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Recent Publications

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

Li, L., Lok, S., Yu, I., Zhang, Y., Kuhn,R.J., Chen, J., and Rossmann,M.G. (2008) The Flavivirus Precursor Membrane-Envelope Protein Complex:  Structure and Maturation.  Science, 319:1830-1834.[Pubmed]

Diao, J., Zhang, Y., Huibregtse, J.M., Zhou,D., and Chen, J. (2008) Crystal structure of SopA, a Salmonella  effector protein mimicking a eukaryotic ubiquitin ligase.  Nat. Struct. & Mol. Biol.,15(1): 65-70. [Pubmed]

Oldham, M.L., Khare, D., Quiocho, Q.A., Davidson, A.L., and Chen, J.  (2007)  Crystal structure of a catalytic intermediate of the maltose transporter.  Nature, 450: 515-521. [Pubmed]

Yu, I., Oldham, M.L., Zhang, J., and Chen, J.  (2006)  Crystal structure of the SARS coronavirus nucleocapsid protein dimerization domain reveals evolutionary linkage between Corona- and Arteri- viridaes. J Biol Chem., 281: 17134-17139. [Pubmed]

Zhang, Y., Higashide, W.M., McCormck, B.A., Chen, J., and Zhou, D. (2006)  The inflammation-associated Salmonella SopA is a HECT-like E3 ubiquitin ligase. Mol Microbiol., 62(3): 786-93.[Pubmed]

Lu, G., Westbrooks, J.M., Davidson, A. L., and Chen, J. (2005)  ATP hydrolysis is required to reset the ATP-binding cassette dimer into the resting state conformation. Proc. Natl. Acad. Sci. USA, Dec 13; 102(50):17969-17974. [Pubmed]

Yu, I., Gustafson, C. , Diao, J., Burgner, II J.W., Li, Z., Zhang, J., and Chen, J.  (2005)  Recombinant SARS coronavirus nucleocapsid protein forms a dimer through its C-terminal domain.  J Biol Chem., 280: 23280-86. [Pubmed]

Davidson, A. L. and Chen, J. (2005) Flipping Lipids: Is the third time the charm?  Science, 308:963-965. [Pubmed]

Chang, J., Chen, J., and Zhou, D.  (2005)  Delineation and characterization of the actin nucleation and effector translocation activities of Salmonella SipC. Mol Microbiol. 55(5):1379-89. [Pubmed]

Davidson, A. L. and Chen, J.  (2004)  ATP-binding cassette transporters in bacteria. Annu Rev Biochem. 73:241-268. [Pubmed]

Samanta, S., Ayvaz, T., Reyes, M., Shuman, H.A., Chen, J., and Davidson, A.L.  (2003)  Disulfide crosslinking 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. [Pubmed]

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

Earlier Publications

Mao, Y.; J. Chen, J. A. Maynard. B. Zhang, and F. A. Quiocho.  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. [Pubmed]

Chen, J., S. Sharma, F. A. Quiocho, and A. L. Davidson.  2001.  Trapping the transition state of an ABC transporter: evidence for a concerted mechanism of maltose transport.  Proc. Natl. Acad. Sci. USA 98:1525-1530. [Pubmed]

Chen, J., S. J. J. Skehel, and D. C. Wiley.  1999.  N- and C-terminal residues combine in the fusion –pH influenza hemmagglutinin HA2 subunit to form an N cap that terminates the triple-stranded coiled coil.  Proc. Natl. Acad. Sci. USA 96:8967-8972. [Pubmed]

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

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

Chen, J., S. A. Wharton, W. Weissenhorn, L. J. Clader, F. M. Hughson, J. J. Skehel, and D. C. Wiley.  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. USA 92:12205-12209. [Pubmed]