메뉴 건너뛰기




Volumn 15, Issue 6, 2005, Pages 659-673

Ribonucleotide reductase: Target therapy for human disease

Author keywords

Cancer; Didox; Hydroxyurea; Ribonucleotide reductase inhibitor; Trimidox; Viral infection; Virostatic agent

Indexed keywords

3,4 DIHYDROXYBENZOHYDROXAMIC ACID; ABACAVIR; ANTINEOPLASTIC AGENT; ANTIRETROVIRUS AGENT; BENZOHYDROXAMIC ACID; CYCLOPHOSPHAMIDE; CYTARABINE; DIDANOSINE; DOXORUBICIN; ENZYME INHIBITOR; HYDROXYLAMINE; HYDROXYUREA; INDINAVIR; PHENOL DERIVATIVE; PROTEIN P53; QUERCETIN; RESVERATROL; RIBONUCLEOTIDE REDUCTASE; RNA DIRECTED DNA POLYMERASE INHIBITOR; STAVUDINE;

EID: 21244443856     PISSN: 13543776     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543776.15.6.659     Document Type: Review
Times cited : (4)

References (114)
  • 1
    • 2542504483 scopus 로고    scopus 로고
    • Structure, function, and mechanism of ribonucleotide redctase
    • KOLBERG M, STRAND KR, GRAFF P et al.: Structure, function, and mechanism of ribonucleotide redctase. Biochemica Biophys Acta (2004) 1699:1-34.
    • (2004) Biochemica Biophys. Acta , vol.1699 , pp. 1-34
    • Kolberg, M.1    Strand, K.R.2    Graff, P.3
  • 2
    • 0026582672 scopus 로고
    • Ribonucleotide reductase: Regulation, regulation, regulation
    • ELLEDGE SJ, ZHOU Z, ALLEN JB: Ribonucleotide reductase: regulation, regulation, regulation. Trends Biochem. Sci. (1992) 17:119-123.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 119-123
    • Elledge, S.J.1    Zhou, Z.2    Allen, J.B.3
  • 3
    • 0014962872 scopus 로고
    • Ribonucleotide reductase and cell proliferation
    • ELFORD HL, FREESE M, PASSAMIANI E et al.: Ribonucleotide reductase and cell proliferation. J. Biol. Chem. (1970) 245:5228-5233.
    • (1970) J. Biol. Chem. , vol.245 , pp. 5228-5233
    • Elford, H.L.1    Freese, M.2    Passamiani, E.3
  • 4
    • 0015457539 scopus 로고
    • Functional regulation of mammalian ribonucleotide reductase
    • ELFORD HL: Functional regulation of mammalian ribonucleotide reductase. (1972) Adv. Enz. Reg. 10:19-38.
    • (1972) Adv. Enz. Reg. , vol.10 , pp. 19-38
    • Elford, H.L.1
  • 5
    • 0017364109 scopus 로고
    • Enzymology of cancer cells
    • WEBER G: Enzymology of cancer cells. N. Engl. J. Med. (1977) 296:486-493.
    • (1977) N. Engl. J. Med. , vol.296 , pp. 486-493
    • Weber, G.1
  • 6
    • 0004155427 scopus 로고    scopus 로고
    • 5th Edition. Freeman & Company, NY, USA
    • STRYER L: Biochemistry, 5th Edition. Freeman & Company, NY, USA (2004).
    • (2004) Biochemistry
    • Stryer, L.1
  • 7
    • 0020541188 scopus 로고
    • Ribonucleotide reductase - A radical enzyme
    • REICHARD P, EHRENBERG A: Ribonucleotide reductase - a radical enzyme. Science (1983) 221:514-519.
    • (1983) Science , vol.221 , pp. 514-519
    • Reichard, P.1    Ehrenberg, A.2
  • 8
    • 0025366033 scopus 로고
    • S-phase-specific expression of mammalian ribonucleotide reductase R1 and R2 subunit mRNAs
    • BJORKLUND S, SKOG S, TRIBUKAIT B et al.: S-phase-specific expression of mammalian ribonucleotide reductase R1 and R2 subunit mRNAs. Biochemistry (1990) 29:5452-5458.
    • (1990) Biochemistry , vol.29 , pp. 5452-5458
    • Bjorklund, S.1    Skog, S.2    Tribukait, B.3
  • 9
    • 0027177564 scopus 로고
    • From RNA to DNA, why so many ribonucleotide reductases?
    • REICHARD P: From RNA to DNA, why so many ribonucleotide reductases? Science (1993) 260:1773-1777.
    • (1993) Science , vol.260 , pp. 1773-1777
    • Reichard, P.1
  • 10
    • 0035544604 scopus 로고    scopus 로고
    • Structure and function of the radical enzyme ribonucleotide reductase
    • EKLUND H, UHLIN U, FARNEGARDH M et al.: Structure and function of the radical enzyme ribonucleotide reductase. Prog. Biophys. Mol. Biol. (2001) 77:177-268.
    • (2001) Prog. Biophys. Mol. Biol. , vol.77 , pp. 177-268
    • Eklund, H.1    Uhlin, U.2    Farnegardh, M.3
  • 11
    • 0026482281 scopus 로고
    • The redox centers of ribonucleotide reductase of Escherichia coli
    • FONTECAVE M, NORDLUND P, EKLUND H et al.: The redox centers of ribonucleotide reductase of Escherichia coli. Adv. Enzymol. (1992) 65:147-183.
    • (1992) Adv. Enzymol. , vol.65 , pp. 147-183
    • Fontecave, M.1    Nordlund, P.2    Eklund, H.3
  • 12
    • 0027283896 scopus 로고
    • Structure and function of the Escherichia coli ribonucleotide reductase protein R2
    • NORDLUND P, EKLUND H: Structure and function of the Escherichia coli ribonucleotide reductase protein R2. J. Mol. Biol. (1993) 232:123-164.
    • (1993) J. Mol. Biol. , vol.232 , pp. 123-164
    • Nordlund, P.1    Eklund, H.2
  • 13
    • 0000269853 scopus 로고    scopus 로고
    • Ribonucleotide reductase in mammalian systems
    • Sigel HA (Ed.), Marcel-Dekker, Inc., NY, USA
    • THELANDER L, GRASLUND A: Ribonucleotide reductase in mammalian systems. In: Metal Ions in Biological Systems. Sigel HA (Ed.), Marcel-Dekker, Inc., NY, USA (1993) 30:109-129.
    • (1993) Metal Ions in Biological Systems , vol.30 , pp. 109-129
    • Thelander, L.1    Graslund, A.2
  • 14
    • 0022763898 scopus 로고
    • Identification of the stable free radical tyrosine residue in ribonucleotide reductase
    • LARSSON A, SJOBERG BM: Identification of the stable free radical tyrosine residue in ribonucleotide reductase. EMBO J. (1986) 5:2037-2040.
    • (1986) EMBO J. , vol.5 , pp. 2037-2040
    • Larsson, A.1    Sjoberg, B.M.2
  • 15
    • 0025364136 scopus 로고
    • Activation of the iron-containing R2 protein of ribonucleotide reductase by hydrogen peroxide
    • SAHLIN M, SJOBERG BM, BACKES G et al.: Activation of the iron-containing R2 protein of ribonucleotide reductase by hydrogen peroxide. Biochem. Biophys. Res. Common. (1990) 167:813-818.
    • (1990) Biochem. Biophys. Res. Common. , vol.167 , pp. 813-818
    • Sahlin, M.1    Sjoberg, B.M.2    Backes, G.3
  • 16
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • HOLMGREN A: Thioredoxin and glutaredoxin systems. J. Biol. Chem. (1989) 264:13963-13966.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 17
    • 0029974121 scopus 로고    scopus 로고
    • Altosteric regulation of the third ribonucleotide reductase (NrdEF enzyme) from enterobacteriaceae
    • ELIASSON R, PONTIS E, JORDAN A et al.: Altosteric regulation of the third ribonucleotide reductase (NrdEF enzyme) from enterobacteriaceae. J. Biol. Chem. (1996) 271:26582-26587.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26582-26587
    • Eliasson, R.1    Pontis, E.2    Jordan, A.3
  • 18
    • 0030009737 scopus 로고    scopus 로고
    • The ribonucleotide reductase system of Lactococcus lactis - Characterization of an nrdEF enzyme and a new electron transport procein
    • JORDON A, PONTIS E, ASLUND F et al.: The ribonucleotide reductase system of Lactococcus lactis - characterization of an nrdEF enzyme and a new electron transport procein. J. Biol. Chem. (1996) 271:8779-8785.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8779-8785
    • Jordon, A.1    Pontis, E.2    Aslund, F.3
  • 19
    • 0028099575 scopus 로고
    • Isolation of ribonucleotide reductase from Mycobacterium tuberculosis and cloning, expression, and purification of the large subunit
    • YANG FD, LU GZ, RUBIN H: Isolation of ribonucleotide reductase from Mycobacterium tuberculosis and cloning, expression, and purification of the large subunit. J Bacteriol. (1994) 176:6738-6743.
    • (1994) J. Bacteriol. , vol.176 , pp. 6738-6743
    • Yang, F.D.1    Lu, G.Z.2    Rubin, H.3
  • 20
    • 0029956573 scopus 로고    scopus 로고
    • The Bacillus subtilis genes for ribonucleotide reductase are similar to the genes for the second class I NrdE/NrdF enzymes of Enterobacteriaceae
    • SCOTTI C, VALBUZZI A, PEREGO M et al.: The Bacillus subtilis genes for ribonucleotide reductase are similar to the genes for the second class I NrdE/NrdF enzymes of Enterobacteriaceae. Microbiol. UK (1996) 142:2995-3004.
    • (1996) Microbiol. UK , vol.142 , pp. 2995-3004
    • Scotti, C.1    Valbuzzi, A.2    Perego, M.3
  • 21
    • 0028829125 scopus 로고
    • The minimal gene complement of Mycoplasma genitalium
    • FRASER CM, VENTER JC: The minimal gene complement of Mycoplasma genitalium. Science (1995) 270:397-403.
    • (1995) Science , vol.270 , pp. 397-403
    • Fraser, C.M.1    Venter, J.C.2
  • 22
    • 0029618389 scopus 로고
    • Two different operons for the same function: Comparison of the Salmonella typhimurium nrdAb and nrdAF genes
    • JORDAN A, GILBERT I, BARBE J: Two different operons for the same function: comparison of the Salmonella typhimurium nrdAb and nrdAF genes. Gene (1995) 167:75-79.
    • (1995) Gene , vol.167 , pp. 75-79
    • Jordan, A.1    Gilbert, I.2    Barbe, J.3
  • 23
    • 0030068006 scopus 로고    scopus 로고
    • Promotor identification and expression analysis of Salmonella typhimurimum and Escherichia coli nrdEF operons encoding one of two class I ribonucleotide reductases present in both bacteria
    • JORDAN A, ARAGALL E, GILBERT I et al.: Promotor identification and expression analysis of Salmonella typhimurimum and Escherichia coli nrdEF operons encoding one of two class I ribonucleotide reductases present in both bacteria. Mol. Microbiol. (1996) 19:777-790.
    • (1996) Mol. Microbiol. , vol.19 , pp. 777-790
    • Jordan, A.1    Aragall, E.2    Gilbert, I.3
  • 24
    • 0028172124 scopus 로고
    • Coenzyme B-12-dependent ribonucleotide reductase: Evidence for the participation of five cysteine residues in ribonucleotide reaction
    • BOOKERS, LICHT S, BRODERICK J et al.: Coenzyme B-12-dependent ribonucleotide reductase: evidence for the participation of five cysteine residues in ribonucleotide reaction. Biochemistry (1994) 33:12676-12685.
    • (1994) Biochemistry , vol.33 , pp. 12676-12685
    • Bookers1    Licht, S.2    Broderick, J.3
  • 25
    • 0024987021 scopus 로고
    • Ribonucleotide reductases
    • STUBBE JA: Ribonucleotide reductases. Adv. Enzymol. (1990) 63:349-419.
    • (1990) Adv. Enzymol. , vol.63 , pp. 349-419
    • Stubbe, J.A.1
  • 26
    • 0031025616 scopus 로고    scopus 로고
    • Ribonucleotide reductase in the archeon Pyrococcus furiosus: A critical enzyme in the evolution of the DNA genomes?
    • RIERA J, ROBB FT, WEISS R et al.: Ribonucleotide reductase in the archeon Pyrococcus furiosus: a critical enzyme in the evolution of the DNA genomes? Proc. Soc. Natl. Acad. Sci. USA (1997) 94:514-519.
    • (1997) Proc. Soc. Natl. Acad. Sci. USA , vol.94 , pp. 514-519
    • Riera, J.1    Robb, F.T.2    Weiss, R.3
  • 27
    • 0000269853 scopus 로고    scopus 로고
    • The B-12 dependent ribonucleotide reductase in mammalian systems
    • Sigel, HA (Ed.), Marcel Dekker, Inc., NY, USA
    • TAUER A, BENNER SA: The B-12 dependent ribonucleotide reductase in mammalian systems. In: Metal Ions in Biological Systems. Sigel, HA (Ed.), Marcel Dekker, Inc., NY, USA (1997) 30:109-129.
    • (1997) Metal Ions in Biological Systems , vol.30 , pp. 109-129
    • Tauer, A.1    Benner, S.A.2
  • 28
    • 0030603925 scopus 로고    scopus 로고
    • The ten-suranded β/α barrel in ribonucleotide reductase protein R1
    • UHLIN U, EKLUND H: The ten-suranded β/α barrel in ribonucleotide reductase protein R1. J. Mol. Biol. (1996) 262:358-369.
    • (1996) J. Mol. Biol. , vol.262 , pp. 358-369
    • Uhlin, U.1    Eklund, H.2
  • 29
    • 0025363362 scopus 로고
    • The anaerobic ribonucleoside triphosphate reductase from Escherichia coli ribonucleotide reductase requires S-adenosylmethionine as a cofactor
    • ELIASSON R, FONTECAVE M, JORNVALL H et al.: The anaerobic ribonucleoside triphosphate reductase from Escherichia coli ribonucleotide reductase requires S-adenosylmethionine as a cofactor. Proc. Natl. Acad. Sci. USA (1990) 87:3314-3318.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3314-3318
    • Eliasson, R.1    Fontecave, M.2    Jornvall, H.3
  • 30
    • 0035849574 scopus 로고    scopus 로고
    • Activation of class III ribonucleotide reductase from Escherichia coli. The electron transfer from the iron-sulfur center to S-adenosylmethionine
    • PADOVANI D, THOMAS F, TRAUTWEIN AX et al.: Activation of class III ribonucleotide reductase from Escherichia coli. The electron transfer from the iron-sulfur center to S-adenosylmethionine. Biochemistry (2001) 40:6713-6719.
    • (2001) Biochemistry , vol.40 , pp. 6713-6719
    • Padovani, D.1    Thomas, F.2    Trautwein, A.X.3
  • 31
    • 0035823567 scopus 로고    scopus 로고
    • The anaerobic ribonucleotide reductase from Lactococcus lactis. Interactions between the two proteins NRDD and NRDG
    • TORRENTS E, ELIASSON R, WOLPHNER H et al.: The anaerobic ribonucleotide reductase from Lactococcus lactis. Interactions between the two proteins NRDD and NRDG. J. Biol. Chem. (2001) 276:33488-33494.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33488-33494
    • Torrents, E.1    Eliasson, R.2    Wolphner, H.3
  • 32
    • 0028837286 scopus 로고    scopus 로고
    • Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activating enzyme
    • SUN XY, ELIAISSON R, PONTIS F et al.: Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activating enzyme. J. Biol. Chem. 270:2443-2446.
    • J. Biol. Chem. , vol.270 , pp. 2443-2446
    • Sun, X.Y.1    Eliaisson, R.2    Pontis, F.3
  • 33
    • 0029048182 scopus 로고
    • Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli
    • MULLIEZ E, OLLAGNIER S, FONTECAVE M et al.: Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli. Proc. Natl. Acad. Soc. USA (1995) 92:8759-8762.
    • (1995) Proc. Natl. Acad. Soc. USA , vol.92 , pp. 8759-8762
    • Mulliez, E.1    Ollagnier, S.2    Fontecave, M.3
  • 34
    • 13344279373 scopus 로고    scopus 로고
    • The free radical of the anaerobic ribonucleotide reductase from Escherichia coli is at glycine 681
    • SUN X, OLLAGNIER S, SCHMIDT PP et al.: The free radical of the anaerobic ribonucleotide reductase from Escherichia coli is at glycine 681. J. Biol. Chem. (1996) 271:6827-6831.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6827-6831
    • Sun, X.1    Ollagnier, S.2    Schmidt, P.P.3
  • 35
    • 0027492116 scopus 로고
    • Unusual clustering of carboxyl side chains in the core of iron-free ribonucleotide reductase
    • ABERG A, NORLUND P, EKLUND H: Unusual clustering of carboxyl side chains in the core of iron-free ribonucleotide reductase. Nature (1993) 361:276-278.
    • (1993) Nature , vol.361 , pp. 276-278
    • Aberg, A.1    Norlund, P.2    Eklund, H.3
  • 36
    • 0032575296 scopus 로고    scopus 로고
    • Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: Structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins
    • LOGAN DT, DEMARE F, PERSSON BO et al.: Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants: structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins. Biochemistry (1998) 37:10798-10807.
    • (1998) Biochemistry , vol.37 , pp. 10798-10807
    • Logan, D.T.1    Demare, F.2    Persson, B.O.3
  • 37
    • 0032516890 scopus 로고    scopus 로고
    • Preserved catalytic site in an engineered ribonucletide reductase R2 protein with a nonphysiological radical transfer pathway. The importance of hydrogen bond connections between the participating residues
    • EKBERG M, POTSCH S, SADIN E et al.: Preserved catalytic site in an engineered ribonucletide reductase R2 protein with a nonphysiological radical transfer pathway. The importance of hydrogen bond connections between the participating residues. J. Biol. Chem. (1998) 273:21003-21008.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21003-21008
    • Ekberg, M.1    Potsch, S.2    Sadin, E.3
  • 38
    • 0030721530 scopus 로고    scopus 로고
    • Reactivity of the tyrosyl radical of Escherichia coli ribonucleotide reductase - Control by the protein
    • GEREZ C, ELLEINGARD K, KAUPPI B et al.: Reactivity of the tyrosyl radical of Escherichia coli ribonucleotide reductase - control by the protein. Eur. J. Biochem. (1997) 249:401-407.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 401-407
    • Gerez, C.1    Elleingard, K.2    Kauppi, B.3
  • 39
    • 21244440158 scopus 로고    scopus 로고
    • Structural and functional characterization of two mutated R2 proteins of Escherichia coli ribonucleotide reductase
    • LARSSON A, CLIMENT I, NORDLUND P et al.: Structural and functional characterization of two mutated R2 proteins of Escherichia coli ribonucleotide reductase. EMBO. J. (1996) 5:2037-2040.
    • (1996) EMBO. J. , vol.5 , pp. 2037-2040
    • Larsson, A.1    Climent, I.2    Nordlund, P.3
  • 40
    • 19244377006 scopus 로고    scopus 로고
    • Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase by time-resolved physical biochemical methods and X-ray crystallography
    • TONG W, BURDI D, RIGGS-GELASCO P et al.: Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase by time-resolved physical biochemical methods and X-ray crystallography. Biochemistry (1998) 37:5840-5848.
    • (1998) Biochemistry , vol.37 , pp. 5840-5848
    • Tong, W.1    Burdi, D.2    Riggs-Gelasco, P.3
  • 41
    • 0030580112 scopus 로고    scopus 로고
    • The three dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site then Escherichia coli
    • KAUPPI B, NIELSEN BA, RAMASWAMY S et al.: The three dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site then Escherichia coli. J. Mol. Biol. (1996) 262:706-720.
    • (1996) J. Mol. Biol. , vol.262 , pp. 706-720
    • Kauppi, B.1    Nielsen, B.A.2    Ramaswamy, S.3
  • 42
    • 0032558402 scopus 로고    scopus 로고
    • Structure of Salmonella typhimurium nrdF ribonucleotide reductase in its oxidized and reduced form
    • ERIKSSON M, JORDAN A, EKLUND H: Structure of Salmonella typhimurium nrdF ribonucleotide reductase in its oxidized and reduced form. Biochemistry (1998) 37:13359-13369.
    • (1998) Biochemistry , vol.37 , pp. 13359-13369
    • Eriksson, M.1    Jordan, A.2    Eklund, H.3
  • 43
    • 4244053232 scopus 로고    scopus 로고
    • Radical generation and transfer in ribonucleotide reductase
    • Department of Molecular Biology and Functional Genomics, Stockholm University, Stockholm, Sweden
    • HUQUE Y. Radical generation and transfer in ribonucleotide reductase. Department of Molecular Biology and Functional Genomics, Stockholm University, Stockholm, Sweden (2001).
    • (2001)
    • Huque, Y.1
  • 44
    • 0028486194 scopus 로고
    • Structure of ribonucleotide reductase protein R1
    • UHLIN U, EKLUND H: Structure of ribonucleotide reductase protein R1. Nature (1994) 370:533-539.
    • (1994) Nature , vol.370 , pp. 533-539
    • Uhlin, U.1    Eklund, H.2
  • 45
    • 0021162352 scopus 로고
    • Primary structure of the Escherichia coli ribonucleotide reductase operon
    • CARLSON J, FUCHS JA, MESSING J: Primary structure of the Escherichia coli ribonucleotide reductase operon. Proc. Natl. Acad. Soc. USA (1984) 81:4294-4297.
    • (1984) Proc. Natl. Acad. Soc. USA , vol.81 , pp. 4294-4297
    • Carlson, J.1    Fuchs, J.A.2    Messing, J.3
  • 46
    • 0026347398 scopus 로고
    • Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase
    • BOLLINGER JM JR, EDMONDSON DE, HUYNH BH et al.: Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase. Science (1991) 253:292-298.
    • (1991) Science , vol.253 , pp. 292-298
    • Bollinger Jr., J.M.1    Edmondson, D.E.2    Huynh, B.H.3
  • 47
    • 0024593917 scopus 로고
    • Reduced forms of the iron-containing small subunit of ribonucleotide reductase from Escherichia coli
    • SAHLIN M, GRASLUND A, PETERSSON L et al.: Reduced forms of the iron-containing small subunit of ribonucleotide reductase from Escherichia coli. Biochemistry (1989) 28:2618-2625.
    • (1989) Biochemistry , vol.28 , pp. 2618-2625
    • Sahlin, M.1    Graslund, A.2    Petersson, L.3
  • 48
    • 0018135309 scopus 로고
    • The tyrosine free radical in ribonucleotide reductase from Escherichia coli
    • SJOBERG BM, REICHARD P, GRASLUND A et al.: The tyrosine free radical in ribonucleotide reductase from Escherichia coli. J. Biol. Chem. (1978) 253:6863-6865.
    • (1978) J. Biol. Chem. , vol.253 , pp. 6863-6865
    • Sjoberg, B.M.1    Reichard, P.2    Graslund, A.3
  • 49
    • 0034594895 scopus 로고    scopus 로고
    • p53 sends nucleotides to repair DNA
    • LOZANO G, ELLEDGE SJ: p53 sends nucleotides to repair DNA. Nature (2000) 404:24-25.
    • (2000) Nature , vol.404 , pp. 24-25
    • Lozano, G.1    Elledge, S.J.2
  • 50
    • 0034738967 scopus 로고    scopus 로고
    • A ribonucleotide reductase gene is a transcriptional target of p53 and p73
    • NAKANO K, BALINT E, ASHCROFT M et al.: A ribonucleotide reductase gene is a transcriptional target of p53 and p73. Oncogene (2000) 19:4283-4289.
    • (2000) Oncogene , vol.19 , pp. 4283-4289
    • Nakano, K.1    Balint, E.2    Ashcroft, M.3
  • 51
    • 0034594978 scopus 로고    scopus 로고
    • A ribonucleotide reductase gene involved in p53-dependent cell-cycle checkpoint for DNA damage
    • TANAKA H, ARAKAWA H, YAMAGUCHI T et al.: A ribonucleotide reductase gene involved in p53-dependent cell-cycle checkpoint for DNA damage. Nature (2000) 404:42-49.
    • (2000) Nature , vol.404 , pp. 42-49
    • Tanaka, H.1    Arakawa, H.2    Yamaguchi, T.3
  • 52
    • 0034625375 scopus 로고    scopus 로고
    • Controlled protein degradation regulates ribonucleotide reductase activity in proliferating mammalian cells during the normal cell cycle and in response to DNA damage and replication blocks
    • CHABES A, THELANDER L: Controlled protein degradation regulates ribonucleotide reductase activity in proliferating mammalian cells during the normal cell cycle and in response to DNA damage and replication blocks. J. Biol. Chem. (2000) 275:17747-17753.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17747-17753
    • Chabes, A.1    Thelander, L.2
  • 53
    • 0032497529 scopus 로고    scopus 로고
    • A Mecl- and Rad53-dependent checkpoint controls late-firing origins of DNA replication
    • SANTOCANALE C, DIFFLEY JF: A Mecl- and Rad53-dependent checkpoint controls late-firing origins of DNA replication. Nature (2000) 395:615-618.
    • (2000) Nature , vol.395 , pp. 615-618
    • Santocanale, C.1    Diffley, J.F.2
  • 54
    • 0031464519 scopus 로고    scopus 로고
    • The enzyme ribonucleotide reductase: Target for antitumor and anti-HIV therapy
    • SZEKERES T, FRITZER-SZEKERES M, ELFORD HL: The enzyme ribonucleotide reductase: target for antitumor and anti-HIV therapy. Crit. Rev. Clin. Lab. Sci. (1997) 34:503-528.
    • (1997) Crit. Rev. Clin. Lab. Sci. , vol.34 , pp. 503-528
    • Szekeres, T.1    Fritzer-Szekeres, M.2    Elford, H.L.3
  • 55
  • 56
    • 0343735018 scopus 로고
    • Clinical and pharmacological effects of hydroxyurea
    • Sartorelli AC and Jones DG (Eds), Springer-Verlag, Berlin
    • KRAKOFF IH: Clinical and pharmacological effects of hydroxyurea. In: Antineoplastic and Immunosuppressive Agents. Part II. Sartorelli AC and Jones DG (Eds), Springer-Verlag, Berlin (1975):789-792.
    • (1975) Antineoplastic and Immunosuppressive Agents , Issue.PART II , pp. 789-792
    • Krakoff, I.H.1
  • 57
    • 0024360313 scopus 로고
    • Enzymatic regulation of the radical content of the small subunit of Escherichia coli ribonucleotide reductase involving reduction of its redox centers
    • FONTECAVE M, ELIASSON R, REICHARD P: Enzymatic regulation of the radical content of the small subunit of Escherichia coli ribonucleotide reductase involving reduction of its redox centers. J. Biol. Chem. (1989) 264:9164-9170.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9164-9170
    • Fontecave, M.1    Eliasson, R.2    Reichard, P.3
  • 58
    • 0024593917 scopus 로고
    • Activation of the iron-containing small subunit of ribonucleotide reductase from Escherichia coli
    • SAHLIN M, SJOBERG BM, BACKES G et al.: Activation of the iron-containing small subunit of ribonucleotide reductase from Escherichia coli. Biochemistry (1990) 28:2618-2625.
    • (1990) Biochemistry , vol.28 , pp. 2618-2625
    • Sahlin, M.1    Sjoberg, B.M.2    Backes, G.3
  • 59
    • 0026755811 scopus 로고
    • An overview of the clinical experience with hydroxymea
    • DONEHOWER RC: An overview of the clinical experience with hydroxymea. Semin. Oncol. (1992) 19:11-19.
    • (1992) Semin. Oncol. , vol.19 , pp. 11-19
    • Donehower, R.C.1
  • 60
    • 0026704779 scopus 로고
    • The evolution of hydroxyurea therapy in chronic myelogenous leukemia
    • KENNEDY BJ: The evolution of hydroxyurea therapy in chronic myelogenous leukemia. Semin. Oncol. (1992) 19:21-26.
    • (1992) Semin. Oncol. , vol.19 , pp. 21-26
    • Kennedy, B.J.1
  • 61
    • 0026663210 scopus 로고
    • Concurrent chemoradiation in carcinoma of the uterine cervix
    • STEHMAN FB: Concurrent chemoradiation in carcinoma of the uterine cervix. Semin. Oncol. (1992) 19:88-91.
    • (1992) Semin. Oncol. , vol.19 , pp. 88-91
    • Stehman, F.B.1
  • 62
    • 14344263978 scopus 로고    scopus 로고
    • Safety profile of hydroxyurea in the treatment of patients with Philadelphia-negative chronic myeloproliferative disorders
    • RANDI ML, RUZZON E, LUZZATTO G et al.: Safety profile of hydroxyurea in the treatment of patients with Philadelphia-negative chronic myeloproliferative disorders. Haematologica (2005) 90:261-262.
    • (2005) Haematologica , vol.90 , pp. 261-262
    • Randi, M.L.1    Ruzzon, E.2    Luzzatto, G.3
  • 63
    • 0031849153 scopus 로고    scopus 로고
    • Ribonucleotide reductases and radical reactions
    • FONTECAVE M: Ribonucleotide reductases and radical reactions. Cell Mol. Sci. (1998) 54:684-695.
    • (1998) Cell Mol. Sci. , vol.54 , pp. 684-695
    • Fontecave, M.1
  • 64
    • 0033975268 scopus 로고
    • Triapine (3-aminopyridine-2-carboxaldehyde-thiosemicarbazone): A potent inhibitor of ribonucleotide reductase activity with broad spectrum antitumor activity
    • FINCH RA, LIU M, GRILL SP et al.: Triapine (3-aminopyridine-2-carboxaldehyde-thiosemicarbazone): a potent inhibitor of ribonucleotide reductase activity with broad spectrum antitumor activity. Biochem. Pharmacol. (1992) 59:983-991.
    • (1992) Biochem. Pharmacol. , vol.59 , pp. 983-991
    • Finch, R.A.1    Liu, M.2    Grill, S.P.3
  • 65
    • 0006300527 scopus 로고
    • The inhibition of nucleoside diphosphates reductase by hydroxybenzodroxamic acid derivatives
    • Cory JG, Cory AH (Eds)
    • ELFORD HL, VAN'T RIET B: The inhibition of nucleoside diphosphates reductase by hydroxybenzodroxamic acid derivatives. In: Inbibitors of Ribonucleoside Diphosphate Reductase Activity. Cory JG, Cory AH (Eds), (1989):217-233.
    • (1989) Inbibitors of Ribonucleoside Diphosphate Reductase Activity , pp. 217-233
    • Elford, H.L.1    Van't Riet, B.2
  • 66
    • 0014063045 scopus 로고
    • Inhibition of DNA synthesis by hydroxyurea: Structure-activity relationships
    • YOUNG CW, SCHOCHETMAN G, HODAS S et al.: Inhibition of DNA synthesis by hydroxyurea: structure-activity relationships. Cancer Res. (1967) 27:535-540.
    • (1967) Cancer Res. , vol.27 , pp. 535-540
    • Young, C.W.1    Schochetman, G.2    Hodas, S.3
  • 67
    • 0018701235 scopus 로고
    • Synthesis of hydroxy- and amino substituted benzohydroxamic acids: Inhibition of ribonucleotide reductase and antitumor activity
    • VAN'T RIET B, WAMPLER GL, ELFORD HL: Synthesis of hydroxy- and amino substituted benzohydroxamic acids: inhibition of ribonucleotide reductase and antitumor activity. J. Med. Chem. (1979) 22:589-592.
    • (1979) J. Med. Chem. , vol.22 , pp. 589-592
    • Van't Riet, B.1    Wampler, G.L.2    Elford, H.L.3
  • 68
    • 0018395313 scopus 로고
    • New ribonucleotide reduccase inhibitors with antineoplastic activity
    • ELFORD HL, WAMPLER GL, VAN'T REIT B: New ribonucleotide reduccase inhibitors with antineoplastic activity. Cancer Res. (1979) 39:844-851.
    • (1979) Cancer Res. , vol.39 , pp. 844-851
    • Elford, H.L.1    Wampler, G.L.2    Van't Reit, B.3
  • 69
    • 0019236542 scopus 로고
    • Regulation of ribonucleotide reductase in mammalian cells by chemotherapeutic agents
    • ELFORD HL, VAN'T RIET B, WAMPLER GL et al.: Regulation of ribonucleotide reductase in mammalian cells by chemotherapeutic agents. Adv. Enz. Reg. (1981) 19:151-168.
    • (1981) Adv. Enz. Reg. , vol.19 , pp. 151-168
    • Elford, H.L.1    Van't Riet, B.2    Wampler, G.L.3
  • 70
    • 0344570544 scopus 로고
    • New cancer chemotherapeutic agents that inhibit ribonucleotide reductase
    • Bardos T, Kalman T (Eds), Elsevier Science, NY, USA
    • ELFORD HL, ELFORD RM, WAMPLER G L et al.: New cancer chemotherapeutic agents that inhibit ribonucleotide reductase. In: New Approaches to the Design of Antineoplastic Agents. Bardos T, Kalman T (Eds), Elsevier Science, NY, USA (1982):151-168.
    • (1982) New Approaches to the Design of Antineoplastic Agents , pp. 151-168
    • Elford, H.L.1    Elford, R.M.2    Wampler, G.L.3
  • 71
    • 0014549530 scopus 로고
    • Spectrum and iron content of protein B2 from ribonucleotide diphosphates reductase
    • BROWN NC, ELIASSON R, REICHARD P et al.: Spectrum and iron content of protein B2 from ribonucleotide diphosphates reductase. Eur. J. Biochem. (1969) 9:512-518.
    • (1969) Eur. J. Biochem. , vol.9 , pp. 512-518
    • Brown, N.C.1    Eliasson, R.2    Reichard, P.3
  • 72
    • 0015890741 scopus 로고
    • Iron and free radical in ribonucleotide reductase. Exchange of iron and Mossbauer spectroscopy of the protein B2 subunit of the Escherichia coli enzyme
    • ATKIN CL, THELANDER L, REICHARD P et al.: Iron and free radical in ribonucleotide reductase. Exchange of iron and Mossbauer spectroscopy of the protein B2 subunit of the Escherichia coli enzyme. J. Biol. Chem. (1973) 248:7464-7472.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7464-7472
    • Atkin, C.L.1    Thelander, L.2    Reichard, P.3
  • 73
    • 0018931182 scopus 로고
    • The iron center in ribonucleotide reductase from Escherichia coli
    • PETERSSON L, GRASLUND A, EHRENBERG A et al.: The iron center in ribonucleotide reductase from Escherichia coli. J. Biol. Chem. (1980) 225:6706-6712.
    • (1980) J. Biol. Chem. , vol.225 , pp. 6706-6712
    • Petersson, L.1    Graslund, A.2    Ehrenberg, A.3
  • 74
    • 15144349134 scopus 로고
    • Radikalangereigenschaften einiger Phenole
    • VENKER P, HERZMANN H: Radikalangereigenschaften einiger Phenole. Naturewissenschaften (1960) 47:133-134.
    • (1960) Naturewissenschaften , vol.47 , pp. 133-134
    • Venker, P.1    Herzmann, H.2
  • 75
    • 0030730939 scopus 로고    scopus 로고
    • DNA-protective activity of new ribonucleotide reductase inhibitors
    • RAUKO P, ROMANOVA D, MIADOKOVA E et al.: DNA-protective activity of new ribonucleotide reductase inhibitors. Anticancer Res. (1997) 17:3427-3440.
    • (1997) Anticancer Res. , vol.17 , pp. 3427-3440
    • Rauko, P.1    Romanova, D.2    Miadokova, E.3
  • 76
    • 0019960058 scopus 로고
    • Characterization of the active site of ribonucleotide reductase of Escherichia coli bacteriophage T4 and mammalian cells by inhibition studies with hydroxyurea analogues
    • KJOLLER-LARSEN I, SJOBERG BM, THELANDER L: Characterization of the active site of ribonucleotide reductase of Escherichia coli bacteriophage T4 and mammalian cells by inhibition studies with hydroxyurea analogues. Eur. J. Biochem. (1982) 125:75-81.
    • (1982) Eur. J. Biochem. , vol.125 , pp. 75-81
    • Kjoller-Larsen, I.1    Sjoberg, B.M.2    Thelander, L.3
  • 77
    • 0019182317 scopus 로고
    • On the mechanism of ribonucleotide diphosphate reductase from Escherichia coli: Evidence for 3′-C-H bond cleavage
    • STUBBE JA, ACKLES D: On the mechanism of ribonucleotide diphosphate reductase from Escherichia coli: Evidence for 3′-C-H bond cleavage. J. Biol. Chem. (1980) 225:8027-8030.
    • (1980) J. Biol. Chem. , vol.225 , pp. 8027-8030
    • Stubbe, J.A.1    Ackles, D.2
  • 78
    • 0020567471 scopus 로고
    • Mechanism of inhibition of mammalian ribonucleotide reductase by the iron chelate of 1-formylisoquinoline thiosemicarbazone
    • THELANDER L, GRASLUND A: Mechanism of inhibition of mammalian ribonucleotide reductase by the iron chelate of 1-formylisoquinoline thiosemicarbazone. J. Biol. Chem. (1983) 258:4063-4066.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4063-4066
    • Thelander, L.1    Graslund, A.2
  • 79
    • 0025217061 scopus 로고
    • A Phase I and pharmacokinetic study of didox administered by 36-hr infusion
    • The Cancer Research Campaign Phase I/II Clinical Trials Committee
    • CARMICHAEL J, CANTWELL BM, MANNIX KA: A Phase I and pharmacokinetic study of didox administered by 36-hr infusion. The Cancer Research Campaign Phase I/II Clinical Trials Committee. Br. J. Cancer (1990) 61:447-450.
    • (1990) Br. J. Cancer , vol.61 , pp. 447-450
    • Carmichael, J.1    Cantwell, B.M.2    Mannix, K.A.3
  • 80
    • 0023693722 scopus 로고
    • A Phase I and pharmacokinetic study of didox: A ribonucleotide reductase inhibitor
    • VEALE D, CARMICHAEL J, CANTWELL BM: A Phase I and pharmacokinetic study of didox: a ribonucleotide reductase inhibitor. Br. J. Cancer (1988) 58:70-72.
    • (1988) Br. J. Cancer , vol.58 , pp. 70-72
    • Veale, D.1    Carmichael, J.2    Cantwell, B.M.3
  • 81
    • 0026356576 scopus 로고
    • Phase II trial of didox in advanced breast cancer
    • The Cancer Research Campaign Phase I/II Clinical Trials Committee
    • RUBENS RD, KAYE SB, SOUKOP M: Phase II trial of didox in advanced breast cancer. The Cancer Research Campaign Phase I/II Clinical Trials Committee. Br. J. Cancer (1991) 64:1187-1188.
    • (1991) Br. J. Cancer , vol.64 , pp. 1187-1188
    • Rubens, R.D.1    Kaye, S.B.2    Soukop, M.3
  • 82
    • 21244432589 scopus 로고    scopus 로고
    • The evaluation of didox in the Salmonella-Escherichia coli/microsome plate incorporation assay
    • SRI International. Final Report, commissioned by the National Institute of Allergy and Infectious Disease (NIAID), NIH, Dr Charles Litterst Program Officer. SRI International, 333 Ravenswood Ave, Menlo Park, CA report on file
    • KRISTEN NL, RICCIO ES: The evaluation of didox in the Salmonella-Escherichia coli/microsome plate incorporation assay. SRI International. Final Report, commissioned by the National Institute of Allergy and Infectious Disease (NIAID), NIH, Dr Charles Litterst, Program Officer. SRI International, 333 Ravenswood Ave, Menlo Park, CA (2002) report on file.
    • (2002)
    • Kristen, N.L.1    Riccio, E.S.2
  • 83
    • 1642478198 scopus 로고    scopus 로고
    • Didox (a novel ribonucleotide reductase inhibitor) overcomes Bcl-2 mediated resistance in prostate cancer cell line, PC-3
    • INAYAT MS, CHENDIL D, MOHIUDDIN M et al.: Didox (a novel ribonucleotide reductase inhibitor) overcomes Bcl-2 mediated resistance in prostate cancer cell line, PC-3. Cancer Biol. Ther. (2002) 5:539-545.
    • (2002) Cancer Biol. Ther. , vol.5 , pp. 539-545
    • Inayat, M.S.1    Chendil, D.2    Mohiuddin, M.3
  • 84
    • 0020596551 scopus 로고
    • Isolation of a T-lymphotrophic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS)
    • BARRE-SINOUSI F, CHERMANN JC, REY F et al.: Isolation of a T-lymphotrophic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS). Science (1983) 220:868-871.
    • (1983) Science , vol.220 , pp. 868-871
    • Barre-Sinousi, F.1    Chermann, J.C.2    Rey, F.3
  • 85
    • 0024337928 scopus 로고
    • HIV-1 isolates are rapidly evolving quasi-species: Evidence for viral mixtures and preferred nucleotide substations
    • GOODENOW M, HUET T, SAURIN W et al.: HIV-1 isolates are rapidly evolving quasi-species: evidence for viral mixtures and preferred nucleotide substations. J. Acq. Imm. Defic. Syndr. (1989) 2:344-352.
    • (1989) J. Acq. Imm. Defic. Syndr. , vol.2 , pp. 344-352
    • Goodenow, M.1    Huet, T.2    Saurin, W.3
  • 86
    • 0022966842 scopus 로고
    • Induction of CD4 dependent cell fusion by the HTLV-III/LAV envelope glycoprotein
    • LIFSON JD, FEINBERG MB, REYES GR et al.: Induction of CD4 dependent cell fusion by the HTLV-III/LAV envelope glycoprotein. Nature (1986) 323:725-728.
    • (1986) Nature , vol.323 , pp. 725-728
    • Lifson, J.D.1    Feinberg, M.B.2    Reyes, G.R.3
  • 87
    • 21244438203 scopus 로고
    • Multiple concurrent reverse transcriptase and protease mutations and multidrug resistance of HIV-1 isolates from heavily treated patients
    • SHAFER RW, WINTERS MA, PLAMER S et al.: Multiple concurrent reverse transcriptase and protease mutations and multidrug resistance of HIV-1 isolates from heavily treated patients. Ann. Inn. Med. (1988) 128:1515-1518.
    • (1988) Ann. Inn. Med. , vol.128 , pp. 1515-1518
    • Shafer, R.W.1    Winters, M.A.2    Plamer, S.3
  • 88
    • 0032707973 scopus 로고    scopus 로고
    • Adverse metabolic disorders during highly accive antiretroviral treatments (HAART) of HIV disease
    • VIGOUROUX C, GHARAHANIAN S, SALHI Y et al.: Adverse metabolic disorders during highly accive antiretroviral treatments (HAART) of HIV disease. Diabetes Metab. (1999) 25:383-393.
    • (1999) Diabetes Metab. , vol.25 , pp. 383-393
    • Vigouroux, C.1    Gharahanian, S.2    Salhi, Y.3
  • 89
    • 0033520673 scopus 로고    scopus 로고
    • Residual HIV-1 RNA in blood plasma of patients taking suppressive highly active antiretroviral therapy
    • DORNADULA G, ZHANG H, VAN ULTERT B et al.: Residual HIV-1 RNA in blood plasma of patients taking suppressive highly active antiretroviral therapy. J. Am. Med. Assoc. (1999) 282:1627-1632.
    • (1999) J. Am. Med. Assoc. , vol.282 , pp. 1627-1632
    • Dornadula, G.1    Zhang, H.2    Van Ultert, B.3
  • 91
    • 0033796941 scopus 로고    scopus 로고
    • Effect of antimetabolite drugs of nucleotide metabolism on the anti-human immunodeficiency virus activity of nucleoside reverse transcriptase inhibitors
    • BALZARINI J: Effect of antimetabolite drugs of nucleotide metabolism on the anti-human immunodeficiency virus activity of nucleoside reverse transcriptase inhibitors. Pharmacol. Ther. (2000) 87:175-187.
    • (2000) Pharmacol. Ther. , vol.87 , pp. 175-187
    • Balzarini, J.1
  • 92
    • 0025880937 scopus 로고
    • Mechanism of the potentiating effect of ribavirin on the activity of 2′,3′-dideoxyinosine against human immunodeficiency virus
    • BALARINI J, LEE CK, HERDEWIJIN P et al.: Mechanism of the potentiating effect of ribavirin on the activity of 2′,3′-dideoxyinosine against human immunodeficiency virus. J. Biol. Chem. (1991) 266:21509-21514.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21509-21514
    • Balarini, J.1    Lee, C.K.2    Herdewijin, P.3
  • 93
    • 0032524983 scopus 로고    scopus 로고
    • Selective depletion of DNA precursors: An evolving strategy for potentiation of dideoxynucleoside activity against human immunodeficiency virus
    • JOHNS DG, GAO WY. Selective depletion of DNA precursors: an evolving strategy for potentiation of dideoxynucleoside activity against human immunodeficiency virus. Biochem. Pharmacol. (1998) 55:1551-1556.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 1551-1556
    • Johns, D.G.1    Gao, W.Y.2
  • 94
    • 0027948936 scopus 로고
    • Hydroxyurea as an inhibitor of human immunodeficiency virus-type 1 replication
    • LORI F, MALYKH A, CARA A et al.: Hydroxyurea as an inhibitor of human immunodeficiency virus-type 1 replication. Science (1994) 266:801-805.
    • (1994) Science , vol.266 , pp. 801-805
    • Lori, F.1    Malykh, A.2    Cara, A.3
  • 95
    • 0023025598 scopus 로고
    • Changes of deoxyribonucleoside triphosphate pools induced by hydroxyurea and their relation to DNA synthesis
    • BIANCHI V, PONTIS E, REICHARD P: Changes of deoxyribonucleoside triphosphate pools induced by hydroxyurea and their relation to DNA synthesis. J. Biol. Chem. (1986) 34:16037-16042.
    • (1986) J. Biol. Chem. , vol.34 , pp. 16037-16042
    • Bianchi, V.1    Pontis, E.2    Reichard, P.3
  • 96
    • 0025766796 scopus 로고
    • Deoxyadenosine reverses hydroxyurea inhibition of vaccine virus growth
    • SLABAUGH MB, HOWELL ML, WANG Y et al.: Deoxyadenosine reverses hydroxyurea inhibition of vaccine virus growth. J. Virol. (1991) 65:2290-2298.
    • (1991) J. Virol. , vol.65 , pp. 2290-2298
    • Slabaugh, M.B.1    Howell, M.L.2    Wang, Y.3
  • 97
    • 0029086336 scopus 로고
    • Disparate actions of hydroxyurea in potentiation of purine and pyrimidine 2′,3′-dideoxynucleoside activities against replication of human immunodeficiency virus
    • GAO WY, JOHNS DG, CHOKEKUCHAI S et al.: Disparate actions of hydroxyurea in potentiation of purine and pyrimidine 2′,3′-dideoxynucleoside activities against replication of human immunodeficiency virus. Proc. Natl. Acad. Sci. USA (1995) 92:8333-8337.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8333-8337
    • Gao, W.Y.1    Johns, D.G.2    Chokekuchai, S.3
  • 98
    • 0029018724 scopus 로고
    • Enhancement by hydroxyurea of the anti-human immunodeficiency virus Type 1 potency of 2′-β-fluoro-2′,3′-dideoxyadenosine in peripheral blood mononuclear cells
    • GAO WY, MITSUYA H, DRISCOLL JS et al.: Enhancement by hydroxyurea of the anti-human immunodeficiency virus Type 1 potency of 2′-β-fluoro-2′,3′-dideoxyadenosine in peripheral blood mononuclear cells. Biochem. Pharmacol. (1995) 50:274-276.
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 274-276
    • Gao, W.Y.1    Mitsuya, H.2    Driscoll, J.S.3
  • 99
    • 0032854838 scopus 로고    scopus 로고
    • Hydroxyurea enhances the activities of didanosine, 9-[2-(phosphonylmethoxy)ethyl]adenine, and 9-[2-(phosphonylmethoxy)propyl]adenine against drug-susceptible and drug-resistant human immunodeficiency virus isolates
    • PALMER S, SHAFER RW, MERIGAN TC: Hydroxyurea enhances the activities of didanosine, 9-[2-(phosphonylmethoxy)ethyl]adenine, and 9-[2-(phosphonylmethoxy)propyl]adenine against drug-susceptible and drug-resistant human immunodeficiency virus isolates. Antimicrob. Agents Chemother. (1999) 43:2046-2050.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 2046-2050
    • Palmer, S.1    Shafer, R.W.2    Merigan, T.C.3
  • 100
    • 0034490578 scopus 로고    scopus 로고
    • Long-term safety and antiretroviral activity of hydroxyurea and didanosine in HIV-patients
    • BIRON F, PONCEAU B, BOUHOUR D et al.: Long-term safety and antiretroviral activity of hydroxyurea and didanosine in HIV-patients. J. Acquir. Immune Defic. Syndr. (2000) 25:329-336.
    • (2000) J. Acquir. Immune Defic. Syndr. , vol.25 , pp. 329-336
    • Biron, F.1    Ponceau, B.2    Bouhour, D.3
  • 101
    • 0033791889 scopus 로고    scopus 로고
    • Long-term hydroxyurea in combination with didanosine and stuvadine for the treatment of HIV-1 infection. Swiss Cohort Study
    • RUTSCHMANN OT, OPRAVIL M, ITEN A et al.: Long-term hydroxyurea in combination with didanosine and stuvadine for the treatment of HIV-1 infection. Swiss Cohort Study. AIDS (2000) 14:2145-2151.
    • (2000) AIDS , vol.14 , pp. 2145-2151
    • Rutschmann, O.T.1    Opravil, M.2    Iten, A.3
  • 102
    • 0032840166 scopus 로고    scopus 로고
    • Hydroxyurea and HIV: 5 years later - From antiviral to immune-modulating effects
    • LORI F: Hydroxyurea and HIV: 5 years later - from antiviral to immune-modulating effects. AIDS (1999) 13:1433-1442.
    • (1999) AIDS , vol.13 , pp. 1433-1442
    • Lori, F.1
  • 103
    • 0033303144 scopus 로고    scopus 로고
    • Hydroxyurea in the treatment of HIV-1 infection
    • MASERATI R: Hydroxyurea in the treatment of HIV-1 infection. J. Biol. Regul. Homest. Agents (1999) 13:181-185.
    • (1999) J. Biol. Regul. Homest. Agents , vol.13 , pp. 181-185
    • Maserati, R.1
  • 104
    • 0029923839 scopus 로고    scopus 로고
    • Pharmacokinetics of hydroxyurea in patients infected with human immunodeficiency virus Type I
    • VILLANI P, MASERATI R, REGAZZI MB et al.: Pharmacokinetics of hydroxyurea in patients infected with human immunodeficiency virus Type I. J. Clin. Pharmacol. (1996) 36:117-121.
    • (1996) J. Clin. Pharmacol. , vol.36 , pp. 117-121
    • Villani, P.1    Maserati, R.2    Regazzi, M.B.3
  • 105
    • 3543116597 scopus 로고    scopus 로고
    • Safety of hydroxyurea in the treatment of HIV infeccion
    • LORI F, KELLY LM, FOLI A et al.: Safety of hydroxyurea in the treatment of HIV infeccion. Expert Opin. Drug Saf. (2004) 3:279-288.
    • (2004) Expert Opin. Drug Saf. , vol.3 , pp. 279-288
    • Lori, F.1    Kelly, L.M.2    Foli, A.3
  • 106
    • 21244492645 scopus 로고    scopus 로고
    • A low hydroxyurea (600 mg daily) is found optimal in a randomized, controlled trial (RIGHT 702) AIDS research and human retroviruses
    • in press
    • LORI F, POLLARD R, SHALIT P et al.: A low hydroxyurea (600 mg daily) is found optimal in a randomized, controlled trial (RIGHT 702) AIDS research and human retroviruses. in press.
    • Lori, F.1    Pollard, R.2    Shalit, P.3
  • 107
    • 21244433406 scopus 로고    scopus 로고
    • The effects of hydroxyurea or placebo combined with efavirenz, didanosine and stavudine in treatment naive and experienced patients: Preliminary 24-week results from the 3D study
    • XIII International AIDS Conference Durban, South Africa, WeOrB603
    • MURPHY R, KATLAMA C, AUTRAN B et al.: The effects of hydroxyurea or placebo combined with efavirenz, didanosine and stavudine in treatment naive and experienced patients: preliminary 24-week results from the 3D study. XIII International AIDS Conference, Durban, South Africa, WeOrB603 (2000).
    • (2000)
    • Murphy, R.1    Katlama, C.2    Autran, B.3
  • 108
    • 0344388739 scopus 로고    scopus 로고
    • In vitro antiretroviral activity of ribonucleotide reductase inhibitors hydroxyurea, didox and trimidox in the HIV-infected HuPBMC SCID model and the Rauscher murine leukemia virus (RmuLV) model: Mono-and combination therapy
    • Abstract no. 112
    • USSERY MA, KUNDER SC, GOLDERG G et al.: In vitro antiretroviral activity of ribonucleotide reductase inhibitors hydroxyurea, didox and trimidox in the HIV-infected HuPBMC SCID model and the Rauscher murine leukemia virus (RmuLV) model: mono-and combination therapy. In: Program. Abstract of the International Conference on Antimitocrobial Agents Chemotherapy. (1996) Abstract no. 112.
    • (1996) Program. Abstract of the International Conference on Antimitocrobial Agents Chemotherapy
    • Ussery, M.A.1    Kunder, S.C.2    Golderg, G.3
  • 109
    • 0031261894 scopus 로고    scopus 로고
    • Effective use of ribonucleotide reductase inhibitors (didox and timidox) alone or in combination with didanosine (ddI) to suppress disease progression and increase survival in marine acquired immunodeficiency syndrome (MAIDS)
    • MAYHEW CN, PHILLIPS JD, GREENBERG RN et al.: Effective use of ribonucleotide reductase inhibitors (didox and timidox) alone or in combination with didanosine (ddI) to suppress disease progression and increase survival in marine acquired immunodeficiency syndrome (MAIDS). Cell. Mol. Biol. (1999) 43:1019-1029.
    • (1999) Cell Mol. Biol. , vol.43 , pp. 1019-1029
    • Mayhew, C.N.1    Phillips, J.D.2    Greenberg, R.N.3
  • 110
    • 0036842228 scopus 로고    scopus 로고
    • Suppression of retrovirus-induced immunodeficiency disease (murine AIDS) by trimidox and didox; novel ribonucleotide reductase inhibitors with less bone marrow toxicity than hydroxyurea
    • MAYHEW CN, MAMPURU LJ, CHENDIL D et al.: Suppression of retrovirus-induced immunodeficiency disease (murine AIDS) by trimidox and didox; novel ribonucleotide reductase inhibitors with less bone marrow toxicity than hydroxyurea. Antivir. Res. (2002) 56:167-181.
    • (2002) Antivir. Res. , vol.56 , pp. 167-181
    • Mayhew, C.N.1    Mampuru, L.J.2    Chendil, D.3
  • 111
    • 0032757206 scopus 로고    scopus 로고
    • In vivo and in vitro comparison of the short-term hematopoietic toxicity - Hydroxyurea and trimidox or didox, novel ribonucleotide reductase inhibitors with potential HIV-1 activity
    • MAYHEW CN, PHILLIPS JD, GREENBERG RN et al.: In vivo and in vitro comparison of the short-term hematopoietic toxicity - hydroxyurea and trimidox or didox, novel ribonucleotide reductase inhibitors with potential HIV-1 activity. Stem Cells (1999) 17:1019-1029.
    • (1999) Stem Cells , vol.17 , pp. 1019-1029
    • Mayhew, C.N.1    Phillips, J.D.2    Greenberg, R.N.3
  • 112
    • 2342526590 scopus 로고    scopus 로고
    • In vivo examination of hydroxyurea and the novel ribonucleotide reductase inhibitors abacavir: Suppression of retrovirus-induced immunodeficiency disease
    • SUMPTER LR, INAYAT MS, YOST EE et al.: In vivo examination of hydroxyurea and the novel ribonucleotide reductase inhibitors abacavir: suppression of retrovirus-induced immunodeficiency disease. Antivir. Res. (2004) 62:111-120.
    • (2004) Antivir. Res. , vol.62 , pp. 111-120
    • Sumpter, L.R.1    Inayat, M.S.2    Yost, E.E.3
  • 113
    • 11844260142 scopus 로고    scopus 로고
    • Combination of inhibitors of lymphocyte activation (hydroxyurea, trimidox, and didox) and reverse transcriptase (didanosine) suppresses development of murine retrovirus-induced lymphoproliferative disease
    • MAYHEW CN, SUMPTER LN, INAYAT MS et al.: Combination of inhibitors of lymphocyte activation (hydroxyurea, trimidox, and didox) and reverse transcriptase (didanosine) suppresses development of murine retrovirus-induced lymphoproliferative disease. Antivir. Res. (2005) 65:13-22.
    • (2005) Antivir. Res. , vol.65 , pp. 13-22
    • Mayhew, C.N.1    Sumpter, L.N.2    Inayat, M.S.3
  • 114
    • 0037670160 scopus 로고    scopus 로고
    • Short-term treatment with novel ribonucleotide reductase inhibitors Trimidox and Didox reverse late-stage murine retrovirus-induced lymphoproliferative disease with less bone marrow toxicity than hydroxyurea
    • MAYHEW CN, PHILLIPS JD, CIBULL ML et al.: Short-term treatment with novel ribonucleotide reductase inhibitors Trimidox and Didox reverse late-stage murine retrovirus-induced lymphoproliferative disease with less bone marrow toxicity than hydroxyurea. Antivir. Chem. Chemother. (2002) 13:305-314.
    • (2002) Antivir. Chem. Chemother. , vol.13 , pp. 305-314
    • Mayhew, C.N.1    Phillips, J.D.2    Cibull, M.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.