Publications
Recent Articles | Articles (1991-2003) | Review Articles
Recent Articles
Chen, X.-W., Leto, D., Xiao, J., Goss, J., Wang, Q., Shavit, J. A., Xiong, T., Yu, G., Ginsburg, D., Toomre, D., Xu, Z., and Saltiel, A. R. (2011) Exocyst function is regulated by effector phosphorylation. Nat. Cell Biol., 13, 580-588. PubMed Link
Quan, S., Koldewey, P., Tapley, T., Kirsch, N., Ruane, K.M., Pfizenmaier, J., Shi, R., Hofmann, S., Foit, L., Ren, G., Jakob, U., Xu, Z., Cygler, M., and Bardwell, J.C. (2011) Genetric selection designed to stabilize proteins uncovers a chaperone called Spy. Nat. Struct Mol Biol., 18, 262-269. PubMed Link
Xiao, J., Chen, X.-W., Davies, B. A., Saltiel, A. R., Katzmann, D. J., and Xu, Z. (2009) Structural basis of Ist1 function and Ist1-Did2 interaction in the MVB pathway and cytokinesis. Mol Biol Cell, 20, 3514-3524. Pubmed link
Ren, G., Stephan, D., Xu, Z., Zheng, Y., Tang, D., Harrison, R. S., Kurz, M., Jarrott, R., Shouldice, S. R., Hiniker, A., Martin, J. L., Heras, B., Bardwell, J. C. (2009) Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue. J. Biol. Chem., 284, 10150-10159. Pubmed link
Lai, L., Xu, Z.*, Zhou, J., Lee, K. D., and Amidon, G. L. (2008) Molecular basis of prodrug activation by human valacyclovirase, an alpha-amino acid ester hydrolase. J. Biol. Chem., 283, 9318-9327. (*co-corresponding author) Pubmed link
Azmi, I., Davies, B. A., Xiao, J., Babst, M., Xu, Z., and Katzmann (2008) ESCRT-III family members stimulate Vps4 ATPase activity or via Vta1. Dev. Cell, 14, 50-61. Pubmed link
Xiao, J., Xia, H., Zhou, J., Azmi, I., Davies, B. A., Katzmann, D. J., and Xu, Z. (2008) Structural basis of Vta1 function in the multi-vesicular body sorting pathway. Dev. Cell, 14, 37-49. Pubmed link
Xiao, J., Xia, H., Yoshino-Koh, K., Zhou, J., and Xu, Z. (2007) Structural characterization of the ATPase reaction cycle of endosomal AAA-protein Vps4. J. Mol. Biol, 374, 655-670. Pubmed link
Moore, B. A., Robinson, H. H., and Xu, Z. (2007) The crystal structure of mouse Exo70 reveals unique features of the mammalian exocyst. J. Mol. Biol., 371, 410-421. Pubmed link
Zhang, H. L., Kim, J. K., Edwards, C. A., Xu, Z. H., Taichman, R., & Wang, C. Y. (2005). Clusterin inhibits apoptosis by interacting with activated Bax. Nature Cell Biology, 7, 909-915. PubMed Link
Collet, J. F., Peisach, D., Bardwell, J. C. A., & Xu, Z. H. (2005). The crystal structure of TrxA(CACA): Insights into the formation of a [2Fe-2S] iron-sulfur cluster in an Escherichia coli thioredoxin mutant. Protein Science, 14, 1863-1869. PubMed Link
Song, Y., Peisach, D., Pioszak, A. A., Xu, Z. H., & Ninfa, A. J. (2004). Crystal structure of the c-terminal domain of the two-component system W transmitter protein nitrogen regulator II (NRII; NtrB), regulator of nitrogen assimilation in Escherichia coli. Biochemistry, 43, 6670-6678. PubMed Link
Zhu, M. F., Shao, F., Innes, R. W., Dixon, J. E., & Xu, Z. H. (2004). The crystal structure of Pseudomonas avirulence protein AvrPphB: A papain-like fold with a distinct substrate-binding site. Proceedings of the National Academy of Sciences of the USA, 101, 302-307. PubMed Link
Ludlam, A. V., Moore, B. A., & Xu, Z. H. (2004). The crystal structure of ribosomal chaperone trigger factor from Vibrio cholerae. Proceedings of the National Academy of Sciences of the USA, 101, 13436-13441. PubMed Link
- back to top -
Articles (1991-2003)
Liu, C. Y., Xu, Z. H., & Kaufman, R. J. (2003). Structure and intermolecular interactions of the luminal dimerization domain of human IRE1 alpha. Journal of Biological Chemistry, 278, 17680-17687. PubMed Link
Zhou, J. H., & Xu, Z. H. (2003). Structural determinants of SecB recognition by SecA in bacterial protein translocation. Nature Structural Biology, 10, 942-947. PubMed Link
Peisach, D., Gee, P., Kent, C., & Xu, Z. H. (2003). The crystal structure of choline kinase reveals a eukaryotic protein kinase fold. Structure, 11, 703-713. PubMed Link
Ma, J. P., Sigler, P. B., Xu, Z. H., & Karplus, M. (2000). A dynamic model for the allosteric mechanism of GroEL. Journal of Molecular Biology, 302, 303-313. PubMed Link
Xu, Z. H., Knafels, J. D., & Yoshino, K. (2000). Crystal structure of the bacterial protein export chaperone SecB. Nature Structural Biology, 7, 1172-1177. PubMed Link
Orth, K., Xu, Z. H., Mudgett, M. B., Bao, Z. Q., Palmer, L. E., Bliska, J. B., Mangel, W. F., Staskawicz, B., & Dixon, J. E. (2000). Disruption of signaling by Yersinia effector YopJ, a ubiquitin-like protein protease. Science, 290, 1594-1597. PubMed Link
Xu, Z. H., & Sigler, P. B. (1998). GroEL/GroES: Structure and function of a two-stroke folding machine. Journal of Structural Biology, 124, 129-141. PubMed Link
Xu, Z. H., Horwich, A. L., & Sigler, P. B. (1997). The crystal structure of the asymmetric GroEL-GroES-(ADP)(7) chaperonin complex. Nature, 388, 741-750. PubMed Link
Rye, H. S., Burston, S. G., Fenton, W. A., Beechem, J. M., Xu, Z. H., Sigler, P. B., & Horwich, A. L. (1997). Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature, 388, 792-798. PubMed Link
Xu, Z. H., Bernlohr, D. A., & Banaszak, L. J. (1993). The adipocyte lipid-binding protein at 1.6A resolution - Crystal structures of the apoprotein and with bound saturated and unsaturated fatty acids. Journal of Biological Chemistry, 268, 7874-7884. PubMed Link
Sha, R. S., Kane, C. D., Xu, Z. H., Banaszak, L. J., & Bernlohr, D. A. (1993). Modulation of ligand-binding affinity of the adipocyte lipid-binding protein by selective mutation - Analysis in vitro and in situ. Journal of Biological Chemistry, 268, 7885-7892. PubMed Link
Xu, Z. H., Bernlohr, D. A., & Banaszak, L. J. (1992). Crystal structure of recombinant murine adipocyte lipid-binding protein. Biochemistry, 31, 3484-3492. PubMed Link
Buelt, M. K., Xu, Z. H., Banaszak, L. J., & Bernlohr, D. A. (1992). Structural and functional characterization of the phosphorylated adipocyte lipid-binding protein (PP15). Biochemistry, 31, 3493-3499. PubMed Link
Xu, Z. H., Buelt, M. K., Banaszak, L. J., & Bernlohr, D. A. (1991). Expression, purification, and crystallization of the adipocyte lipid-binding protein. Journal of Biological Chemistry, 266, 14367-14370. PubMed Link
- back to top -
Review Articles
Zhou, J. H., & Xu, Z. H. (2005). The structural view of bacterial translocation-specific chaperone SecB: Implications for function. Molecular Microbiology, 58, 349-357.
Sigler, P. B., Xu, Z. H., Rye, H. S., Burston, S. G., Fenton, W. A., & Horwich, A. L. (1998). Structure and function in GroEL-mediated protein folding. Annual Review of Biochemistry, 67, 581-608.
Banaszak, L., Winter, N., Xu, Z. H., Bernlohr, D. A., Cowan, S., & Jones, T. A. (1994). Lipid-binding proteins - A family of fatty acid and retinoid transport proteins. Advances in Protein Chemistry, 45, 89-151.
- back to top -
