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Volumn 16, Issue 3, 2006, Pages 343-348

Organophosphonic acids as drug candidates

Author keywords

FBPase inhibitor; Phosphate mimetic; Phosphonate; PTP1B inhibitor; Pyridoxal 5 phosphate analogue; RdRp inhibitor; Serine protease inhibitor

Indexed keywords

ADEFOVIR DIPIVOXIL; CATHEPSIN G; CHYMASE; CS 917; ENZYME INHIBITOR; FRUCTOSE BISPHOSPHATASE; FRUCTOSE BISPHOSPHATASE INHIBITOR; HOMOCYSTEINE; MB 06322; NUCLEOTIDYLTRANSFERASE INHIBITOR; PHOSPHONIC ACID DERIVATIVE; PROTEIN TYROSINE PHOSPHATASE 1B; PROTEIN TYROSINE PHOSPHATASE 1B INHIBITOR; PURINE DERIVATIVE; PYRIDOXAL 5 PHOSPHATE; PYRIDOXINE; PYRIMIDINE DERIVATIVE; RNA DIRECTED RNA POLYMERASE; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 33644895702     PISSN: 13543776     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543776.16.3.343     Document Type: Review
Times cited : (10)

References (41)
  • 1
    • 7744241924 scopus 로고    scopus 로고
    • Adefovir dipivoxil: Review of a novel acyclic nucleoside analogue
    • DANTA M, DUSHEIKO G: Adefovir dipivoxil: review of a novel acyclic nucleoside analogue. Int. J. Clin. Pract. (2004) 58:877-886
    • (2004) Int. J. Clin. Pract. , vol.58 , pp. 877-886
    • Danta, M.1    Dusheiko, G.2
  • 2
    • 20344370977 scopus 로고    scopus 로고
    • MB06322 (CS-917): A potent and selective inhibitor of fructose 1,6-bisphosphatase for controlling gluconeogenesis in Type 2 diabetes
    • ERION MD, VAN POELJE PD, DANG Q et al.: MB06322 (CS-917): a potent and selective inhibitor of fructose 1,6-bisphosphatase for controlling gluconeogenesis in Type 2 diabetes. Proc. Natl Acad. Sci. USA (2005) 102:7970-7975.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 7970-7975
    • Erion, M.D.1    Van Poelje, P.D.2    Dang, Q.3
  • 3
    • 0034614490 scopus 로고    scopus 로고
    • Signaling - 2000 and beyond
    • HUNTER T: Signaling - 2000 and beyond. Cell (2000) 100:113-127.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 4
    • 0036181649 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Structure and function, substrate specificity, and inhibitor development
    • ZHANG ZY: Protein tyrosine phosphatases: structure and function, substrate specificity, and inhibitor development. Ann. Rev. Pharmacol. Toxicol. (2002) 42:209-234.
    • (2002) Ann. Rev. Pharmacol. Toxicol. , vol.42 , pp. 209-234
    • Zhang, Z.Y.1
  • 5
    • 0033525870 scopus 로고    scopus 로고
    • Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene
    • ELCHEBLY M, PAYETTE P, MICHALISZYN E et al.: Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. Science (1999) 283:1544-1548.
    • (1999) Science , vol.283 , pp. 1544-1548
    • Elchebly, M.1    Payette, P.2    Michaliszyn, E.3
  • 6
    • 0033942614 scopus 로고    scopus 로고
    • Increased energy expenditures decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice
    • KLAMAN LD, BOSS O, PERONI OD et al.: Increased energy expenditures decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice. Mol. Cell Biol. (2000) 20:5479-5489.
    • (2000) Mol. Cell Biol , vol.20 , pp. 5479-5489
    • Klaman, L.D.1    Boss, O.2    Peroni, O.D.3
  • 7
    • 0037143754 scopus 로고    scopus 로고
    • PTP1B antisense Oligonucleotide lowers PTP1B protein, normalizes blood glucose, and improves insulin sensitiviy in diabetic mice
    • ZINKER BA, RONDINONE CM, TREVILLYAN JM et al.: PTP1B antisense Oligonucleotide lowers PTP1B protein, normalizes blood glucose, and improves insulin sensitiviy in diabetic mice. Proc. Natl. Acad. USA (2002) 99:11357-11362.
    • (2002) Proc. Natl. Acad. USA , vol.99 , pp. 11357-11362
    • Zinker, B.A.1    Rondinone, C.M.2    Trevillyan, J.M.3
  • 9
    • 0041809012 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B inhibition: Opportunities and challenges
    • LIU G: Protein tyrosine phosphatase 1B inhibition: opportunities and challenges. Curr. Med. Chem. (2003) 10:1407-1421.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1407-1421
    • Liu, G.1
  • 10
    • 0036884693 scopus 로고    scopus 로고
    • Dual-specificity phosphatases as targets for antineoplastic agents
    • LYON MA, DUCRUET AP, WIPE P, LAZO JS: Dual-specificity phosphatases as targets for antineoplastic agents. Nat. Rev. Drug Discov. (2002) 1:961-976.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 961-976
    • Lyon, M.A.1    Ducruet, A.P.2    Wipe, P.3    Lazo, J.S.4
  • 11
    • 10744228866 scopus 로고    scopus 로고
    • The development of potent non-peptidic PTP1B inhibitors
    • DUFRESNE C, ROY P, WANG Z et al.: The development of potent non-peptidic PTP1B inhibitors. Bioorg. Med. Chem. Lett. (2004) 14:1039-1042.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 1039-1042
    • Dufresne, C.1    Roy, P.2    Wang, Z.3
  • 12
    • 7944224566 scopus 로고    scopus 로고
    • The role of protease activation of inflammation in allergic respiratory diseases
    • REED CE, KITA H: The role of protease activation of inflammation in allergic respiratory diseases. J Allergy Clin. Immunol. (2004) 114:997-1008.
    • (2004) J Allergy Clin. Immunol. , vol.114 , pp. 997-1008
    • Reed, C.E.1    Kita, H.2
  • 14
    • 24044436201 scopus 로고    scopus 로고
    • A novel, potent dual inhibitor of the leukocyte proteases cathepsin G and chymase
    • DE GARAVILLA L, GRECO MN, SUKUMAR N et al.: A novel, potent dual inhibitor of the leukocyte proteases cathepsin G and chymase. J. Biol. Chem. (2005) 280:18001-18007.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18001-18007
    • De Garavilla, L.1    Greco, M.N.2    Sukumar, N.3
  • 15
    • 0019415752 scopus 로고
    • Receptor and postreceptor defects contribute to the insulin resistance in noninsulin-dependent diabetes mellitus
    • KOLTERMAN OG, GRAY RS, GRIFFIN J et al.: Receptor and postreceptor defects contribute to the insulin resistance in noninsulin-dependent diabetes mellitus. J. Clin. Invest. (1981) 68:957-969.
    • (1981) J. Clin. Invest. , vol.68 , pp. 957-969
    • Kolterman, O.G.1    Gray, R.S.2    Griffin, J.3
  • 16
    • 0024026298 scopus 로고    scopus 로고
    • The triumvirate: β cell, muscle, liver. A collusion responsible for NIDDM
    • DEFRONZO PA: The triumvirate: β cell, muscle, liver. A collusion responsible for NIDDM. Diabetes (1998) 37:667-687.
    • (1998) Diabetes , vol.37 , pp. 667-687
    • Defronzo, P.A.1
  • 17
    • 0024511329 scopus 로고
    • Predominant role of gluconeogenesis in increased hepatic glucose production in NIDDM
    • CONSOLI A, NURJHAN N, CAPANI F, GERICH J: Predominant role of gluconeogenesis in increased hepatic glucose production in NIDDM. Diabetes (1989) 38:550-557.
    • (1989) Diabetes , vol.38 , pp. 550-557
    • Consoli, A.1    Nurjhan, N.2    Capani, F.3    Gerich, J.4
  • 20
    • 0035181809 scopus 로고    scopus 로고
    • Quantitative contributions of gluconeogenesis to glucose production during fasting in Type 2 diabetes mellitus
    • WAJNGOT A, CHANDRAMOULI V, SCHUMANN WC et al.: Quantitative contributions of gluconeogenesis to glucose production during fasting in Type 2 diabetes mellitus. Metabolism (2001) 50:47-52.
    • (2001) Metabolism , vol.50 , pp. 47-52
    • Wajngot, A.1    Chandramouli, V.2    Schumann, W.C.3
  • 21
    • 0005469667 scopus 로고
    • Intracellular concentration and specific activity of carbohydrate-metabolizing enzymes. Application of specific radioimmunoassay
    • Veneziale CM (Ed.), University Park Press, Baltimore, USA
    • VENEZIALE CM, DONOFRIO JC, HANSEN JB, JOHNSON ML, MAZZOTTA MY: Intracellular concentration and specific activity of carbohydrate-metabolizing enzymes. Application of specific radioimmunoassay. In: The Regulation of carbohydrate Formation and Utilization in Mammals. Veneziale CM (Ed.), University Park Press, Baltimore, USA (1981):23-44.
    • (1981) The Regulation of Carbohydrate Formation and Utilization in Mammals , pp. 23-44
    • Veneziale, C.M.1    Donofrio, J.C.2    Hansen, J.B.3    Johnson, M.L.4    Mazzotta, M.Y.5
  • 22
    • 0026520193 scopus 로고
    • Molecular physiology of the regulation of hepatic gluconeogenesis and glycolysis
    • PILKIS SJ, GRANNER DK: Molecular physiology of the regulation of hepatic gluconeogenesis and glycolysis. Ann. Rev. Physiol. (1992) 54:885-909.
    • (1992) Ann. Rev. Physiol. , vol.54 , pp. 885-909
    • Pilkis, S.J.1    Granner, D.K.2
  • 23
    • 0019568187 scopus 로고
    • Inhibition of fructose-1,6-bisphosphatase by fructose-2,6-bisphosphate
    • VAN SCHAFTINGEN E, HERS HG: Inhibition of fructose-1,6-bisphosphatase by fructose-2,6-bisphosphate. Proc. Natl. Acad. Sci. USA (1981) 78:2861-2863.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 2861-2863
    • Van Schaftingen, E.1    Hers, H.G.2
  • 24
    • 0019887960 scopus 로고
    • Inhibition of fructose-1,6-bisphosphatase by fructose-2,6-bisphosphate
    • PILKIS SJ, EL-MAGHRABI MR, PILKIS J, CLAUS T: Inhibition of fructose-1,6-bisphosphatase by fructose-2,6-bisphosphate. J. Biol. Chem. (1981) 256:3619-3622.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3619-3622
    • Pilkis, S.J.1    El-Maghrabi, M.R.2    Pilkis, J.3    Claus, T.4
  • 25
    • 0023918674 scopus 로고
    • Hormonal regulation of hepatic gluconeogenesis and glycolysis
    • PILKIS SJ, EL-MAGHRABI MR, CLAUS TH: Hormonal regulation of hepatic gluconeogenesis and glycolysis. Ann. Rev. Biochem. (1988) 57:755-783.
    • (1988) Ann. Rev. Biochem. , vol.57 , pp. 755-783
    • Pilkis, S.J.1    El-Maghrabi, M.R.2    Claus, T.H.3
  • 26
    • 0001683176 scopus 로고
    • Allosteric inhibition of rat liver fructose-1,6-bisphosphate by adenosine 5′-monophosphate
    • TAKETA K, POGELL BM: Allosteric inhibition of rat liver fructose-1,6-bisphosphate by adenosine 5′-monophosphate. J. Biol. Chem. (1965) 240:651-662.
    • (1965) J. Biol. Chem. , vol.240 , pp. 651-662
    • Taketa, K.1    Pogell, B.M.2
  • 27
    • 0025883747 scopus 로고
    • Conformational transition of fructose-1,6-bisphosphatase: Structure comparison between the AMP complex (T form) and the fructose 6-phosphate complex (R form)
    • KE H, LIANG JY, ZHANG Y, LIPSCOMB WN: Conformational transition of fructose-1,6-bisphosphatase: Structure comparison between the AMP complex (T form) and the fructose 6-phosphate complex (R form). Biochemistry (1991) 30:4412-4420.
    • (1991) Biochemistry , vol.30 , pp. 4412-4420
    • Ke, H.1    Liang, J.Y.2    Zhang, Y.3    Lipscomb, W.N.4
  • 28
    • 0028029482 scopus 로고
    • Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphatase
    • ZHANG Y, LIANG JY, HUANG S, LIPSCOMB WN: Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphatase. J. Mol. Biol. (1994) 244:609-624.
    • (1994) J. Mol. Biol. , vol.244 , pp. 609-624
    • Zhang, Y.1    Liang, J.Y.2    Huang, S.3    Lipscomb, W.N.4
  • 29
    • 0038778445 scopus 로고    scopus 로고
    • 3-(2-Carboxy-ethyl)-4,6-dichloro-1H-indole-2-carboxylic acid: An allosteric inhibitor of fructose-1,6-bisphosphatase bind at the AMP site
    • WRIGHT SW, CARLO AA, DANLEY DE et al.: 3-(2-Carboxy-ethyl)-4,6-dichloro-1H-indole-2-carboxylic acid: an allosteric inhibitor of fructose-1,6-bisphosphatase bind at the AMP site. Bioorg. Med. Chem. Lett. (2003) 13:2055-2058.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 2055-2058
    • Wright, S.W.1    Carlo, A.A.2    Danley, D.E.3
  • 30
    • 0037194657 scopus 로고    scopus 로고
    • Anilinoquinazoline inhibitors of fructose-1,6-bisphosphatase bind at a novel allosteric site: Synthesis, in vitro characterization, and X-ray crystallography
    • WRIGHT SW, CARLO AA, CARTY MD et al.: Anilinoquinazoline inhibitors of fructose-1,6-bisphosphatase bind at a novel allosteric site: synthesis, in vitro characterization, and X-ray crystallography. J. Med. Chem. (2002) 45:3865-3877.
    • (2002) J. Med. Chem. , vol.45 , pp. 3865-3877
    • Wright, S.W.1    Carlo, A.A.2    Carty, M.D.3
  • 31
    • 0021723506 scopus 로고
    • Stereoselective synthesis and biological activin of β- and α-D-arabinose 1,5-diphosphate: Analogues of a potent metabolic regulator
    • MARYANOFF BE, REITZ AB, TUTWILER GF, BENKOVIC SJ, BENKOVIC PA, PILKIS SJ: Stereoselective synthesis and biological activin of β- and α-D-arabinose 1,5-diphosphate: analogues of a potent metabolic regulator. J. Am. Chem. Soc. (1984) 106:7851-7853.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 7851-7853
    • Maryanoff, B.E.1    Reitz, A.B.2    Tutwiler, G.F.3    Benkovic, S.J.4    Benkovic, P.A.5    Pilkis, S.J.6
  • 32
    • 0032501990 scopus 로고    scopus 로고
    • Preventing coronary heart disease: B vitamins and homocysteine
    • OMENN GS, BERESFORD SA, MOTULSKY AG: Preventing coronary heart disease: B vitamins and homocysteine. Circulation (1998) 97:421-424.
    • (1998) Circulation , vol.97 , pp. 421-424
    • Omenn, G.S.1    Beresford, S.A.2    Motulsky, A.G.3
  • 33
    • 0032501963 scopus 로고    scopus 로고
    • 6 concentrations: Risk factors for stroke, peripheral vascular disease, and coronary artery disease
    • 6 concentrations: risk factors for stroke, peripheral vascular disease, and coronary artery disease. Circulation (1998) 97:437-443.
    • (1998) Circulation , vol.97 , pp. 437-443
    • Robinson, K.1    Arheart, K.2    Refsum, H.3
  • 34
    • 12144260229 scopus 로고    scopus 로고
    • Control of hepatitis C: A medicinal chemistry perspective
    • GORDON CP, KELLER PA: Control of hepatitis C: a medicinal chemistry perspective. J. Med. Chem. (2005) 48: 1.
    • (2005) J. Med. Chem. , vol.48 , pp. 1
    • Gordon, C.P.1    Keller, P.A.2
  • 35
    • 0141426816 scopus 로고    scopus 로고
    • Targeting NS5B RNA-dependent RNA polymerase for anti-HCV chemotherapy
    • WU JZ, HONG Z: Targeting NS5B RNA-dependent RNA polymerase for anti-HCV chemotherapy. Curr. Drug Targets Infect. Disord. (2003) 3:207-219.
    • (2003) Curr. Drug Targets Infect. Disord. , vol.3 , pp. 207-219
    • Wu, J.Z.1    Hong, Z.2
  • 36
    • 17444388557 scopus 로고    scopus 로고
    • Design, synthesis, and antiviral activity of adenosine 5′-phosphonate analogues as chain terminators against hepatitis C virus
    • KOH Y, SHIM JH, WU JZ, ZHONG W, HONG Z, GIRARDET JL: Design, synthesis, and antiviral activity of adenosine 5′-phosphonate analogues as chain terminators against hepatitis C virus. J. Med. Chem. (2005) 48:2867-2875.
    • (2005) J. Med. Chem. , vol.48 , pp. 2867-2875
    • Koh, Y.1    Shim, J.H.2    Wu, J.Z.3    Zhong, W.4    Hong, Z.5    Girardet, J.L.6
  • 38
    • 0028819889 scopus 로고
    • Mononucleoside phosphotriester derivatives with S-acyl-2-thioethyl bioreversible phosphates protecting groups: Intracellular delivery of 3′-azido-2′,3′-dideoxythymidine 5′-minophosphate
    • LEFEBVRE I, PERIGAUD C, POMPON A et al.: Mononucleoside phosphotriester derivatives with S-acyl-2-thioethyl bioreversible phosphates protecting groups: Intracellular delivery of 3′-azido-2′,3′-dideoxythymidine 5′-minophosphate. J. Med. Chem. (1995) 38:3941-3950.
    • (1995) J. Med. Chem. , vol.38 , pp. 3941-3950
    • Lefebvre, I.1    Perigaud, C.2    Pompon, A.3
  • 39
    • 11144357250 scopus 로고    scopus 로고
    • 450 3A-activated prodrugs (HepDirect prodrugs) useful for targeting phosph(on)ate-based drugs to the liver
    • 450 3A-activated prodrugs (HepDirect prodrugs) useful for targeting phosph(on)ate-based drugs to the liver. J. Am. Chem. Soc. (2004) 126:5154-5163.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5154-5163
    • Erion, M.D.1    Reddy, K.R.2    Boyer, S.H.3
  • 41
    • 0027284753 scopus 로고
    • Intracellular delivery of bioactive AZT nucleotides by aryl phosphate derivatives of AZT
    • MCGUIGAN C, PATHIRANA RN, BALZARINI J, DE CLERCQ E: Intracellular delivery of bioactive AZT nucleotides by aryl phosphate derivatives of AZT. J. Med. Chem. (1993) 36:1048-1052.
    • (1993) J. Med. Chem. , vol.36 , pp. 1048-1052
    • Mcguigan, C.1    Pathirana, R.N.2    Balzarini, J.3    De Clercq, E.4


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