Chen-Chen Kan
General Atomics
14 Papers
311 Citations
Chen-Chen Kan is an academic researcher from General Atomics. The author has contributed to research in topics: Kinase activity & MAP2K7. The author has an hindex of 11, co-authored 14 publications.
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Papers
Crystal structure of the kinase domain of human vascular endothelial growth factor receptor 2: a key enzyme in angiogenesis.
Michele Ann Mctigue,John A Wickersham,Chris Pinko,Richard E. Showalter,Camran V Parast,Anna Tempczyk-Russell,Michael R Gehring,Barbara Mroczkowski,Chen-Chen Kan,J. Ernest Villafranca,Krzysztof Appelt +10 more
TL;DR: This VEGFR2 kinase structure provides a target for design of selective anti-angiogenic therapeutic agents and may serve to properly orient the KID for signal transduction.
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Structure of and kinetic channelling in bifunctional dihydrofolate reductase-thymidylate synthase.
Daniel R. Knighton,Chen-Chen Kan,Eleanor F. Howland,Cheryl A. Janson,Zuzana Hostomska,Katherine M. Welsh,David A. Matthews +6 more
TL;DR: The X–ray structure of dihydrofolate reductase–thymidylate synthase from Leishmania major indicates that transfer of diHydro Folate between these sites does not occur by transient binding at both sites but rather by movement of di hydrofolates across the surface of the protein.
202
Implications for Chk1 Regulation: The 1.7 Å Crystal Structure of Human Cell Cycle Checkpoint Kinase Chk1
Ping Chen,Luo Chun,Yali Deng,Kevin Ryan,James Register,Stephen Margosiak,Anna Tempczyk-Russell,Binh Nguyen,Pamela Myers,Karen Lundgren,Chen-Chen Kan,Patrick M O'Connor +11 more
TL;DR: Molecular modeling of the interaction of a Cdc25C peptide with Chk1 has uncovered several conserved residues that are important for substrate selectivity and it is found that the less conserved C-terminal region negatively impacts Chk2 kinase activity.
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Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase
TL;DR: The three-dimensional structure of phosphoribosylglycinamide formyltransferase is a modified doubly wound alpha/beta sheet with flexibility in the active site, including a disordered loop in the apo structure, which is ordered in the ternary complex structure.
102
Single-chain Recombinant Human Cytomegalovirus Protease ACTIVITY AGAINST ITS NATURAL PROTEIN SUBSTRATE AND FLUOROGENIC PEPTIDE SUBSTRATES
Christopher Pinko,Stephen Margosiak,Vanderpool Darin Louis,Jeanine C. Gutowski,Brad Condon,Chen-Chen Kan +5 more
TL;DR: The production of active recombinant single-chain human cytomegalovirus protease in Escherichia coli and development of a continuous assay for this protease are reported, which can detect nM HCMV protease activity.
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