Z. Xu publications

Recent Articles

Yang, Z., Vild, C., Ju, J., Zhang, X., Liu, J., Shen, J., Zhao, B., Lan, W., Gong, F., Liu, M., Cao, C., Xu, Z. (2012). Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway. Journal of Biological Chemistry, 287(52):43899-43908. PubMed link

Yang, Z., Shen, J., Zhang, X., Vild, C., Lan, W., Liu, M., Xu, Z., Cao, C. (2012). 1H, 13C and 15N resonance assignments of the N-terminal domain of Vta1-Vps60 peptide complex. Biomolecular NMR Assignments, 1-4. Article in Press.PubMed link

Diao, L., Dong, Q., Xu, Z., Yang, S., Zhou, J., Freudl, R. (2012). Functional implementation of the posttranslational SecB-SecA protein-targeting pathway in Bacillus subtilis. Applied and Environmental Microbiology, 78 (3), 651-659. PubMed link

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

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

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.