SEARCH

SEARCH BY CITATION

References

  • Abbott, C.A., McCaughan, G.W., and Gorrell, M.D. 1999. Two highly conserved glutamic acid residues in the predicted β propeller domain of dipeptidyl peptidase IV are required for its enzyme activity. FEBS Lett. 458: 278284.
  • Aertgeerts, K., Ye, S., Shi, L., Prasad, S.G., Witmer, D., Chi, E., Sang, B.-C., Wijnands, R.A., Webb, D.R., and Swanson, R.V. 2004. N-linked glycosylation of dipeptidyl peptidase IV (CD26): Effects on enzyme activity, homodimer formation, and adenosine deaminase binding. Protein Sci. 13: 145154.
  • Ahren, B. 2000. Autonomic regulation of islet hormone secretion—Implications for health and disease. Diabetologia 43: 393410.
  • Ahren, B., Simonsson, E., Larsson, H., Landin-Olsson, M., Torgeirsson, H., Jansson, P.A., Sandqvist, M., Bavenholm, P., Efendic, S., Eriksson, J.W., et al. 2002. Inhibition of dipeptidyl peptidase IV improves metabolic control over a 4-week study period in type 2 diabetes. Diabetes Care 25: 869875.
  • Ajami, K., Abbott, C.A., Obradovic, M., Gysbers, V., Kahne, T., McCaughan, G.W., and Gorrell, M.D. 2003. Structural requirements for catalysis, expression, and dimerization in the CD26/DPIV gene family. Biochemistry 42: 694701.
  • Balkan, B., Kwasnik, L., Miserendino, R., Holst, J.J., and Li, X. 1999. Inhibition of dipeptidyl peptidase IV with NVP-DPP728 increases plasma GLP-1 (7–36 amide) concentrations and improves oral glucose tolerance in obese Zucker rats. Diabetologia 42: 13241331.
  • Bednarczyk, J.L., Carroll, S.M., Marin, C., and McIntyre, B.W. 1991. Triggering of the proteinase dipeptidyl peptidase IV (CD26) amplifies human T lymphocyte proliferation. J. Cell. Biochem. 46: 206218.
  • Berger, A. and Schechter, I. 1970. Mapping the active site of papain with the aid of peptide substrates and inhibitors. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 257: 249264.
  • Bongers, J., Lambros, T., Ahmad, M., and Heimer, E.P. 1992. Kinetics of dipeptidyl peptidase IV proteolysis of growth hormone-releasing factor and analogs. Biochim. Biophys. Acta 1122: 147153.
  • CCP4 (Collaborative Computational Project 4). 1994. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50: 760763.
  • Deacon, C.F., Hughes, T.E., and Holst, J.J. 1998. Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide 1 in the anesthetized pig. Diabetes 47: 764769.
  • de La Fortelle, E. and Bricogne, G. 1997. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276: 472494.
  • De Meester, I., Vanhoof, G., Hendriks, D., Demuth, H.U., Yaron, A., and Scharpe, S. 1992. Characterization of dipeptidyl peptidase IV (CD26) from human lymphocytes. Clin. Chim. Acta 210: 2334.
  • De Meester, I., Korom, S., Van Damme, J., and Scharpe, S. 1999. CD26, let it cut or cut it down. Immunol. Today 20: 367375.
  • Drucker, D.J. 2003. Therapeutic potential of dipeptidyl peptidase IV inhibitors for the treatment of type 2 diabetes. Expert Opin. Investig. Drugs 12: 87100.
  • Durinx, C., Lambeir, A.M., Bosmans, E., Falmagne, J.B., Berghmans, R., Haemers, A., Scharpe, S., and De Meester, I. 2000. Molecular characterization of dipeptidyl peptidase activity in serum: Soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides. Eur. J. Biochem. 267: 56085613.
  • Engel, M., Hoffmann, T., Wagner, L., Wermann, M., Heiser, U., Kiefersauer, R., Huber, R., Bode, W., Demuth, H.U., and Brandstetter, H. 2003. The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism. Proc. Natl. Acad. Sci. 100: 50635068.
  • Franco, R., Valenzuela, A., Lluis, C., and Blanco, J. 1998. Enzymatic and extraenzymatic role of ecto-adenosine deaminase in lymphocytes. Immunol. Rev. 161: 2742.
  • Fulop, V., Bocskei, Z., and Polgar, L. 1998. Prolyl oligopeptidase: An unusual β-propeller domain regulates proteolysis. Cell 94: 161170.
  • Fulop, V., Szeltner, Z., and Polgar, L. 2000. Catalysis of serine oligopeptidases is controlled by a gating filter mechanism. EMBO Rep. 1: 277281.
  • Ghersi, G., Chen, W., Lee, E.W., and Zukowska, Z. 2001. Critical role of dipeptidyl peptidase IV in neuropeptide Y-mediated endothelial cell migration in response to wounding. Peptides 22: 453458.
  • Gorrell, M.D., Gysbers, V., and McCaughan, G.W. 2001. CD26: A multifunctional integral membrane and secreted protein of activated lymphocytes. Scan. J. Immunol. 54: 249264.
  • Hegen, M., Kameoka, J., Dong, R.P., Morimoto, C., and Schlossman, S.F. 1997. Structure of CD26 (dipeptidyl peptidase IV) and function in human T cell activation. Adv. Exp. Med. Biol. 421: 109116.
  • Hinke, S.A., Pospisilik, J.A., Demuth, H.U., Mannhart, S., Kuhn-Wache, K., Hoffmann, T., Nishimura, E., Pederson, R.A., and McIntosh, C.H. 2000. Dipeptidyl peptidase IV (DPIV/CD26) degradation of glucagon. Characterization of glucagon degradation products and DPIV-resistant analogs. J. Biol. Chem. 275: 38273834.
  • Hiramatsu, H., Kyono, K., Higashiyama, Y., Fukushima, C., Shima, H., Sugiyama, S., Inaka, K., Yamamoto, A., and Shimizu, R. 2003. The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed β-propeller fold. Biochem. Biophys. Res. Commun. 302: 849854.
  • Hosfield, D., Palan, J., Hilgers, M., Scheibe, D., McRee, D.E., and Stevens, R.C. 2003. A fully integrated protein crystallization platform for small-molecule drug discovery. J. Struct. Biol. 142: 207217.
  • Iwaki-Egawa, S., Watanabe, Y., Kikuya, Y., and Fujimoto, Y. 1998. Dipeptidyl peptidase IV from human serum: Purification, characterization, and N-terminal amino acid sequence. J. Biochem. 124: 428433.
  • Kahne, T., Lendeckel, U., Wrenger, S., Neubert, K., Ansorge, S., and Reinhold, D. 1999. Dipeptidyl peptidase IV: A cell surface peptidase involved in regulating T cell growth (review). Int. J. Mol. Med. 4: 315.
  • Kraulis, P.J. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 946950.
  • Lambeir, A.M., Proost, P., Durinx, C., Bal, G., Senten, K., Augustyns, K., Scharpe, S., Van Damme, J., and De Meester, I. 2001a. Kinetic investigation of chemokine truncation by CD26/dipeptidyl peptidase IV reveals a striking selectivity within the chemokine family. J. Biol. Chem. 276: 2983929845.
  • Lambeir, A.M., Durinx, C., Proost, P., Van Damme, J., Scharpe, S., and De Meester, I. 2001b. Kinetic study of the processing by dipeptidyl-peptidase IV/CD26 of neuropeptides involved in pancreatic insulin secretion. FEBS Lett. 507: 327330.
  • Lambeir, A.M., Proost, P., Scharpe, S., and De Meester, I. 2002. A kinetic study of glucagon-like peptide-1 and glucagon-like peptide-2 truncation by dipeptidyl peptidase IV, in vitro. Biochem. Pharmacol. 64: 17531756.
  • Lambeir, A.M., Durinx, C., Scharpe, S., and De Meester, I. 2003. Dipeptidyl-peptidase IV from bench to bedside: An update on structural properties, functions, and clinical aspects of the enzyme DPP IV. Crit. Rev. Clin. Lab. Sci. 40: 209294.
  • Leiting, B., Pryor, K.D., Wu, J.K., Marsilio, F., Patel, R.A., Craik, C.S., Ellman, J.A., Cummings, R.T., and Thornberry, N.A. 2003. Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII. Biochem J. 371: 525532.
  • Leslie, A.G., Powell, H.R., Winter, G., Svensson, O., Spruce, D., McSweeney, S., Love, D., Kinder, S., Duke, E., and Nave, C. 2002. Automation of the collection and processing of X-ray diffraction data—A generic approach. Acta Crystallogr. D Biol. Crystallogr. 58: 19241928.
  • McRee, D.E. 1999. XtalView/Xfit—A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125: 156165.
  • Mentlein, R. 1999. Dipeptidyl-peptidase IV (CD26)—Role in the inactivation of regulatory peptides. Regul. Pept. 85: 924.
  • Mentlein, R., Dahms, P., Grandt, D., and Kruger, R. 1993. Proteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV. Regul. Pept. 49: 133144.
  • Merritt, E.A. and Bacon, D.J.1997. Raster3D: Photorealistic molecular graphics. Methods Enzymol. 277: 505524
  • Morimoto, C. and Schlossman, S.F. 1998. The structure and function of CD26 in the T-cell immune response. Immunol. Rev. 161: 5570.
  • Morrison, M.E., Vijayasaradhi, S., Engelstein, D., Albino, A.P., and Houghton, A.N. 1993. A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase. J. Exp. Med. 177: 11351143.
  • Nardini, M. and Dijkstra, B.W. 1999. α/β hydrolase fold enzymes: The family keeps growing. Curr. Opin. Struct. Biol. 9: 732737.
  • Neer, E.J. and Smith, T.F. 1996. G protein heterodimers: New structures propel new questions. Cell 84: 175178.
  • Oefner, C., D'Arcy, A., Mac Sweeney, A., Pierau, S., Gardiner, R., and Dale, G.E. 2003. High-resolution structure of human apo dipeptidyl peptidase IV/CD26 and its complex with 1-[([2-[(5-iodopyridin-2-yl)amino]-ethyl] amino)-acetyl]-2-cyano-(S)-pyrrolidine. Acta Crystallogr. D Biol. Crystallogr. 59: 12061212.
  • Ogata, S., Misumi, Y., Tsuji, E., Takami, N., Oda, K., and Ikehara, Y. 1992. Identification of the active site residues in dipeptidyl peptidase IV by affinity labeling and site-directed mutagenesis. Biochemistry 31: 25822587.
  • Otwinowski, Z. and Minor, W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307326.
  • Pauly, R.P., Demuth, H.U., Rosche, F., Schmidt, J., White, H.A., Lynn, F., McIntosh, C.H., and Pederson, R.A. 1999. Improved glucose tolerance in rats treated with the dipeptidyl peptidase IV (CD26) inhibitor Ile-thiazolidide. Metabolism 48: 385389.
  • Rasmussen, H.B., Branner, S., Wiberg, F.C., and Wagtmann, N. 2003. Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog. Nat. Struct. Biol. 10: 1925.
  • Sheldrick, G.1998. Direct methods for solving macromolecular structures. Kluwer Academic Publishers, Dordrecht, The Netherlands.
  • Thoma, R., Loffler, B., Stihle, M., Huber, W., Ruf, A., and Hennig, M. 2003. Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV. Structure 11: 947959.
  • Topf, M., Varnai, P., Schofield, C.J., and Richards, W.G. 2002a. Molecular dynamics simulations of the acyl-enzyme and the tetrahedral intermediate in the deacylation step of serine proteases. Proteins 47: 357369.
  • Topf, M., Varnai, P., and Richards, W.G. 2002b. Ab initio QM/MM dynamics simulation of the tetrahedral intermediate of serine proteases: Insights into the active site hydrogen-bonding network. J. Am. Chem. Soc. 124: 1478014788.
  • Wilmouth, R.C., Edman, K., Neutze, R., Wright, P.A., Clifton, I.J., Schneider, T.R., Schofield, C.J., and Hajdu, J. 2001. X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate. Nat. Struct. Biol. 8: 689694.
  • Zhu, L., Tamvakopoulos, C., Xie, D., Dragovic, J., Shen, X., Fenyk-Melody, J.E., Schmidt, K., Bagchi, A., Griffin, P.R., Thornberry, N.A., et al. 2003. The role of dipeptidyl peptidase IV in the cleavage of glucagon family peptides: In vivo metabolism of pituitary adenylate cyclase activating polypeptide-(1–38). J. Biol. Chem. 278: 2241822423.