Z. Zhang

发表

Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanism of catalysis.

Z. Zhang, Z Y Zhang, Z. Zhang, 1998, Critical reviews in biochemistry and molecular biology.

Active site labeling of the Yersinia protein tyrosine phosphatase: the determination of the pKa of the active site cysteine and the function of the conserved histidine 402.

J. Dixon, J. Dixon, Z. Zhang, 1993, Biochemistry.

Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design.

D S Lawrence, S. Almo, D. Lawrence, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Regulation of PTP1B via glutathionylation of the active site cysteine 215.

P. B. Chock, W. Barrett, Y. Keng, 1999, Biochemistry.

Expression, purification, and physicochemical characterization of a recombinant Yersinia protein tyrosine phosphatase.

J. C. Clemens, J. Dixon, J. Stuckey, 1992, The Journal of biological chemistry.

A continuous spectrophotometric and fluorimetric assay for protein tyrosine phosphatase using phosphotyrosine-containing peptides.

J. Dixon, J. Dixon, Z. Zhang, 1993, Analytical biochemistry.

Dissecting the catalytic mechanism of protein-tyrosine phosphatases.

J. Dixon, J. Dixon, Z. Zhang, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction.

L. Wu, A. Hengge, Z. Zhang, 1995, Biochemistry.

The single sulfur to oxygen substitution in the active site nucleophile of the Yersinia protein-tyrosine phosphatase leads to substantial structural and functional perturbations.

L. Wu, Z. Zhang, 1997, Biochemistry.

A phosphotyrosyl mimetic peptide reverses impairment of insulin-stimulated translocation of GLUT4 caused by overexpression of PTP1B in rat adipose cells.

M. Quon, L. Wu, T. Burke, 1999, Biochemistry.

Probing the function of Asp128 in the lower molecular weight protein-tyrosine phosphatase-catalyzed reaction. A pre-steady-state and steady-state kinetic investigation.

L. Wu, Z. Zhang, L. Wu, 1996, Biochemistry.

A general method for the preparation of internally quenched fluorogenic protease substrates using solid-phase peptide synthesis.

Z. Zhang, L. Maggiora, C. W. Smith, 1992, Journal of medicinal chemistry.

Synthesis and characterization of a novel class of protein tyrosine phosphatase inhibitors.

L. Wu, O. Ibrahimi, Z. Zhang, 2000, Bioorganic & medicinal chemistry letters.

Probing the function of the conserved tryptophan in the flexible loop of the Yersinia protein-tyrosine phosphatase.

L. Wu, Y. Keng, Z. Zhang, 2008, European journal of biochemistry.

Purification and characterization of the low molecular weight protein tyrosine phosphatase, Stp1, from the fission yeast Schizosaccharomyces pombe.

P. Russell, G. Zhou, J. Denu, 1995, Biochemistry.

Cloning, expression, and catalytic mechanism of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart.

Ming-Ming Zhou, Y. Wo, Z. Zhang, 1992, Biochemistry.

Inhibition of protein tyrosine phosphatases by low-molecular-weight S-nitrosothiols and S-nitrosylated human serum albumin.

Z. Zhang, M. Xian, J. Cheng, 2000, Biochemical and biophysical research communications.

Covalent modification and site-directed mutagenesis of an active site tryptophan of human prostatic acid phosphatase.

Z. Zhang, R. V. Van Etten, K. Ostanin, 1997, Acta biochimica Polonica.

Covalent modification and active site-directed inactivation of a low molecular weight phosphotyrosyl protein phosphatase.

Z. Zhang, R. V. Van Etten, J. Davis, 1992, Biochemistry.

Quiescent affinity inactivators of protein tyrosine phosphatases.

Z. Zhang, T. Widlanski, W. P. Taylor, 1996, Bioorganic & medicinal chemistry.

Structure-based design and synthesis of small molecule protein-tyrosine phosphatase 1B inhibitors.

L. Wu, T. Burke, Z. Zhang, 1998, Bioorganic & medicinal chemistry.

Purification and characterization of a low-molecular-weight acid phosphatase--a phosphotyrosyl-protein phosphatase from bovine heart.

Z. Zhang, R. V. Van Etten, R. L. Etten, 1990, Archives of biochemistry and biophysics.

Phospho-Azatyrosine, a less effective protein-tyrosine phosphatase substrate than phosphotyrosine.

L. Wu, T. Burke, A. Otaka, 2001, Bioorganic & medicinal chemistry letters.

Potent inhibition of protein-tyrosine phosphatase-1B using the phosphotyrosyl mimetic fluoro-O-malonyl tyrosine (FOMT).

L. Wu, P. Roller, T. Burke, 1998, Bioorganic & medicinal chemistry letters.

Potent inhibition of protein-tyrosine phosphatase by phosphotyrosine-mimic containing cyclic peptides.

M. Akamatsu, P. Roller, T. Burke, 1997, Bioorganic & medicinal chemistry.

Why is phosphonodifluoromethyl phenylalanine a more potent inhibitory moiety than phosphonomethyl phenylalanine toward protein-tyrosine phosphatases?

L. Wu, P. Roller, J. den Hertog, 1995, Biochemical and biophysical research communications.

Protein tyrosine phosphatases: prospects for therapeutics.

Z. Zhang, Z Y Zhang, Z. Zhang, 2001, Current opinion in chemical biology.

Utilization of a peptide lead for the discovery of a novel PTP1B-binding motif.

L. Wu, T. Burke, Z. Zhang, 2001, Journal of medicinal chemistry.

Low-affinity binding determined by titration calorimetry using a high-affinity coupling ligand: a thermodynamic study of ligand binding to protein tyrosine phosphatase 1B.

Z. Zhang, Y. L. Zhang, Z. Zhang, 1998, Analytical biochemistry.

Quantitative liquid chromatography/mass spectrometry/mass spectrometry warfarin assay for in vitro cytochrome P450 studies.

Y. Wong, Z. Zhang, B. M. King, 2001, Analytical biochemistry.

Protein tyrosine phosphatases: mechanism of catalysis and substrate specificity.

J. Dixon, Z. Zhang, 1994, Advances in enzymology and related areas of molecular biology.

Structure, mechanism, and specificity of protein-tyrosine phosphatases.

Z. Zhang, Z. Zhang, 1997, Current topics in cellular regulation.

Pre-steady-state and steady-state kinetic analysis of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart.

Z. Zhang, R. L. Vanetten, Robert, 1991, The Journal of biological chemistry.

Leaving group dependence and proton inventory studies of the phosphorylation of a cytoplasmic phosphotyrosyl protein phosphatase from bovine heart.

Z. Zhang, R. V. Van Etten, 1991, Biochemistry.

Dissociative inhibition of dimeric enzymes. Kinetic characterization of the inhibition of HIV-1 protease by its COOH-terminal tetrapeptide.

R. Heinrikson, R. Poorman, Z. Zhang, 1991, The Journal of biological chemistry.

Sequence specificity in recognition of the epidermal growth factor receptor by protein tyrosine phosphatase 1B.

D. Mcnamara, E. Dobrusin, S. Decker, 1993, The Journal of biological chemistry.

Transition state and rate-limiting step of the reaction catalyzed by the human dual-specificity phosphatase, VHR.

L. Wu, Z. Zhang, L. Chen, 1995, Biochemistry.

In vitro activation of the transcription factor ISGF3 by interferon alpha involves a membrane-associated tyrosine phosphatase and tyrosine kinase.

J. Dixon, M. David, J. Dixon, 1993, The Journal of biological chemistry.

Zinc inhibition of renin and the protease from human immunodeficiency virus type 1.

A. Tomasselli, I. Reardon, R. Heinrikson, 1991, Biochemistry.

Reactivity of alcohols toward the phosphoenzyme intermediate in the protein-tyrosine phosphatase-catalyzed reaction: probing the transition state of the dephosphorylation step.

Y. Zhao, Z. Zhang, Z Y Zhang, 1996, Biochemistry.

Catalytic function of the conserved hydroxyl group in the protein tyrosine phosphatase signature motif.

L. Wu, Y. Zhao, Y. Zhao, 1995, Biochemistry.

The Cys(X)5Arg catalytic motif in phosphoester hydrolysis.

E. Fauman, J. Dixon, L. Wu, 1994, Biochemistry.

Nature of the rate-determining steps of the reaction catalyzed by the Yersinia protein-tyrosine phosphatase.

J. Dixon, Z. Zhang, W. Malachowski, 1994, The Journal of biological chemistry.

Protein tyrosine phosphatase substrate specificity: size and phosphotyrosine positioning requirements in peptide substrates.

J. Dixon, D. Mcnamara, J. Dixon, 1994, Biochemistry.

Examination of the transition state of the low-molecular mass small tyrosine phosphatase 1. Comparisons with other protein phosphatases.

L. Wu, Y. Zhao, A. Hengge, 1997, Biochemistry.

Substrate specificity of the protein tyrosine phosphatases.

J. Dixon, D. Mcnamara, E. Dobrusin, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Structural basis of plasticity in protein tyrosine phosphatase 1B substrate recognition.

D S Lawrence, S. Almo, D. Lawrence, 2000, Biochemistry.

Effects on general acid catalysis from mutations of the invariant tryptophan and arginine residues in the protein tyrosine phosphatase from Yersinia.

L. Wu, Y. Keng, A. Hengge, 2000, Biochemistry.

Conformational and dynamic changes of Yersinia protein tyrosine phosphatase induced by ligand binding and active site mutation and revealed by H/D exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry.

A G Marshall, M. Emmett, L. Wu, 1998, Biochemistry.

Structure-based discovery of small molecule inhibitors targeted to protein tyrosine phosphatase 1B.

Y. Keng, Z. Luo, Z. Zhang, 2000, Journal of medicinal chemistry.

Small molecule interactions with protein-tyrosine phosphatase PTP1B and their use in inhibitor design.

Xinjian Yan, Bin Ye, D. Barford, 1996, Biochemistry.

Rapid loop dynamics of Yersinia protein tyrosine phosphatases.

Z. Zhang, D. Gottfried, L Wu, 1997, Biochemistry.

Asp129 of low molecular weight protein tyrosine phosphatase is involved in leaving group protonation.

Z. Zhang, E. Harms, R. V. Van Etten, 1994, The Journal of biological chemistry.

Restoration of potent protein-tyrosine phosphatase activity into the membrane-distal domain of receptor protein-tyrosine phosphatase alpha.

J. den Hertog, Y. Keng, Z. Zhang, 1999, Biochemistry.

PTP1B inhibition and antihyperglycemic activity in the ob/ob mouse model of novel 11-arylbenzo[b]naphtho[2,3-d]furans and 11-arylbenzo[b]naphtho[2,3-d]thiophenes.

C. Moxham, Z. Zhang, J. Sredy, 1999, Journal of medicinal chemistry.

Potent and highly selective inhibitors of the protein tyrosine phosphatase 1B.

D. Lawrence, Y. Keng, Z. Zhang, 1999, Biochemistry.

Impaired transition state complementarity in the hydrolysis of O-arylphosphorothioates by protein-tyrosine phosphatases.

D. Herschlag, F. Hollfelder, Y. Keng, 1999, Biochemistry.

VHR and PTP1 protein phosphatases exhibit remarkably different active site specificities toward low molecular weight nonpeptidic substrates.

D. Lawrence, Z. Zhang, L. Chen, 1996, Biochemistry.