,Edward Arnold,Robert M. Krug,Gaetano T. Montelione +11 more
TL;DR: The crystal structure identifies a CPSF30 binding pocket on NS1A comprised of amino acid residues that are highly conserved among human influenza A viruses that is a potential target for antiviral drug development.
Journal ArticleDOI
Structure of antibacterial peptide microcin J25: a 21-residue lariat protoknot.
Marvin J. Bayro,Jayanta Mukhopadhyay,G. V. T. Swapna,Janet Y. Huang,Li Chung Ma,Elena V. Sineva,Philip E. Dawson,Gaetano T. Montelione,Richard H. Ebright +8 more
TL;DR: MccJ25 is the first example of a lariat protoknot involving a backbone-side chain amide linkage, and it is shown that the published covalent and three-dimensional structures are incorrect, and that MCCJ25 in fact is a 21-residue "lariat protoksnot".
Journal ArticleDOI
Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase.
Farhad Forouhar,J. L. Ross Anderson,Christopher G. Mowat,Sergey M. Vorobiev,A. Hussain,Mariam Abashidze,Chiara Bruckmann,Sarah J. Thackray,Jayaraman Seetharaman,Todd Tucker,Rong Xiao,Li Chung Ma,Li Zhao,Thomas Acton,Gaetano T. Montelione,Stephen K Chapman,Liang Tong +16 more
TL;DR: In this paper, structural and biochemical studies of the Xanthomonas campestris TDO and a related protein SO4414 from Shewanella oneidensis were performed.