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Volumn 7, Issue 5, 2012, Pages

Pan-pathway based interaction profiling of FDA-approved nucleoside and nucleobase analogs with enzymes of the human nucleotide metabolism

Author keywords

[No Author keywords available]

Indexed keywords

5 AZA 2' DEOXYCYTIDINE; ACICLOVIR; ADENOSINE TRIPHOSPHATE; CLADRIBINE; CLOFARABINE; CYTARABINE; DEOXYCYTIDINE KINASE; EMTRICITABINE; ENZYME; FLOXURIDINE; FLUOROURACIL; GANCICLOVIR; GEMCITABINE; GUANINE DEAMINASE; IDOXURIDINE; LAMIVUDINE; MERCAPTOPURINE; NUCLEIC ACID BASE; NUCLEOSIDE ANALOG; PENCICLOVIR; TELBIVUDINE; TIOGUANINE; TRIFLURIDINE; UNCLASSIFIED DRUG; UNINDEXED DRUG; URIDINE PHOSPHORYLASE; URIDINE PHOSPHORYLASE 1; VALACICLOVIR; VIDARABINE; ZALCITABINE; ZIDOVUDINE;

EID: 84861467901     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0037724     Document Type: Article
Times cited : (17)

References (43)
  • 1
    • 61449189645 scopus 로고    scopus 로고
    • Anti-HIV drugs: 25 compounds approved within 25 years after the discovery of HIV
    • De Clercq E, (2009) Anti-HIV drugs: 25 compounds approved within 25 years after the discovery of HIV. Int J Antimicrob Agents 33: 307-20.
    • (2009) Int J Antimicrob Agents , vol.33 , pp. 307-320
    • de Clercq, E.1
  • 2
    • 30344486584 scopus 로고    scopus 로고
    • Antiviral prodrugs - the development of successful prodrug strategies for antiviral chemotherapy
    • De Clercq E, Field HJ, (2006) Antiviral prodrugs- the development of successful prodrug strategies for antiviral chemotherapy. Br J Pharmacol 147: 1-11.
    • (2006) Br J Pharmacol , vol.147 , pp. 1-11
    • de Clercq, E.1    Field, H.J.2
  • 3
    • 0036636579 scopus 로고    scopus 로고
    • Nucleoside analogues and nucleobases in cancer treatment
    • Galmarini CM, Mackey JR, Dumontet C, (2002) Nucleoside analogues and nucleobases in cancer treatment. Lancet Oncol 3: 415-24.
    • (2002) Lancet Oncol , vol.3 , pp. 415-424
    • Galmarini, C.M.1    Mackey, J.R.2    Dumontet, C.3
  • 4
    • 0018247948 scopus 로고
    • The fluoropyrimidines: biochemical mechanisms and design of clinical trials
    • Friedman MA, Sadee W, (1978) The fluoropyrimidines: biochemical mechanisms and design of clinical trials. Cancer Chemother Pharmacol 1: 77-82.
    • (1978) Cancer Chemother Pharmacol , vol.1 , pp. 77-82
    • Friedman, M.A.1    Sadee, W.2
  • 5
    • 77952303898 scopus 로고    scopus 로고
    • Understanding specificity in metabolic pathways-structural biology of human nucleotide metabolism
    • Welin M, Nordlund P, (2010) Understanding specificity in metabolic pathways-structural biology of human nucleotide metabolism. Biochem Biophys Res Commun 396: 157-63.
    • (2010) Biochem Biophys Res Commun , vol.396 , pp. 157-163
    • Welin, M.1    Nordlund, P.2
  • 6
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • Ericsson UB, Hallberg BM, Detitta GT, Dekker N, Nordlund P, (2006) Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal Biochem 357: 289-98.
    • (2006) Anal Biochem , vol.357 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    Detitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 7
    • 33750470057 scopus 로고    scopus 로고
    • Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination
    • Vedadi M, Niesen FH, Allali-Hassani A, Fedorov OY, Finerty PJ Jr, et al. (2006) Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination. Proc Natl Acad Sci U S A 103: 15835-40.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 15835-15840
    • Vedadi, M.1    Niesen, F.H.2    Allali-Hassani, A.3    Fedorov, O.Y.4    Finerty Jr., P.J.5
  • 8
    • 38049155899 scopus 로고    scopus 로고
    • A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases
    • Fedorov O, Marsden B, Pogacic V, Rellos P, Muller S, et al. (2007) A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases. Proc Natl Acad Sci U S A 104: 20523-8.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 20523-20528
    • Fedorov, O.1    Marsden, B.2    Pogacic, V.3    Rellos, P.4    Muller, S.5
  • 10
    • 33751559579 scopus 로고    scopus 로고
    • Screening for ligands using a generic and high-throughput light-scattering-based assay
    • Senisterra GA, Markin E, Yamazaki K, Hui R, Vedadi M, et al. (2006) Screening for ligands using a generic and high-throughput light-scattering-based assay. J Biomol Screen 11: 940-8.
    • (2006) J Biomol Screen , vol.11 , pp. 940-948
    • Senisterra, G.A.1    Markin, E.2    Yamazaki, K.3    Hui, R.4    Vedadi, M.5
  • 13
    • 77958614232 scopus 로고    scopus 로고
    • Hepatitis C treatment: current and future perspectives
    • Munir S, Saleem S, Idrees M, Tariq A, Butt S, et al. (2010) Hepatitis C treatment: current and future perspectives. Virol J 7: 296.
    • (2010) Virol J , vol.7 , pp. 296
    • Munir, S.1    Saleem, S.2    Idrees, M.3    Tariq, A.4    Butt, S.5
  • 14
    • 78650780786 scopus 로고    scopus 로고
    • Treatment of chronic hepatitis B: Evolution over two decades
    • Yuen MF, Lai CL, (2011) Treatment of chronic hepatitis B: Evolution over two decades. J Gastroenterol Hepatol 26: 138-43.
    • (2011) J Gastroenterol Hepatol , vol.26 , pp. 138-143
    • Yuen, M.F.1    Lai, C.L.2
  • 15
    • 77956191215 scopus 로고    scopus 로고
    • Biophysical characterization of recombinant proteins: a key to higher structural genomics success
    • Vedadi M, Arrowsmith CH, Allali-Hassani A, Senisterra G, Wasney GA, (2010) Biophysical characterization of recombinant proteins: a key to higher structural genomics success. J Struct Biol 172: 107-19.
    • (2010) J Struct Biol , vol.172 , pp. 107-119
    • Vedadi, M.1    Arrowsmith, C.H.2    Allali-Hassani, A.3    Senisterra, G.4    Wasney, G.A.5
  • 17
    • 33947103315 scopus 로고    scopus 로고
    • Deoxynucleoside Analogs in Cancer Therapy
    • First edition, ed. Teicher BA, Humana Press Inc. Totowa, New Jersey
    • Peters GJ, (2006) Deoxynucleoside Analogs in Cancer Therapy. First edition, ed. Teicher BA, Humana Press Inc. Totowa, New Jersey.
    • (2006)
    • Peters, G.J.1
  • 18
    • 0036078423 scopus 로고    scopus 로고
    • Cytotoxic activity of 2',2'-difluorodeoxycytidine, 5-aza-2'-deoxycytidine and cytosine arabinoside in cells transduced with deoxycytidine kinase gene
    • Beausejour CM, Gagnon J, Primeau M, Momparler RL, (2002) Cytotoxic activity of 2',2'-difluorodeoxycytidine, 5-aza-2'-deoxycytidine and cytosine arabinoside in cells transduced with deoxycytidine kinase gene. Biochem Biophys Res Commun 293: 1478-84.
    • (2002) Biochem Biophys Res Commun , vol.293 , pp. 1478-1484
    • Beausejour, C.M.1    Gagnon, J.2    Primeau, M.3    Momparler, R.L.4
  • 19
    • 77952554598 scopus 로고    scopus 로고
    • The kinetic mechanism of human uridine phosphorylase 1: Towards the development of enzyme inhibitors for cancer chemotherapy
    • Renck D, Ducati RG, Palma MS, Santos DS, Basso LA, (2010) The kinetic mechanism of human uridine phosphorylase 1: Towards the development of enzyme inhibitors for cancer chemotherapy. Arch Biochem Biophys 497: 35-42.
    • (2010) Arch Biochem Biophys , vol.497 , pp. 35-42
    • Renck, D.1    Ducati, R.G.2    Palma, M.S.3    Santos, D.S.4    Basso, L.A.5
  • 20
    • 0037089505 scopus 로고    scopus 로고
    • Uridine phosphorylase (-/-) murine embryonic stem cells clarify the key role of this enzyme in the regulation of the pyrimidine salvage pathway and in the activation of fluoropyrimidines
    • Cao D, Russell RL, Zhang D, Leffert JJ, Pizzorno G, (2002) Uridine phosphorylase (-/-) murine embryonic stem cells clarify the key role of this enzyme in the regulation of the pyrimidine salvage pathway and in the activation of fluoropyrimidines. Cancer Res 62: 2313-7.
    • (2002) Cancer Res , vol.62 , pp. 2313-2317
    • Cao, D.1    Russell, R.L.2    Zhang, D.3    Leffert, J.J.4    Pizzorno, G.5
  • 21
    • 0018247948 scopus 로고
    • The fluoropyrimidines: biochemical mechanisms and design of clinical trials
    • Friedman MA, Sadee W, (1978) The fluoropyrimidines: biochemical mechanisms and design of clinical trials. Cancer Chemother Pharmacol 1: 77-82.
    • (1978) Cancer Chemother Pharmacol , vol.1 , pp. 77-82
    • Friedman, M.A.1    Sadee, W.2
  • 22
    • 0037130273 scopus 로고    scopus 로고
    • Homeostatic control of uridine and the role of uridine phosphorylase: a biological and clinical update
    • Pizzorno G, Cao D, Leffert JJ, Russell RL, Zhang D, et al. (2002) Homeostatic control of uridine and the role of uridine phosphorylase: a biological and clinical update. Biochim Biophys Acta 1587: 133-44.
    • (2002) Biochim Biophys Acta , vol.1587 , pp. 133-144
    • Pizzorno, G.1    Cao, D.2    Leffert, J.J.3    Russell, R.L.4    Zhang, D.5
  • 23
    • 15644382548 scopus 로고    scopus 로고
    • Phase I clinical and pharmacological studies of benzylacyclouridine, a uridine phosphorylase inhibitor
    • Pizzorno G, Yee L, Burtness BA, Marsh JC, Darnowski JW, et al. (1998) Phase I clinical and pharmacological studies of benzylacyclouridine, a uridine phosphorylase inhibitor. Clin Cancer Res 4: 1165-75.
    • (1998) Clin Cancer Res , vol.4 , pp. 1165-1175
    • Pizzorno, G.1    Yee, L.2    Burtness, B.A.3    Marsh, J.C.4    Darnowski, J.W.5
  • 24
    • 0025221427 scopus 로고
    • Benzylacyclouridine reverses azidothymidine-induced marrow suppression without impairment of anti-human immunodeficiency virus activity
    • Calabresi P, Falcone A, St Clair MH, Wiemann MC, Chu SH, et al. (1990) Benzylacyclouridine reverses azidothymidine-induced marrow suppression without impairment of anti-human immunodeficiency virus activity. Blood 76: 2210-5.
    • (1990) Blood , vol.76 , pp. 2210-2215
    • Calabresi, P.1    Falcone, A.2    St Clair, M.H.3    Wiemann, M.C.4    Chu, S.H.5
  • 25
    • 0033583291 scopus 로고    scopus 로고
    • Cloning and characterization of human guanine deaminase. Purification and partial amino acid sequence of the mouse protein
    • Yuan G, Bin JC, McKay DJ, Snyder FF, (1999) Cloning and characterization of human guanine deaminase. Purification and partial amino acid sequence of the mouse protein. J Biol Chem 274: 8175-80.
    • (1999) J Biol Chem , vol.274 , pp. 8175-8180
    • Yuan, G.1    Bin, J.C.2    McKay, D.J.3    Snyder, F.F.4
  • 27
    • 33750324770 scopus 로고    scopus 로고
    • Histochemical and immunohistochemical investigation of guanase and nedasin in human tissues
    • Kubo K, Honda H, Honda H, Sannomiya K, Aying Y, et al. (2006) Histochemical and immunohistochemical investigation of guanase and nedasin in human tissues. J Med Invest 53: 264-70.
    • (2006) J Med Invest , vol.53 , pp. 264-270
    • Kubo, K.1    Honda, H.2    Honda, H.3    Sannomiya, K.4    Aying, Y.5
  • 28
    • 0037762732 scopus 로고    scopus 로고
    • Clinical value of the determination of serum guanase activity in patients with chronic hepatitis type C
    • Matsunaga H, Honda H, Kubo K, Sannomiya K, Cui X, et al. (2003) Clinical value of the determination of serum guanase activity in patients with chronic hepatitis type C. J Med Invest 50: 64-71.
    • (2003) J Med Invest , vol.50 , pp. 64-71
    • Matsunaga, H.1    Honda, H.2    Kubo, K.3    Sannomiya, K.4    Cui, X.5
  • 29
    • 62949134540 scopus 로고    scopus 로고
    • Phylogenetic analysis and molecular evolution of guanine deaminases: from guanine to dendrites
    • Fernandez JR, Byrne B, Firestein BL, (2009) Phylogenetic analysis and molecular evolution of guanine deaminases: from guanine to dendrites. J Mol Evol 69: 227-35.
    • (2009) J Mol Evol , vol.69 , pp. 227-235
    • Fernandez, J.R.1    Byrne, B.2    Firestein, B.L.3
  • 30
    • 0018791276 scopus 로고
    • Characterization of purified guanine aminohydrolase
    • Bergstrom JD, Bieber AL, (1979) Characterization of purified guanine aminohydrolase. Arch Biochem Biophys 194: 107-16.
    • (1979) Arch Biochem Biophys , vol.194 , pp. 107-116
    • Bergstrom, J.D.1    Bieber, A.L.2
  • 31
    • 0017828080 scopus 로고
    • Purification and properties of pig brain guanine deaminase
    • Rossi CA, Hakim G, Solaini G, (1978) Purification and properties of pig brain guanine deaminase. Biochim Biophys Acta 526: 235-46.
    • (1978) Biochim Biophys Acta , vol.526 , pp. 235-246
    • Rossi, C.A.1    Hakim, G.2    Solaini, G.3
  • 32
    • 77956344237 scopus 로고    scopus 로고
    • Identification of small molecule compounds with higher binding affinity to guanine deaminase (cypin) than guanine
    • Fernandez JR, Sweet ES, Welsh WJ, Firestein BL, (2010) Identification of small molecule compounds with higher binding affinity to guanine deaminase (cypin) than guanine. Bioorg Med Chem 18: 6748-55.
    • (2010) Bioorg Med Chem , vol.18 , pp. 6748-6755
    • Fernandez, J.R.1    Sweet, E.S.2    Welsh, W.J.3    Firestein, B.L.4
  • 33
    • 0037082119 scopus 로고    scopus 로고
    • Ribonucleotide reductases: the evolution of allosteric regulation
    • Reichard P, (2002) Ribonucleotide reductases: the evolution of allosteric regulation. Arch Biochem Biophys 397: 149-55.
    • (2002) Arch Biochem Biophys , vol.397 , pp. 149-155
    • Reichard, P.1
  • 35
    • 79952331478 scopus 로고    scopus 로고
    • Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization
    • Fairman JW, Wijerathna SR, Ahmad MF, Xu H, Nakano R, et al. (2011) Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Nat Struct Mol Biol 18: 316-22.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 316-322
    • Fairman, J.W.1    Wijerathna, S.R.2    Ahmad, M.F.3    Xu, H.4    Nakano, R.5
  • 36
    • 0030769662 scopus 로고    scopus 로고
    • The effects of high salt concentrations on the regulation of the substrate specificity of human recombinant deoxycytidine kinase
    • Usova EV, Eriksson S, (1997) The effects of high salt concentrations on the regulation of the substrate specificity of human recombinant deoxycytidine kinase. Eur J Biochem 248: 762-6.
    • (1997) Eur J Biochem , vol.248 , pp. 762-766
    • Usova, E.V.1    Eriksson, S.2
  • 37
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W, (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Cryst 26: 795-800.
    • (1993) J Appl Cryst , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 39
  • 42
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K, (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60: 2256-68.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 43
    • 0842302302 scopus 로고    scopus 로고
    • DeLano Scientific LLC
    • Available at, version, CA, USA: Palo Alto
    • DeLano WL, (2008) DeLano Scientific LLC, CA, USA: Palo Alto. 1.2) Available at http://www.pymol.org (version.
    • (2008) , vol.1 , Issue.2
    • DeLano, W.L.1


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