메뉴 건너뛰기




Volumn 1804, Issue 5, 2010, Pages 1223-1230

Modifications to the dNTP triphosphate moiety: From mechanistic probes for DNA polymerases to antiviral and anti-cancer drug design

Author keywords

Anti cancer; Antiviral; Bisphosphonate; DNA polymerase; Drug delivery; Drug targeting; Nucleotide analogue

Indexed keywords

BISPHOSPHONIC ACID DERIVATIVE; CYTARABINE; DNA POLYMERASE; FLOXURIDINE; GEMCITABINE; NUCLEOSIDE ANALOG; ZIDOVUDINE;

EID: 77949551370     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.01.005     Document Type: Review
Times cited : (31)

References (80)
  • 1
    • 33751206730 scopus 로고    scopus 로고
    • Regulation of DNA repair fidelity by molecular checkpoints: "gates" in DNA polymerase beta's substrate selection
    • Radhakrishnan R., Arora K., Wang Y., Beard W.A., Wilson S.H., and Schlick T. Regulation of DNA repair fidelity by molecular checkpoints: "gates" in DNA polymerase beta's substrate selection. Biochemistry 45 (2006) 15142-15156
    • (2006) Biochemistry , vol.45 , pp. 15142-15156
    • Radhakrishnan, R.1    Arora, K.2    Wang, Y.3    Beard, W.A.4    Wilson, S.H.5    Schlick, T.6
  • 2
    • 8544278025 scopus 로고    scopus 로고
    • DNA polymerase fidelity: kinetics, structure, and checkpoints
    • Joyce C.M., and Benkovic S.J. DNA polymerase fidelity: kinetics, structure, and checkpoints. Biochemistry 43 (2004) 14317-14324
    • (2004) Biochemistry , vol.43 , pp. 14317-14324
    • Joyce, C.M.1    Benkovic, S.J.2
  • 3
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-I reverse transcriptase: implications for drug resistance
    • Huang H.F., Chopra R., Verdine G.L., and Harrison S.C. Structure of a covalently trapped catalytic complex of HIV-I reverse transcriptase: implications for drug resistance. Science 282 (1998) 1669-1675
    • (1998) Science , vol.282 , pp. 1669-1675
    • Huang, H.F.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 4
    • 0032535528 scopus 로고    scopus 로고
    • Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation
    • Li Y., Korolev S., and Waksman G. Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation. EMBO J. 17 (1998) 7514-7525
    • (1998) EMBO J. , vol.17 , pp. 7514-7525
    • Li, Y.1    Korolev, S.2    Waksman, G.3
  • 5
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 angstrom resolution
    • Doublie S., Tabor S., Long A.M., Richardson C.C., and Ellenberger T. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 angstrom resolution. Nature 391 (1998) 251-258
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 6
    • 0035369086 scopus 로고    scopus 로고
    • Structure of the replicating complex of a pol alpha family DNA polymerase
    • Franklin M.C., Wang J.M., and Steitz T.A. Structure of the replicating complex of a pol alpha family DNA polymerase. Cell 105 (2001) 657-667
    • (2001) Cell , vol.105 , pp. 657-667
    • Franklin, M.C.1    Wang, J.M.2    Steitz, T.A.3
  • 7
    • 0030930760 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: evidence for an induced fit mechanism
    • Sawaya M.R., Prasad R., Wilson S.H., Kraut J., and Pelletier H. Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: evidence for an induced fit mechanism. Biochemistry 36 (1997) 11205-11215
    • (1997) Biochemistry , vol.36 , pp. 11205-11215
    • Sawaya, M.R.1    Prasad, R.2    Wilson, S.H.3    Kraut, J.4    Pelletier, H.5
  • 8
    • 0026033193 scopus 로고
    • Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant
    • Patel S.S., Wong I., and Johnson K.A. Pre-steady-state kinetic analysis of processive DNA replication including complete characterization of an exonuclease-deficient mutant. Biochemistry 30 (1991) 511-525
    • (1991) Biochemistry , vol.30 , pp. 511-525
    • Patel, S.S.1    Wong, I.2    Johnson, K.A.3
  • 9
    • 0035966270 scopus 로고    scopus 로고
    • Yeast DNA polymerase eta utilizes an induced-fit mechanism of nucleotide incorporation
    • Washington M.T., Prakash L., and Prakash S. Yeast DNA polymerase eta utilizes an induced-fit mechanism of nucleotide incorporation. Cell 107 (2001) 917-927
    • (2001) Cell , vol.107 , pp. 917-927
    • Washington, M.T.1    Prakash, L.2    Prakash, S.3
  • 10
    • 0025799903 scopus 로고
    • Kinetic mechanism of DNA polymerase 1 (Klenow fragment): identification of a second conformational change and evaluation of the internal equilibrium constant
    • Dahlberg M.E., and Benkovic S.J. Kinetic mechanism of DNA polymerase 1 (Klenow fragment): identification of a second conformational change and evaluation of the internal equilibrium constant. Biochemistry 30 (1991) 4835-4843
    • (1991) Biochemistry , vol.30 , pp. 4835-4843
    • Dahlberg, M.E.1    Benkovic, S.J.2
  • 11
    • 51849149950 scopus 로고    scopus 로고
    • Mismatched and matched dNTP incorporation by DNA polymerase beta proceed via analogous kinetic pathways
    • Roettger M.P., Bakhtina M., and Tsai M.-D. Mismatched and matched dNTP incorporation by DNA polymerase beta proceed via analogous kinetic pathways. Biochemistry 47 (2008) 9718-9727
    • (2008) Biochemistry , vol.47 , pp. 9718-9727
    • Roettger, M.P.1    Bakhtina, M.2    Tsai, M.-D.3
  • 12
    • 65249138188 scopus 로고    scopus 로고
    • Contribution of the reverse rate of the conformational step to polymerase beta fidelity
    • Bakhtina M., Roettger M.P., and Tsai M.-D. Contribution of the reverse rate of the conformational step to polymerase beta fidelity. Biochemistry 48 (2009) 3197-3208
    • (2009) Biochemistry , vol.48 , pp. 3197-3208
    • Bakhtina, M.1    Roettger, M.P.2    Tsai, M.-D.3
  • 13
    • 49449091485 scopus 로고    scopus 로고
    • DNA polymerases as therapeutic targets
    • Berdis A.J. DNA polymerases as therapeutic targets. Biochemistry 47 (2008) 8253-8260
    • (2008) Biochemistry , vol.47 , pp. 8253-8260
    • Berdis, A.J.1
  • 14
    • 38949125404 scopus 로고    scopus 로고
    • New cancer chemotherapy agents: inhibitors of DNA polymerase
    • Sakaguchi K., and Sugawara F. New cancer chemotherapy agents: inhibitors of DNA polymerase. Curr. Drug Ther. 3 (2008) 44-53
    • (2008) Curr. Drug Ther. , vol.3 , pp. 44-53
    • Sakaguchi, K.1    Sugawara, F.2
  • 15
    • 49449118333 scopus 로고    scopus 로고
    • Non-natural nucleotide analogs as probes of DNA polymerase activity
    • Devadoss B., and Berdis A.J. Non-natural nucleotide analogs as probes of DNA polymerase activity. Curr. Chem. Biol. 1 (2007) 241-264
    • (2007) Curr. Chem. Biol. , vol.1 , pp. 241-264
    • Devadoss, B.1    Berdis, A.J.2
  • 16
    • 63449116519 scopus 로고    scopus 로고
    • Current status of older and new purine nucleoside analogues in the treatment of lymphoproliferative diseases
    • Robak T., Korycka A., Lech-Maranda E., and Robak P. Current status of older and new purine nucleoside analogues in the treatment of lymphoproliferative diseases. Molecules 14 (2009) 1172-1215
    • (2009) Molecules , vol.14 , pp. 1172-1215
    • Robak, T.1    Korycka, A.2    Lech-Maranda, E.3    Robak, P.4
  • 17
    • 55949103581 scopus 로고    scopus 로고
    • Antivirals: current state of the art
    • De Clercq E. Antivirals: current state of the art. Future Virol. 3 (2008) 393-405
    • (2008) Future Virol. , vol.3 , pp. 393-405
    • De Clercq, E.1
  • 18
    • 67649111006 scopus 로고    scopus 로고
    • Produg approaches to improving the oral absorption of antiviral nucleotide analogues
    • Peterson L.W., and McKenna C.E. Produg approaches to improving the oral absorption of antiviral nucleotide analogues. Expert Opin. Drug Del. 6 (2009) 405-420
    • (2009) Expert Opin. Drug Del. , vol.6 , pp. 405-420
    • Peterson, L.W.1    McKenna, C.E.2
  • 19
    • 33644692006 scopus 로고    scopus 로고
    • Scientific perspectives on drug transporters and their role in drug interactions
    • Zhang L., Strong J.M., Qiu W., Lesko L.J., and Huang S.M. Scientific perspectives on drug transporters and their role in drug interactions. Mol. Pharm. 3 (2006) 62-69
    • (2006) Mol. Pharm. , vol.3 , pp. 62-69
    • Zhang, L.1    Strong, J.M.2    Qiu, W.3    Lesko, L.J.4    Huang, S.M.5
  • 20
    • 0033736202 scopus 로고    scopus 로고
    • Pronucleotides: toward the in vivo delivery of antiviral and anticancer nucleotides
    • Wagner C.R., Iyer V.V., and McIntee E.J. Pronucleotides: toward the in vivo delivery of antiviral and anticancer nucleotides. Med. Res. Rev. 20 (2000) 417-451
    • (2000) Med. Res. Rev. , vol.20 , pp. 417-451
    • Wagner, C.R.1    Iyer, V.V.2    McIntee, E.J.3
  • 21
    • 70349209354 scopus 로고    scopus 로고
    • HAART in treatment-experienced patients in the 21st century: the audacity of hope
    • Conway B. HAART in treatment-experienced patients in the 21st century: the audacity of hope. Future Virol. 4 (2009) 39-41
    • (2009) Future Virol. , vol.4 , pp. 39-41
    • Conway, B.1
  • 22
    • 11144311321 scopus 로고    scopus 로고
    • Antiretroviral therapy in previously untreated adults infected with the human immunodeficiency virus type I: established and potential determinants of virological outcome
    • Lowe S.H., Prins J.M., and Lange J.M.A. Antiretroviral therapy in previously untreated adults infected with the human immunodeficiency virus type I: established and potential determinants of virological outcome. Neth. J. Med. 62 (2004) 424-440
    • (2004) Neth. J. Med. , vol.62 , pp. 424-440
    • Lowe, S.H.1    Prins, J.M.2    Lange, J.M.A.3
  • 23
    • 0028144849 scopus 로고
    • Metabolism of 3′-azido-3′-deoxythymidine (AZT) in human placental trophoblasts and Hofbauer cells
    • Qian M., Bui T., Ho R.J.Y., and Unadkat J.D. Metabolism of 3′-azido-3′-deoxythymidine (AZT) in human placental trophoblasts and Hofbauer cells. Biochem. Pharmacol. 48 (1994) 383-389
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 383-389
    • Qian, M.1    Bui, T.2    Ho, R.J.Y.3    Unadkat, J.D.4
  • 24
    • 0025770911 scopus 로고
    • Thymidine and zidovudine metabolism in chronically zidovudine-exposed cells in vitro
    • Agarwal R.P., and Mian A.M. Thymidine and zidovudine metabolism in chronically zidovudine-exposed cells in vitro. Biochem. Pharmacol. 42 (1991) 905-911
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 905-911
    • Agarwal, R.P.1    Mian, A.M.2
  • 25
    • 48849091390 scopus 로고    scopus 로고
    • Restoration of the antiviral activity of 3′-azido-3′-deoxythymidine (AZT) against AZT-resistant human immunodeficiency virus by delivery of engineered thymidylate kinase to T cells
    • Lavie A., Su Y., Ghassemi M., Novak R.M., Caffrey M., Sekulic N., Monnerjahn C., Konrad M., and Cook J.L. Restoration of the antiviral activity of 3′-azido-3′-deoxythymidine (AZT) against AZT-resistant human immunodeficiency virus by delivery of engineered thymidylate kinase to T cells. J. Gen. Virol. 89 (2008) 1672-1679
    • (2008) J. Gen. Virol. , vol.89 , pp. 1672-1679
    • Lavie, A.1    Su, Y.2    Ghassemi, M.3    Novak, R.M.4    Caffrey, M.5    Sekulic, N.6    Monnerjahn, C.7    Konrad, M.8    Cook, J.L.9
  • 27
    • 0041412840 scopus 로고    scopus 로고
    • Factors associated with mitochondrial dysfunction in circulating peripheral blood lymphocytes from HIV-infected people
    • Polo R., Martinez S., Madrigal P., and Gonzalez-Munoz M. Factors associated with mitochondrial dysfunction in circulating peripheral blood lymphocytes from HIV-infected people. J. Acquir. Immune Defic. Syndr. 34 (2003) 32-36
    • (2003) J. Acquir. Immune Defic. Syndr. , vol.34 , pp. 32-36
    • Polo, R.1    Martinez, S.2    Madrigal, P.3    Gonzalez-Munoz, M.4
  • 28
    • 0242363266 scopus 로고    scopus 로고
    • Mitochondrial toxicity of NRTI antiviral drugs: an integrated cellular perspective
    • Lewis W., Day B.J., and Copeland W.C. Mitochondrial toxicity of NRTI antiviral drugs: an integrated cellular perspective. Nat. Rev. Drug Discov. 2 (2003) 812-822
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 812-822
    • Lewis, W.1    Day, B.J.2    Copeland, W.C.3
  • 29
    • 67649342599 scopus 로고    scopus 로고
    • Long patch base excision repair proceeds via coordinated stimulation of the multienzyme DNA repair complex
    • Balakrishnan L., Brandt P.D., Lindsey-Boltz L.A., Sancar A., and Bambara R.A. Long patch base excision repair proceeds via coordinated stimulation of the multienzyme DNA repair complex. J. Biol. Chem. 284 (2009) 15158-15172
    • (2009) J. Biol. Chem. , vol.284 , pp. 15158-15172
    • Balakrishnan, L.1    Brandt, P.D.2    Lindsey-Boltz, L.A.3    Sancar, A.4    Bambara, R.A.5
  • 30
    • 37149051581 scopus 로고    scopus 로고
    • Structure/function analysis of the interaction of adenomatous polyposis coli with DNA polymerase beta and its implications for base excision repair
    • Balusu R., Jaiswal A.S., Armas M.L., Kundu C.N., Bloom L.B., and Narayan S. Structure/function analysis of the interaction of adenomatous polyposis coli with DNA polymerase beta and its implications for base excision repair. Biochemistry 46 (2007) 13961-13974
    • (2007) Biochemistry , vol.46 , pp. 13961-13974
    • Balusu, R.1    Jaiswal, A.S.2    Armas, M.L.3    Kundu, C.N.4    Bloom, L.B.5    Narayan, S.6
  • 31
    • 67249087934 scopus 로고    scopus 로고
    • Human DNA polymerase beta polymorphism, Arg137Gln, impairs its polymerase activity and interaction with PCNA and the cellular base excision repair capacity
    • Guo Z., Zheng L., Dai H., Zhou M., Xu H., and Shen B. Human DNA polymerase beta polymorphism, Arg137Gln, impairs its polymerase activity and interaction with PCNA and the cellular base excision repair capacity. Nucleic Acids Res. 37 (2009) 3431-3441
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3431-3441
    • Guo, Z.1    Zheng, L.2    Dai, H.3    Zhou, M.4    Xu, H.5    Shen, B.6
  • 32
    • 65249169526 scopus 로고    scopus 로고
    • Sequence context-specific mutagenesis and base excision repair
    • Donigan K.A., and Sweasy J.B. Sequence context-specific mutagenesis and base excision repair. Mol. Carcinog. 48 (2009) 362-368
    • (2009) Mol. Carcinog. , vol.48 , pp. 362-368
    • Donigan, K.A.1    Sweasy, J.B.2
  • 37
    • 67649616341 scopus 로고    scopus 로고
    • A computational study of the hydrolysis of dGTP analogues with halomethylene-modified leaving groups in solution: implications for the mechanism of DNA polymerases
    • Kamerlin S.C.L., McKenna C.E., Goodman M.F., and Warshel A. A computational study of the hydrolysis of dGTP analogues with halomethylene-modified leaving groups in solution: implications for the mechanism of DNA polymerases. Biochemistry 48 (2009) 5963-5971
    • (2009) Biochemistry , vol.48 , pp. 5963-5971
    • Kamerlin, S.C.L.1    McKenna, C.E.2    Goodman, M.F.3    Warshel, A.4
  • 38
    • 77949560478 scopus 로고    scopus 로고
    • Halogenated β,γ-Methylene- and Ethylidene-dGTP-DNA Ternary Complexes with DNA Polymerase β: Structural Evidence for Stereospecific Binding of the Fluoromethylene Analogues
    • submitted
    • V.K. Batra, L.C. Pedersen, W.A. Beard, S.H. Wilson, B.A. Kashemirov, T.G. Upton, M.F. Goodman, C.E. McKenna, "Halogenated β,γ-Methylene- and Ethylidene-dGTP-DNA Ternary Complexes with DNA Polymerase β: Structural Evidence for Stereospecific Binding of the Fluoromethylene Analogues", submitted.
    • Batra, V.K.1    Pedersen, L.C.2    Beard, W.A.3    Wilson, S.H.4    Kashemirov, B.A.5    Upton, T.G.6    Goodman, M.F.7    McKenna, C.E.8
  • 39
    • 40149105373 scopus 로고    scopus 로고
    • Treatment of breast cancer with bone metastasis: bisphosphonate treatment - current and future
    • Kohno N. Treatment of breast cancer with bone metastasis: bisphosphonate treatment - current and future. Int. J. Clin. Oncol. 13 (2008) 18-23
    • (2008) Int. J. Clin. Oncol. , vol.13 , pp. 18-23
    • Kohno, N.1
  • 40
    • 44649087001 scopus 로고    scopus 로고
    • Emerging role of bisphosphonates in the clinic - antitumor activity and prevention of metastasis to bone
    • Lipton A. Emerging role of bisphosphonates in the clinic - antitumor activity and prevention of metastasis to bone. Cancer Treat. Rev. 34 (2008) S25-S30
    • (2008) Cancer Treat. Rev. , vol.34
    • Lipton, A.1
  • 42
    • 5644240878 scopus 로고    scopus 로고
    • Bisphosphonates in the treatment of skeletal metastases
    • Conte P., and Coleman R. Bisphosphonates in the treatment of skeletal metastases. Semin. Oncol. 31 (2004) 59-63
    • (2004) Semin. Oncol. , vol.31 , pp. 59-63
    • Conte, P.1    Coleman, R.2
  • 43
  • 45
    • 0035209393 scopus 로고    scopus 로고
    • Inhibition of bone resorption by alendronate and risedronate does not require osteoclast apoptosis
    • Halasy-Nagy J.M., Rodan G.A., and Reszka A.A. Inhibition of bone resorption by alendronate and risedronate does not require osteoclast apoptosis. Bone 29 (2001) 553-559
    • (2001) Bone , vol.29 , pp. 553-559
    • Halasy-Nagy, J.M.1    Rodan, G.A.2    Reszka, A.A.3
  • 46
    • 0032996153 scopus 로고    scopus 로고
    • Farnesol and geranylgeraniol prevent activation of caspases by aminobisphosphonates: biochemical evidence for two distinct pharmacological classes of bisphosphonate drugs
    • Benford H.L., Frith J.C., Auriola S., Monkkonen J., and Rogers M.J. Farnesol and geranylgeraniol prevent activation of caspases by aminobisphosphonates: biochemical evidence for two distinct pharmacological classes of bisphosphonate drugs. Mol. Pharmacol. 56 (1999) 131-140
    • (1999) Mol. Pharmacol. , vol.56 , pp. 131-140
    • Benford, H.L.1    Frith, J.C.2    Auriola, S.3    Monkkonen, J.4    Rogers, M.J.5
  • 47
    • 0242503684 scopus 로고    scopus 로고
    • New insights into the molecular mechanism of action of bisphosphonates
    • Rogers M.J. New insights into the molecular mechanism of action of bisphosphonates. Curr. Pharm. Design 9 (2003) 2643-2658
    • (2003) Curr. Pharm. Design , vol.9 , pp. 2643-2658
    • Rogers, M.J.1
  • 49
    • 0035146537 scopus 로고    scopus 로고
    • Structure-activity relationships for inhibition of farnesyl diphosphate synthase in vitro and inhibition of bone resorption in vivo by nitrogen-containing bisphosphonates
    • Dunford J.E., Thompson K., Coxon F.P., Luckman S.P., Hahn F.M., Poulter C.D., Ebetino F.H., and Rogers M.J. Structure-activity relationships for inhibition of farnesyl diphosphate synthase in vitro and inhibition of bone resorption in vivo by nitrogen-containing bisphosphonates. J. Pharmacol. Exp. Ther. 296 (2001) 235-242
    • (2001) J. Pharmacol. Exp. Ther. , vol.296 , pp. 235-242
    • Dunford, J.E.1    Thompson, K.2    Coxon, F.P.3    Luckman, S.P.4    Hahn, F.M.5    Poulter, C.D.6    Ebetino, F.H.7    Rogers, M.J.8
  • 50
    • 0027080882 scopus 로고
    • In vitro and in vivo anticalcification effects of novel bishydroxyiminophosphonates
    • Golomb G., Schlossman A., Eitan Y., Saadeh H., Vangelder J.M., and Breuer E. In vitro and in vivo anticalcification effects of novel bishydroxyiminophosphonates. J. Pharm. Sci. 81 (1992) 1004-1007
    • (1992) J. Pharm. Sci. , vol.81 , pp. 1004-1007
    • Golomb, G.1    Schlossman, A.2    Eitan, Y.3    Saadeh, H.4    Vangelder, J.M.5    Breuer, E.6
  • 52
    • 51049117949 scopus 로고    scopus 로고
    • Biodistribution and pharmacokinetic studies of bone-targeting N-(2-hydroxypropyl)methacrylamide copolymer-alendronate conjugates
    • Pan H.Z., Sima M., Kopeckova P., Wu K., Gao S.Q., Liu J.H., Wang D., Miller S.C., and Kopecek J. Biodistribution and pharmacokinetic studies of bone-targeting N-(2-hydroxypropyl)methacrylamide copolymer-alendronate conjugates. Mol. Pharm. 5 (2008) 548-558
    • (2008) Mol. Pharm. , vol.5 , pp. 548-558
    • Pan, H.Z.1    Sima, M.2    Kopeckova, P.3    Wu, K.4    Gao, S.Q.5    Liu, J.H.6    Wang, D.7    Miller, S.C.8    Kopecek, J.9
  • 53
    • 38149074045 scopus 로고    scopus 로고
    • Chemotherapeutic bone-targeted bisphosphonate prodrugs with hydrolytic mode of activation
    • Erez R., Ebner S., Attali B., and Shabat D. Chemotherapeutic bone-targeted bisphosphonate prodrugs with hydrolytic mode of activation. Bioorg. Med. Chem. Lett. 18 (2008) 816-820
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 816-820
    • Erez, R.1    Ebner, S.2    Attali, B.3    Shabat, D.4
  • 54
    • 44949170797 scopus 로고    scopus 로고
    • Bisphosphonate derivatives of nucleoside antimetabolites: hydrolytic stability and hydroxyapatite adsorption of 5′-beta, gamma-methylene and 5′-beta, gamma-(1-hydroxyethylidene) triphosphates of 5-fluorouridine and ara-cytidine
    • Ora M., Lonnberg T., Florea-Wang D., Zinnen S., Karpeisky A., and Lonnberg H. Bisphosphonate derivatives of nucleoside antimetabolites: hydrolytic stability and hydroxyapatite adsorption of 5′-beta, gamma-methylene and 5′-beta, gamma-(1-hydroxyethylidene) triphosphates of 5-fluorouridine and ara-cytidine. J. Org. Chem. 73 (2008) 4123-4130
    • (2008) J. Org. Chem. , vol.73 , pp. 4123-4130
    • Ora, M.1    Lonnberg, T.2    Florea-Wang, D.3    Zinnen, S.4    Karpeisky, A.5    Lonnberg, H.6
  • 55
    • 0029763197 scopus 로고    scopus 로고
    • Gamma-phosphate-substituted 2′-deoxynucleoside 5′-triphosphates as substrates for DNA polymerases
    • Arzumanov A.A., Semizarov D.G., Victorova L.S., Dyatkina N.B., and Krayevsky A.A. Gamma-phosphate-substituted 2′-deoxynucleoside 5′-triphosphates as substrates for DNA polymerases. J. Biol. Chem. 271 (1996) 24389-24394
    • (1996) J. Biol. Chem. , vol.271 , pp. 24389-24394
    • Arzumanov, A.A.1    Semizarov, D.G.2    Victorova, L.S.3    Dyatkina, N.B.4    Krayevsky, A.A.5
  • 56
    • 0032004388 scopus 로고    scopus 로고
    • 2′-Deoxynucleoside 5′-triphosphates modified at alpha-, beta- and gamma-phosphates as substrates for DNA polymerases
    • Alexandrova L.A., Skoblov A.Y., Jasko M.V., Victorova L.S., and Krayevsky A.A. 2′-Deoxynucleoside 5′-triphosphates modified at alpha-, beta- and gamma-phosphates as substrates for DNA polymerases. Nucleic Acids Res. 26 (1998) 778-786
    • (1998) Nucleic Acids Res. , vol.26 , pp. 778-786
    • Alexandrova, L.A.1    Skoblov, A.Y.2    Jasko, M.V.3    Victorova, L.S.4    Krayevsky, A.A.5
  • 61
    • 14744280358 scopus 로고    scopus 로고
    • Terminal phosphate-labeled nucleotides with improved substrate properties for homogeneous nucleic acid assays
    • Sood A., Kumar S., Nampalli S., Nelson J.R., Macklin J., and Fuller C.W. Terminal phosphate-labeled nucleotides with improved substrate properties for homogeneous nucleic acid assays. J. Am. Chem. Soc. 127 (2005) 2394-2395
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2394-2395
    • Sood, A.1    Kumar, S.2    Nampalli, S.3    Nelson, J.R.4    Macklin, J.5    Fuller, C.W.6
  • 62
    • 0032506228 scopus 로고    scopus 로고
    • Unblocking of chain-terminated primer by HIV-1 reverse transcriptase through a nucleotide-dependent mechanism
    • Meyer P.R., Matsuura S.E., So A.G., and Scott W.A. Unblocking of chain-terminated primer by HIV-1 reverse transcriptase through a nucleotide-dependent mechanism. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 13471-13476
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 13471-13476
    • Meyer, P.R.1    Matsuura, S.E.2    So, A.G.3    Scott, W.A.4
  • 63
    • 33750593306 scopus 로고    scopus 로고
    • Chain-terminating dinucleoside tetraphosphates are substrates for DNA polymerization by human immunodeficiency virus type 1 reverse transcriptase with increased activity against thymidine analog-resistant mutants
    • Meyer P.R., Smith A.J., Matsuura S.E., and Scott W.A. Chain-terminating dinucleoside tetraphosphates are substrates for DNA polymerization by human immunodeficiency virus type 1 reverse transcriptase with increased activity against thymidine analog-resistant mutants. Antimicrob. Agents Chemother. 50 (2006) 3607-3614
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 3607-3614
    • Meyer, P.R.1    Smith, A.J.2    Matsuura, S.E.3    Scott, W.A.4
  • 65
    • 15244349653 scopus 로고    scopus 로고
    • Substrate properties of dinucleoside 5′,5″-oligophosphates in the reactions catalyzed by HIV reverse transcriptase, E. coli DNA polymerase I, and E. coli RNA polymerase, Russ
    • Skoblov A.Y., Sosunov V.V., Victorova L.S., Skoblov Y.S., and Kukhanova M.K. Substrate properties of dinucleoside 5′,5″-oligophosphates in the reactions catalyzed by HIV reverse transcriptase, E. coli DNA polymerase I, and E. coli RNA polymerase, Russ. J. Bioorg. Chem. 31 (2005) 48-57
    • (2005) J. Bioorg. Chem. , vol.31 , pp. 48-57
    • Skoblov, A.Y.1    Sosunov, V.V.2    Victorova, L.S.3    Skoblov, Y.S.4    Kukhanova, M.K.5
  • 66
    • 43049106403 scopus 로고    scopus 로고
    • Novel HIV-1 reverse transcriptase inhibitors
    • Jochmans D. Novel HIV-1 reverse transcriptase inhibitors. Virus Res. 134 (2008) 171-185
    • (2008) Virus Res. , vol.134 , pp. 171-185
    • Jochmans, D.1
  • 67
    • 0033990454 scopus 로고    scopus 로고
    • Boranophosphate backbone: a mimic of phosphodiesters, phosphorothioates, and methyl phosphonates
    • Shaw B.R., Sergueev D., He K., Porter K., Summers J., Sergueeva Z., and Rait V. Boranophosphate backbone: a mimic of phosphodiesters, phosphorothioates, and methyl phosphonates. Methods Enzymol. 313 (2000) 226-257
    • (2000) Methods Enzymol. , vol.313 , pp. 226-257
    • Shaw, B.R.1    Sergueev, D.2    He, K.3    Porter, K.4    Summers, J.5    Sergueeva, Z.6    Rait, V.7
  • 70
    • 0033165851 scopus 로고    scopus 로고
    • A mechanism of AZT resistance: an increase in nucleotide-dependent primer unblocking by mutant HIV-1 reverse transcriptase
    • Meyer P.R., Matsuura S.E., Mian A.M., So A.G., and Scott W.A. A mechanism of AZT resistance: an increase in nucleotide-dependent primer unblocking by mutant HIV-1 reverse transcriptase. Mol. Cell 4 (1999) 35-43
    • (1999) Mol. Cell , vol.4 , pp. 35-43
    • Meyer, P.R.1    Matsuura, S.E.2    Mian, A.M.3    So, A.G.4    Scott, W.A.5
  • 71
    • 0032506055 scopus 로고    scopus 로고
    • Phenotypic mechanism of HIV-1 resistance to 3′-azido-3′-deoxythymidine (AZT): increased polymerization processivity and enhanced sensitivity to pyrophosphate of the mutant viral reverse transcriptase
    • Arion D., Kaushik N., McCormick S., Borkow G., and Parniak M.A. Phenotypic mechanism of HIV-1 resistance to 3′-azido-3′-deoxythymidine (AZT): increased polymerization processivity and enhanced sensitivity to pyrophosphate of the mutant viral reverse transcriptase. Biochemistry 37 (1998) 15908-15917
    • (1998) Biochemistry , vol.37 , pp. 15908-15917
    • Arion, D.1    Kaushik, N.2    McCormick, S.3    Borkow, G.4    Parniak, M.A.5
  • 73
    • 24344467910 scopus 로고    scopus 로고
    • Polyplex nanogel formulations for drug delivery of cytotoxic nucleoside analogs
    • Vinogradov S.V., Zeman A.D., Batrakova E.V., and Kabanov A.V. Polyplex nanogel formulations for drug delivery of cytotoxic nucleoside analogs. J. Control. Release 107 (2005) 143-157
    • (2005) J. Control. Release , vol.107 , pp. 143-157
    • Vinogradov, S.V.1    Zeman, A.D.2    Batrakova, E.V.3    Kabanov, A.V.4
  • 75
    • 29244487909 scopus 로고    scopus 로고
    • 2′, 3′-Dideoxynucleoside 5′-beta, gamma-(difluoromethylene) triphosphates with alpha-P-thio or alpha-P-seleno modifications: synthesis and their inhibition of HIV-1 reverse transcriptase
    • Boyle N., Fagan P., Brooks J., Prhavc M., Lambert J., and Cook P.D. 2′, 3′-Dideoxynucleoside 5′-beta, gamma-(difluoromethylene) triphosphates with alpha-P-thio or alpha-P-seleno modifications: synthesis and their inhibition of HIV-1 reverse transcriptase. Nucleosides Nucleotides Nucleic Acids 24 (2005) 1651-1664
    • (2005) Nucleosides Nucleotides Nucleic Acids , vol.24 , pp. 1651-1664
    • Boyle, N.1    Fagan, P.2    Brooks, J.3    Prhavc, M.4    Lambert, J.5    Cook, P.D.6
  • 76
    • 77949546606 scopus 로고    scopus 로고
    • Bioreversible protection of nucleosidediphosphates - synthesis and properties
    • Schulz T., Jessen H.J., Balzarini J., and Meier C. Bioreversible protection of nucleosidediphosphates - synthesis and properties. Antiviral Res. 82 (2009) A63
    • (2009) Antiviral Res. , vol.82
    • Schulz, T.1    Jessen, H.J.2    Balzarini, J.3    Meier, C.4
  • 77
    • 33646875941 scopus 로고    scopus 로고
    • Comparison of nanogel drug carriers and their formulations with nucleoside 5′-triphosphates
    • Vinogradov S.V., Kohli E., and Zeman A.D. Comparison of nanogel drug carriers and their formulations with nucleoside 5′-triphosphates. Pharm. Res. 23 (2006) 920-930
    • (2006) Pharm. Res. , vol.23 , pp. 920-930
    • Vinogradov, S.V.1    Kohli, E.2    Zeman, A.D.3
  • 78
    • 55749093075 scopus 로고    scopus 로고
    • Polymeric nanogels containing the triphosphate form of cytotoxic nucleoside analogues show antitumor activity against breast and colorectal cancer cell lines
    • Galmarini C.M., Warren G., Kohli E., Zeman A., Mitin A., and Vinogradov S.V. Polymeric nanogels containing the triphosphate form of cytotoxic nucleoside analogues show antitumor activity against breast and colorectal cancer cell lines. Mol. Cancer Ther. 7 (2008) 3373-3380
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 3373-3380
    • Galmarini, C.M.1    Warren, G.2    Kohli, E.3    Zeman, A.4    Mitin, A.5    Vinogradov, S.V.6
  • 79
    • 60049085781 scopus 로고    scopus 로고
    • Advanced nanogel engineering for drug delivery
    • Raemdonck K., Demeester J., and De Smedt S. Advanced nanogel engineering for drug delivery. Soft Matter 5 (2009) 707-715
    • (2009) Soft Matter , vol.5 , pp. 707-715
    • Raemdonck, K.1    Demeester, J.2    De Smedt, S.3
  • 80
    • 0037183526 scopus 로고    scopus 로고
    • A reexamination of the nucleotide incorporation fidelity of DNA polymerases
    • Showalter A.K., and Tsai M.-D. A reexamination of the nucleotide incorporation fidelity of DNA polymerases. Biochemistry 41 (2002) 10571-10576
    • (2002) Biochemistry , vol.41 , pp. 10571-10576
    • Showalter, A.K.1    Tsai, M.-D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.