Publications

Journal

Davidson, A. L, E. Dassa, C. Orelle, and J. Chen. 2008. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol Mol Biol Rev. 72: 317-364.

Diao, J., Zhang, Y., Huibregtse, J. M., Zhou, D., Chen, J. 2008. Crystal structure of SopA, a Salmonella effector protein mimicking a eukaryotic ubiquitin ligase. Nat Struct Mol Biol. 15: 65-70.

Yu, I. M., Zhang, W., Holdaway, H. A., Li, L., Kostyuchenko, V. A., Chipman, P. R., Kuhn, R. J., Rossmann, M. G., Chen, J. 2008. Structure of the immature dengue virus at low pH primes proteolytic maturation. Science. 319: 1834-1837. view article

Li, L., Lok, S. M., Yu, I. M., Zhang, Y., Kuhn, R. J., Chen, J., Rossmann, M. G. 2008. The flavivirus precursor membrane-envelope protein complex: structure and maturation. Science. 319: 1830-1834. view article

Oldham, M. L., Khare, D., Quiocho, F. A., Davidson, A. L., Chen, J. 2007. Crystal structure of a catalytic intermediate of the maltose transporter. Nature. 450: 515-521.

Yu, I. M., Oldham, M. L., Zhang, J., Chen, J. 2006. Crystal structure of the SARS coronavirus nucleocapsid protein dimerization domain reveals evolutionary linkage between Corona- and Arteri- viridae. J Biol Chem.

Zhang, Y., Higashide, W. M., McCormick, B. A., Chen, J., Zhou, D. 2006. The inflammation-associated Salmonella SopA is a HECT-like E3 ubiquitin ligase. Mol Microbiol. 62: 786-793.

Chang, J., Chen, J., Zhou, D. 2005. Delineation and characterization of the actin nucleation and effector translocation activities of Salmonella SipC. Mol Microbiol. 55: 1379-1389.

Davidson, A. L., Chen, J. 2005. Structural biology. Flipping lipids: is the third time the charm?. Science. 308: 963-965.

Lu, G., Westbrooks, J. M., Davidson, A. L., Chen, J. 2005. ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting-state conformation. Proc Natl Acad Sci U S A. 102: 17969-17974.

Yu, I. M., Gustafson, C. L., Diao, J., Burgner, J. W., 2nd, Li, Z., Zhang, J., Chen, J. 2005. Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain. J Biol Chem. 280: 23280-23286.

Davidson, A. L., Chen, J. 2004. ATP-binding cassette transporters in bacteria. Annu Rev Biochem. 73: 241-268.

Chen, J., Lu, G., Lin, J., Davidson, A. L., Quiocho, F. A. 2003. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol Cell. 12: 651-661.

Samanta, S., Ayvaz, T., Reyes, M., Shuman, H. A., Chen, J., Davidson, A. L. 2003. Disulfide cross-linking reveals a site of stable interaction between C-terminal regulatory domains of the two MalK subunits in the maltose transport complex. J Biol Chem. 278: 35265-35271.

Chen, J., Sharma, S., Quiocho, F. A., Davidson, A. L. 2001. Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport. Proc Natl Acad Sci U S A. 98: 1525-1530.

Mao, Y., Chen, J., Maynard, J. A., Zhang, B., Quiocho, F. A. 2001. A novel all helix fold of the AP180 amino-terminal domain for phosphoinositide binding and clathrin assembly in synaptic vesicle endocytosis. Cell. 104: 433-440.

Chen, J., Skehel, J. J., Wiley, D. C. 1999. N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil. Proc Natl Acad Sci U S A. 96: 8967-8972.

Chen, J., Skehel, J. J., Wiley, D. C. 1998. A polar octapeptide fused to the N-terminal fusion peptide solubilizes the influenza virus HA2 subunit ectodomain. Biochemistry. 37: 13643-13649.

Chen, J., Lee, K. H., Steinhauer, D. A., Stevens, D. J., Skehel, J. J., Wiley, D. C. 1998. Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell. 95: 409-417.

Chen, J., Wharton, S. A., Weissenhorn, W., Calder, L. J., Hughson, F. M., Skehel, J. J., Wiley, D. C. 1995. A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation. Proc Natl Acad Sci U S A. 92: 12205-12209.