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Volumn 66, Issue 3, 2010, Pages 271-277

Thiacalix[4]arene as molecular platform for design of alkaline phosphatase inhibitors

Author keywords

Alkaline phosphatase; Calix 4 arene; Inhibition; Molecular docking; Phosphonic acid; Thiacalix 4 arene

Indexed keywords


EID: 77952292132     PISSN: 09230750     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10847-009-9607-9     Document Type: Article
Times cited : (19)

References (31)
  • 1
    • 1542690351 scopus 로고
    • Phosphonates as analogues of natural phosphates
    • Engel, R.: Phosphonates as analogues of natural phosphates. Chem. Rev. 77, 349-367 (1977).
    • (1977) Chem. Rev. , vol.77 , pp. 349-367
    • Engel, R.1
  • 6
    • 13444271786 scopus 로고    scopus 로고
    • Alternative bisphosphonate targets and mechanisms of action
    • Bukowski, J. F., Dascher, C. C., Das, H.: Alternative bisphosphonate targets and mechanisms of action. Biochem. Biophys. Res. Commun. 328, 746-750 (2005).
    • (2005) Biochem. Biophys. Res. Commun. , vol.328 , pp. 746-750
    • Bukowski, J.F.1    Dascher, C.C.2    Das, H.3
  • 8
    • 33644784660 scopus 로고    scopus 로고
    • Calix[4]arene α-aminophosphonic acids: Asymmetric synthesis and enantioselective inhibition of an alkaline phosphatase
    • Cherenok, S., Vovk, A., Muravyova, I., Shivanyuk, A., Kukhar, V., Lipkowski, J., Kalchenko, V.: Calix[4]arene α-aminophosphonic acids: asymmetric synthesis and enantioselective inhibition of an alkaline phosphatase. Org. Lett. 8, 549-552 (2006).
    • (2006) Org. Lett. , vol.8 , pp. 549-552
    • Cherenok, S.1    Vovk, A.2    Muravyova, I.3    Shivanyuk, A.4    Kukhar, V.5    Lipkowski, J.6    Kalchenko, V.7
  • 9
    • 0037147253 scopus 로고    scopus 로고
    • Structural evidence of functional divergence in human alkaline phosphatases
    • Le Du, M. H., Millan, J. L.: Structural evidence of functional divergence in human alkaline phosphatases. J. Biol. Chem. 277, 49808-49814 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 49808-49814
    • Le Du, M.H.1    Millan, J.L.2
  • 10
    • 27744480314 scopus 로고    scopus 로고
    • Phosphodiesterase activity of alkaline phosphatase in ATP-initiated Ca(2 +) and phosphate deposition in isolated chicken matrix vesicles
    • Zhang, L., Balcerzak, M., Radisson, J., Thouverey, C., Pikula, S., Azzar, G., Buchet, R.: Phosphodiesterase activity of alkaline phosphatase in ATP-initiated Ca(2 +) and phosphate deposition in isolated chicken matrix vesicles. J. Biol. Chem. 280, 37289-37296 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 37289-37296
    • Zhang, L.1    Balcerzak, M.2    Radisson, J.3    Thouverey, C.4    Pikula, S.5    Azzar, G.6    Buchet, R.7
  • 11
    • 0031764923 scopus 로고    scopus 로고
    • Alkaline phosphatase (EC 3.1.3.1) in serum is inhibited by physiological concentrations of inorganic phosphate
    • Coburn, S. P., Mahuren, J. D., Jain, M., Zubovic, Y., Wortsman, J.: Alkaline phosphatase (EC 3. 1. 3. 1) in serum is inhibited by physiological concentrations of inorganic phosphate. J. Clin. Endocrinology and Metabolism. 83, 3951-3957 (1998).
    • (1998) J. Clin. Endocrinology and Metabolism. , vol.83 , pp. 3951-3957
    • Coburn, S.P.1    Mahuren, J.D.2    Jain, M.3    Zubovic, Y.4    Wortsman, J.5
  • 12
    • 24344435113 scopus 로고    scopus 로고
    • Calcification of human valve interstitial cells is dependent on alkaline phosphatase activity
    • Mathieu, P., Voisine, P., Pepin, A., Shetty, R., Savard, N., Dagenais, F.: Calcification of human valve interstitial cells is dependent on alkaline phosphatase activity. J. Heart Valve Dis. 14, 353-357 (2005).
    • (2005) J. Heart Valve Dis. , vol.14 , pp. 353-357
    • Mathieu, P.1    Voisine, P.2    Pepin, A.3    Shetty, R.4    Savard, N.5    Dagenais, F.6
  • 14
    • 25844451632 scopus 로고    scopus 로고
    • Extremely high levels of alkaline phosphatase in adult patients as a manifestation of bacteremia
    • Tung, C. B., Tung, C. F., Yang, D. Y., Hu, W. H., Hung, D. Z., Peng, Y. C., Chang, C. S.: Extremely high levels of alkaline phosphatase in adult patients as a manifestation of bacteremia. Hepatogastroenterology 52, 1347-1350 (2005).
    • (2005) Hepatogastroenterology , vol.52 , pp. 1347-1350
    • Tung, C.B.1    Tung, C.F.2    Yang, D.Y.3    Hu, W.H.4    Hung, D.Z.5    Peng, Y.C.6    Chang, C.S.7
  • 15
    • 0033605749 scopus 로고    scopus 로고
    • A model of the transition state in the alkaline phosphatase reaction
    • Holtz, K. M., Stec, B., Kantrowitz, E. R.: A model of the transition state in the alkaline phosphatase reaction. J. Biol. Chem. 274, 8351-8354 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 8351-8354
    • Holtz, K.M.1    Stec, B.2    Kantrowitz, E.R.3
  • 16
    • 0034119452 scopus 로고    scopus 로고
    • Alternate modes of binding in two crystal structures of alkaline phosphatase-inhibitor complexes
    • Holtz, K. M., Stec, B., Myers, J. K., Antonelli, S. M., Widlanski, T. S., Kantrowitz, E. R.: Alternate modes of binding in two crystal structures of alkaline phosphatase-inhibitor complexes. Protein Sci. 9, 907-915 (2000).
    • (2000) Protein Sci. , vol.9 , pp. 907-915
    • Holtz, K.M.1    Stec, B.2    Myers, J.K.3    Antonelli, S.M.4    Widlanski, T.S.5    Kantrowitz, E.R.6
  • 17
    • 20444506123 scopus 로고    scopus 로고
    • Structural studies of human placental alkaline phosphatase in complex with functional ligands
    • Llinas, P., Stura, E. A., Menez, A., Kiss, Z., Stigbrand, T., Millan, J. L., Le Du, M. H.: Structural studies of human placental alkaline phosphatase in complex with functional ligands. J. Mol. Biol. 350, 441-451 (2005).
    • (2005) J. Mol. Biol. , vol.350 , pp. 441-451
    • Llinas, P.1    Stura, E.A.2    Menez, A.3    Kiss, Z.4    Stigbrand, T.5    Millan, J.L.6    Le Du, M.H.7
  • 18
    • 0000285995 scopus 로고
    • Chloromethylation of calixarenes and synthesis of new water soluble macrocyclic hosts
    • Almi, M., Arduini, A., Casnati, A., Pochini, A., Ungaro, R.: Chloromethylation of calixarenes and synthesis of new water soluble macrocyclic hosts. Tetrahedron 45, 2177-2182 (1989).
    • (1989) Tetrahedron , vol.45 , pp. 2177-2182
    • Almi, M.1    Arduini, A.2    Casnati, A.3    Pochini, A.4    Ungaro, R.5
  • 20
    • 0004282059 scopus 로고
    • (in Russian, Mir, Moscow), London: Longman
    • Dixon, M., Webb, E. C.: Enzymes. Longman, London (1982). (in Russian, Mir, Moscow).
    • (1982) Enzymes
    • Dixon, M.1    Webb, E.C.2
  • 21
    • 0030203710 scopus 로고    scopus 로고
    • Distributed automated docking of flexible ligands to proteins: Parallel applications of AutoDock 2.4
    • Morris, G. M., Goodsell, D. S., Huey, R., Olson, A. J.: Distributed automated docking of flexible ligands to proteins: parallel applications of AutoDock 2. 4. J. Comput. Aided Mol. Des. 10, 293-304 (1996).
    • (1996) J. Comput. Aided Mol. Des. , vol.10 , pp. 293-304
    • Morris, G.M.1    Goodsell, D.S.2    Huey, R.3    Olson, A.J.4
  • 22
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function
    • Morris, G. M., Goodsel, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., Olson, A. J.: Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function. J. Comput. Chem. 19, 1639-1662 (1998).
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsel, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 24
    • 0029115487 scopus 로고
    • Zinc binding in proteins and solution: A simple but accurate nonbonded representation
    • Stote, R. H., Karplus, M.: Zinc binding in proteins and solution: a simple but accurate nonbonded representation. Proteins 23, 12-31 (1995).
    • (1995) Proteins , vol.23 , pp. 12-31
    • Stote, R.H.1    Karplus, M.2
  • 26
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., Peitsch, M. C.: SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723 (1997).
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 29
    • 37049083055 scopus 로고
    • Solvents effects on the conformations and hydrogen bond structure of partially methylated p-tret-butylcalix[4]arenes
    • Groenen, L. G., Steinwender, E., Lutz, B. T. G., van der Maas, J. H., Reinhoudt, D. N.: Solvents effects on the conformations and hydrogen bond structure of partially methylated p-tret-butylcalix[4]arenes. J. Chem. Soc., Perkin Trans. 2, 1893-1898 (1992).
    • (1992) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 1893-1898
    • Groenen, L.G.1    Steinwender, E.2    Lutz, B.T.G.3    van der Maas, J.H.4    Reinhoudt, D.N.5
  • 30
    • 0032483442 scopus 로고    scopus 로고
    • Genetic complexity, structure, and characterization of highly active bovine intestinal alkaline phosphatases
    • Manes, T., Hoylaerts, M. F., Muller, R., Lottspeich, F., Holke, W., Millan, J. L.: Genetic complexity, structure, and characterization of highly active bovine intestinal alkaline phosphatases. J. Biol. Chem. 273, 23353-23360 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 23353-23360
    • Manes, T.1    Hoylaerts, M.F.2    Muller, R.3    Lottspeich, F.4    Holke, W.5    Millan, J.L.6
  • 31
    • 40849126492 scopus 로고    scopus 로고
    • Comparative study of calix[4]arene derivatives: Implications for ligand design
    • Hong, J., Ham, S.: Comparative study of calix[4]arene derivatives: implications for ligand design. Tetrahedron Lett. 49, 2393-2396 (2008).
    • (2008) Tetrahedron Lett. , vol.49 , pp. 2393-2396
    • Hong, J.1    Ham, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.