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Volumn 4, Issue 9, 1996, Pages 1077-1092

Human dUTP pyrophosphatase: Uracil recognition by a β hairpin and active sites formed by three separate subunits

Author keywords

crystal structure; DNA repair; enzyme DNA interactions; nucleotide recognition motif; protein structure function; RNA world

Indexed keywords

ESCHERICHIA COLI; EUKARYOTA;

EID: 0030587564     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00114-1     Document Type: Article
Times cited : (167)

References (74)
  • 1
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl, T. (1994). Instability and decay of the primary structure of DNA. Nature 362, 709-715.
    • (1994) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 2
    • 0028934537 scopus 로고
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: Structura basis for specificity and catalysis
    • Mol, C.D., et al., & Tainer, J.A. (1995). Crystal structure and mutational analysis of human uracil-DNA glycosylase: structura basis for specificity and catalysis. Cell 80, 869-878.
    • (1995) Cell , vol.80 , pp. 869-878
    • Mol, C.D.1    Tainer, J.A.2
  • 3
    • 0013608322 scopus 로고
    • Transient accumulation of Okazaki fragments as a result of uracil incorporation into nascent DNA
    • Tye, B.K., Nyman, P.O., Lehman, I.R., Hochhauser, S. & Weiss, B. (1977). Transient accumulation of Okazaki fragments as a result of uracil incorporation into nascent DNA. Proc. Natl. Acad. Sci. USA 74, 154-157.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 154-157
    • Tye, B.K.1    Nyman, P.O.2    Lehman, I.R.3    Hochhauser, S.4    Weiss, B.5
  • 4
    • 0026711129 scopus 로고
    • Multiple mutant of Escherichia coli synthesizing virtually thymineless DNA during limited growth
    • El-Hajj, H.H., Wang, L. & Weiss, B. (1992). Multiple mutant of Escherichia coli synthesizing virtually thymineless DNA during limited growth. J. Bacteriol. 174, 4450-4456.
    • (1992) J. Bacteriol. , vol.174 , pp. 4450-4456
    • El-Hajj, H.H.1    Wang, L.2    Weiss, B.3
  • 5
    • 0026603423 scopus 로고
    • Uracil interference, a rapid and general method for defining protein-DNA interactions involving the 5-methyl group of thymines: The GCN4-DNA complex
    • Pu, W.T. & Struhl, K. (1992). Uracil interference, a rapid and general method for defining protein-DNA interactions involving the 5-methyl group of thymines: the GCN4-DNA complex. Nucleic Acids Res. 20, 771-775.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 771-775
    • Pu, W.T.1    Struhl, K.2
  • 6
    • 0023650405 scopus 로고
    • Thymine methyls and DNA-protein interactions
    • Ivarie, R. (1987). Thymine methyls and DNA-protein interactions. Nucleic Acids Res. 15, 9975-9983.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 9975-9983
    • Ivarie, R.1
  • 7
    • 0022506923 scopus 로고
    • DNA fragmentation and cytotoxicity from increased cellular deoxyuridylate
    • Ingraham, H.A., Dickey, L. & Goulian, M. (1986). DNA fragmentation and cytotoxicity from increased cellular deoxyuridylate. Biochemistry 25, 3225-3230.
    • (1986) Biochemistry , vol.25 , pp. 3225-3230
    • Ingraham, H.A.1    Dickey, L.2    Goulian, M.3
  • 9
    • 0020034884 scopus 로고
    • Genetic and biochemical consequences of thymidylate stress
    • Barclay, B.J., Kunz, B.A., Little, J.G., & Haynes, R.H. (1982). Genetic and biochemical consequences of thymidylate stress. Can. J. Biochem. 60, 172-194.
    • (1982) Can. J. Biochem. , vol.60 , pp. 172-194
    • Barclay, B.J.1    Kunz, B.A.2    Little, J.G.3    Haynes, R.H.4
  • 10
    • 0019205414 scopus 로고
    • The effect of methotrexate on levels of dUTP in animal cells
    • Goulian, M., Bleile, B. & Tseng, B.Y. (1980). The effect of methotrexate on levels of dUTP in animal cells. J. Biol. Chem. 255, 10630-10637.
    • (1980) J. Biol. Chem. , vol.255 , pp. 10630-10637
    • Goulian, M.1    Bleile, B.2    Tseng, B.Y.3
  • 11
    • 0023967987 scopus 로고
    • Lethality of a dut (deoxyuridine triphosphatase) mutation in Escherichia coli
    • El-Hajj, H., Zhang, H. & Weiss, B. (1988). Lethality of a dut (deoxyuridine triphosphatase) mutation in Escherichia coli. J. Bacteriol. 170, 1069-1075.
    • (1988) J. Bacteriol. , vol.170 , pp. 1069-1075
    • El-Hajj, H.1    Zhang, H.2    Weiss, B.3
  • 12
    • 0027426749 scopus 로고
    • dUTP pyrophosphatase is an essential enzyme in Saccharomyces cerevisiae
    • Gadsden, M.H., McIntosh, E.M., Game, J.C., Wilson, P.J. & Haynes, R.H. (1993). dUTP pyrophosphatase is an essential enzyme in Saccharomyces cerevisiae. EMBO J. 12, 4425-4431.
    • (1993) EMBO J. , vol.12 , pp. 4425-4431
    • Gadsden, M.H.1    McIntosh, E.M.2    Game, J.C.3    Wilson, P.J.4    Haynes, R.H.5
  • 14
    • 0026733623 scopus 로고
    • Herpes simplex type I dUTPase mutants are attenuated for neurovirulence, neuro-invasiveness and reactivation from latency
    • Pyles, R.B., Sawtell, N.M. & Thompson, R.L. (1992). Herpes simplex type I dUTPase mutants are attenuated for neurovirulence, neuro-invasiveness and reactivation from latency. J. Virol. 66, 6706-6713.
    • (1992) J. Virol. , vol.66 , pp. 6706-6713
    • Pyles, R.B.1    Sawtell, N.M.2    Thompson, R.L.3
  • 15
    • 0029152095 scopus 로고
    • Incorporation of uracil into viral DNA correlates with reduced replication of EIAV in macrophages
    • Steagall, W.K., Robek, M.D., Perry, S.T., Fuller, F.J. & Payne, S.L. (1995). Incorporation of uracil into viral DNA correlates with reduced replication of EIAV in macrophages. Virol. 210, 302-313.
    • (1995) Virol. , vol.210 , pp. 302-313
    • Steagall, W.K.1    Robek, M.D.2    Perry, S.T.3    Fuller, F.J.4    Payne, S.L.5
  • 16
    • 9044231763 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 vpr protein binds to the uracil DNA glycosylase DNA repair enzyme
    • Bouhamdan, M., et al., & Sire, J. (1996). Human immunodeficiency virus type 1 vpr protein binds to the uracil DNA glycosylase DNA repair enzyme. J. Virol. 70, 697-704.
    • (1996) J. Virol. , vol.70 , pp. 697-704
    • Bouhamdan, M.1    Sire, J.2
  • 17
    • 0029912969 scopus 로고    scopus 로고
    • Characterization of distinct nuclear and mitochondria forms of human deoxyuridine triphosphate nucleotidohydrolase
    • Ladner, R.D., McNulty, D.E., Carr, S.A., Roberts, G.D. & Caradonna, S.J. (1996). Characterization of distinct nuclear and mitochondria forms of human deoxyuridine triphosphate nucleotidohydrolase. J. Biol. Chem. 271, 7745-7751.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7745-7751
    • Ladner, R.D.1    McNulty, D.E.2    Carr, S.A.3    Roberts, G.D.4    Caradonna, S.J.5
  • 18
    • 0029979550 scopus 로고    scopus 로고
    • Identification of a consensus cyclin-dependent kinase phosphorylation site unique to the nuclear form of human deoxyuridine triphosphate nucleotidohydrolase
    • Ladner, R.D., Carr, S.A., Huddleston, M.J., McNulty, D.E. & Caradonna, S.J. (1996). Identification of a consensus cyclin-dependent kinase phosphorylation site unique to the nuclear form of human deoxyuridine triphosphate nucleotidohydrolase. J. Biol. Chem. 271, 7752-7757.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7752-7757
    • Ladner, R.D.1    Carr, S.A.2    Huddleston, M.J.3    McNulty, D.E.4    Caradonna, S.J.5
  • 19
    • 0022488360 scopus 로고
    • Enhancement of methotrexate toxicity by uracil analogues that inhibit deoxyuridine triphosphate nucleotidohydrolase (dUTPase) activity
    • Beck, W.R., Wright, G.E., Nusbaum, N.J., Chang, J.D. & Isselbacher, E.M. (1986). Enhancement of methotrexate toxicity by uracil analogues that inhibit deoxyuridine triphosphate nucleotidohydrolase (dUTPase) activity. Adv. Exp. Med. Biol. B 195, 97-104.
    • (1986) Adv. Exp. Med. Biol. B , vol.195 , pp. 97-104
    • Beck, W.R.1    Wright, G.E.2    Nusbaum, N.J.3    Chang, J.D.4    Isselbacher, E.M.5
  • 20
    • 0026666132 scopus 로고
    • Human dUTP pyrophosphatase: cDNA sequence and potential biological importance of the enzyme
    • McIntosh, E.M., Ager, D.D., Gadsden, M.H. & Haynes, R.H. (1992). Human dUTP pyrophosphatase: cDNA sequence and potential biological importance of the enzyme. Proc. Natl. Acad. Sci. USA 89, 8020-8024.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8020-8024
    • McIntosh, E.M.1    Ager, D.D.2    Gadsden, M.H.3    Haynes, R.H.4
  • 21
    • 0022656338 scopus 로고
    • Effects of mercury (II) compounds on the activity of dUTPases from various sources
    • Williams, M.V. (1986). Effects of mercury (II) compounds on the activity of dUTPases from various sources. Mol. Pharm. 29, 288-292.
    • (1986) Mol. Pharm. , vol.29 , pp. 288-292
    • Williams, M.V.1
  • 22
    • 0022302734 scopus 로고
    • Induction of a deoxyuridine triphosphate nucleotidohydrolase activity in Epstein-Barr virus-infected cells
    • Williams, M.V., Holliday, J. & Glaser, R. (1985). Induction of a deoxyuridine triphosphate nucleotidohydrolase activity in Epstein-Barr virus-infected cells. Virology 142, 326-333.
    • (1985) Virology , vol.142 , pp. 326-333
    • Williams, M.V.1    Holliday, J.2    Glaser, R.3
  • 23
    • 0024075248 scopus 로고
    • Herpes simplex virus-induced dUTPase: A target site for antiviral chemotherapy
    • Williams, M.V. (1988). Herpes simplex virus-induced dUTPase: a target site for antiviral chemotherapy. Virol. 166, 262-264.
    • (1988) Virol. , vol.166 , pp. 262-264
    • Williams, M.V.1
  • 25
    • 0018778778 scopus 로고
    • Human deoxyuridine triphisphate nucleotidohydrolase
    • Williams, M.V. & Cheng, Y. (1979). Human deoxyuridine triphisphate nucleotidohydrolase. J. Biol. Chem. 254, 2897-2901.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2897-2901
    • Williams, M.V.1    Cheng, Y.2
  • 26
    • 0026598186 scopus 로고
    • 2+-induced inhibition of deoxyuridine 5′-triphosphatase activity in rat liver cytosol
    • 2+-induced inhibition of deoxyuridine 5′-triphosphatase activity in rat liver cytosol. Mol. Cell. Biochem. 110, 25-29.
    • (1992) Mol. Cell. Biochem. , vol.110 , pp. 25-29
    • Yamaguchi, M.1    Sakurai, T.2
  • 28
    • 0001257560 scopus 로고
    • The beta bulge: A common small unit of non-repetitive protein structure
    • Richardson, J.S., Getzoff, E.D. & Richardson, D.C. (1978). The beta bulge: a common small unit of non-repetitive protein structure. Proc. Natl. Acad. Sci. USA 75, 2574-2578.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 2574-2578
    • Richardson, J.S.1    Getzoff, E.D.2    Richardson, D.C.3
  • 29
    • 0028201833 scopus 로고
    • Identification of tyrosine as a functional residue in the active site of Escherichia coli dUTPase
    • Vertessy, B.G., Zalud, P., Nyman, P.O. & Zeppezauer, M. (1994). Identification of tyrosine as a functional residue in the active site of Escherichia coli dUTPase. Biochem. Biophys. Acta 1205, 146-150.
    • (1994) Biochem. Biophys. Acta , vol.1205 , pp. 146-150
    • Vertessy, B.G.1    Zalud, P.2    Nyman, P.O.3    Zeppezauer, M.4
  • 30
    • 0027420358 scopus 로고
    • Molecular cloning and characterization of deoxyuridine triphosphatase from feline immunodeficiency virus (FIV)
    • Wagaman, P.C., Hasselkus-Light, C.S., Henson, M., Lerner, D.L., Phillips, T.R. & Elder, J.H. (1993). Molecular cloning and characterization of deoxyuridine triphosphatase from feline immunodeficiency virus (FIV). Virology 196, 451-457.
    • (1993) Virology , vol.196 , pp. 451-457
    • Wagaman, P.C.1    Hasselkus-Light, C.S.2    Henson, M.3    Lerner, D.L.4    Phillips, T.R.5    Elder, J.H.6
  • 31
  • 32
    • 0025293893 scopus 로고
    • Protein sequence comparisons show that the 'pseudoproteases' encoded by poxviruses and certain retroviruses belong to the deoxyuridine triphosphatase family
    • McGeoch, D.J. (1990). Protein sequence comparisons show that the 'pseudoproteases' encoded by poxviruses and certain retroviruses belong to the deoxyuridine triphosphatase family. Nucleic Acids Res. 18, 4105-4110.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4105-4110
    • McGeoch, D.J.1
  • 33
    • 0024215739 scopus 로고
    • Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products
    • Shirakihara, Y. & Evans, P.R. (1989). Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products. J. Mol. Biol. 204, 973-994.
    • (1989) J. Mol. Biol. , vol.204 , pp. 973-994
    • Shirakihara, Y.1    Evans, P.R.2
  • 34
    • 0027408171 scopus 로고
    • Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor
    • Zheng, J., et al., & Sowadski, J.M. (1993). Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor. Biochemistry 32, 2154-2161.
    • (1993) Biochemistry , vol.32 , pp. 2154-2161
    • Zheng, J.1    Sowadski, J.M.2
  • 35
    • 0000127673 scopus 로고
    • 2.2 Å refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor
    • Zheng, J., et al., & Sowadski, J.M. (1993). 2.2 Å refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor. Acta Cryst. D 49, 362-365.
    • (1993) Acta Cryst. D , vol.49 , pp. 362-365
    • Zheng, J.1    Sowadski, J.M.2
  • 38
    • 0028959237 scopus 로고
    • The structural basis of specific base-excision repair by uracil-DNA glycosylase
    • Savva, R., McAuley-Hecht, K., Brown, T. & Pearl, L. (1995). The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature 373, 487-493.
    • (1995) Nature , vol.373 , pp. 487-493
    • Savva, R.1    McAuley-Hecht, K.2    Brown, T.3    Pearl, L.4
  • 39
    • 0025311258 scopus 로고
    • Structure, multiple site binding, and segmenta accommodation in thymidylate synthase on binding dUMP and an anti-folate
    • Montfort, W.R., et al., & Stroud, R.M. (1990). Structure, multiple site binding, and segmenta accommodation in thymidylate synthase on binding dUMP and an anti-folate. Biochemistry 29, 6964-6977.
    • (1990) Biochemistry , vol.29 , pp. 6964-6977
    • Montfort, W.R.1    Stroud, R.M.2
  • 40
    • 0028942595 scopus 로고
    • Substrate specificity and assembly of the catalytic center derived from two structures of ligated uridylate kinase
    • Mueller-Dieckmann, H.-J. & Schulz, G.E. (1995). Substrate specificity and assembly of the catalytic center derived from two structures of ligated uridylate kinase. J. Mol. Biol. 246, 522-530.
    • (1995) J. Mol. Biol. , vol.246 , pp. 522-530
    • Mueller-Dieckmann, H.-J.1    Schulz, G.E.2
  • 41
    • 0026079373 scopus 로고
    • The refined structure of the complex between adenylate kinase from beef heart mitochondria matrix and its substrate AMP at 1.85 Å Resolution
    • Diederichs, K. & Schulz, G.E. (1991). The refined structure of the complex between adenylate kinase from beef heart mitochondria matrix and its substrate AMP at 1.85 Å Resolution. J. Mol. Biol. 217, 541-549.
    • (1991) J. Mol. Biol. , vol.217 , pp. 541-549
    • Diederichs, K.1    Schulz, G.E.2
  • 42
    • 0024463212 scopus 로고
    • Structure of the guanine-nucleotide-binding domain of the H-ras oncogene product p21 in the triphosphate conformaton
    • Pai, E.F., Kabsch, W., Krengel, U., Holmes, K.C., John, J. & Wittinghofer, A. (1989). Structure of the guanine-nucleotide-binding domain of the H-ras oncogene product p21 in the triphosphate conformaton. Nature 341, 209-214.
    • (1989) Nature , vol.341 , pp. 209-214
    • Pai, E.F.1    Kabsch, W.2    Krengel, U.3    Holmes, K.C.4    John, J.5    Wittinghofer, A.6
  • 43
    • 33845318295 scopus 로고
    • Interaction of pyrophosphate moieties with α-helices in dinucleotide binding proteins
    • Wierenga, R.K., De Maeyer, M.C.H. & Hol, W.G.J. (1985). Interaction of pyrophosphate moieties with α-helices in dinucleotide binding proteins. Biochemistry 24, 1346-1357.
    • (1985) Biochemistry , vol.24 , pp. 1346-1357
    • Wierenga, R.K.1    De Maeyer, M.C.H.2    Hol, W.G.J.3
  • 44
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution
    • Zhang, F., Strand, A., Robbins, D., Cobb, M.H. & Goldsmith, E.J. (1994). Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. Nature 367, 704-710.
    • (1994) Nature , vol.367 , pp. 704-710
    • Zhang, F.1    Strand, A.2    Robbins, D.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 45
    • 0028083309 scopus 로고
    • The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP
    • Eads, J.C., Scapin, G., Xu, Y., Grubmeyer, C. & Sacchettini, J.C. (1994). The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP. Cell 78, 325-334.
    • (1994) Cell , vol.78 , pp. 325-334
    • Eads, J.C.1    Scapin, G.2    Xu, Y.3    Grubmeyer, C.4    Sacchettini, J.C.5
  • 46
    • 12944300317 scopus 로고
    • Binding of nucleotides by proteins
    • Schulz, G.E. (1992). Binding of nucleotides by proteins. Curr. Opin Struct. Biol. 2, 61-67.
    • (1992) Curr. Opin Struct. Biol. , vol.2 , pp. 61-67
    • Schulz, G.E.1
  • 47
    • 1542563485 scopus 로고
    • Evolutionary and structural relationships among dehydrogenases
    • Boyer, P., ed., Academic Press, NY, USA
    • Rossman, M.G., Liljas, A., Branden, C.-I. & Banaszak, L.J. (1975). Evolutionary and structural relationships among dehydrogenases. In The Enzymes, Vol 11. (Boyer, P., ed.), pp. 61-102, Academic Press, NY, USA.
    • (1975) The Enzymes , vol.11 , pp. 61-102
    • Rossman, M.G.1    Liljas, A.2    Branden, C.-I.3    Banaszak, L.J.4
  • 48
    • 0018945849 scopus 로고
    • Gene duplication in glutathione reductase
    • Schulz, G.E. (1980). Gene duplication in glutathione reductase. J. Mol. Biol. 138, 335-347.
    • (1980) J. Mol. Biol. , vol.138 , pp. 335-347
    • Schulz, G.E.1
  • 49
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J.E., Saraste, M., Runswick, M.J. & Gay, N.J. (1982). Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 8, 945-951.
    • (1982) EMBO J. , vol.8 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 50
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H ras p21 at 1.35 Å resolution: Implications for the mechanism of GTP hydrolysis
    • Pai, E.F., Petsko, G.A., Goody, R.S., Kabsch, W. & Wittinghofer, A. (1990). Refined crystal structure of the triphosphate conformation of H ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9, 2351-2359.
    • (1990) EMBO J. , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Petsko, G.A.2    Goody, R.S.3    Kabsch, W.4    Wittinghofer, A.5
  • 51
    • 0023024626 scopus 로고
    • The glycine-rich loop of adenylate kinase forms a giant anion hole
    • Dreusicke, D. & Schulz, G.E. (1986). The glycine-rich loop of adenylate kinase forms a giant anion hole. FEBS Letts 208, 301-304.
    • (1986) FEBS Letts , vol.208 , pp. 301-304
    • Dreusicke, D.1    Schulz, G.E.2
  • 52
    • 0028063891 scopus 로고
    • Adenosine 5′-diphosphate binding and the active site of nucleoside diphosphate kinase
    • Morera, S., et al., & Janin, J. (1994). Adenosine 5′-diphosphate binding and the active site of nucleoside diphosphate kinase. Biochemistry 33, 459-467.
    • (1994) Biochemistry , vol.33 , pp. 459-467
    • Morera, S.1    Janin, J.2
  • 53
    • 0026662162 scopus 로고
    • Crystallographic structure of the nitrogenase iron protein from azotobacter vinelandii
    • Georgiadis, M.M., Komiya, H., Chakrabarti, P., Woo, D., Kornuc, J.J. & Rees, D.C. (1992). Crystallographic structure of the nitrogenase iron protein from azotobacter vinelandii. Science 257, 1653-1659.
    • (1992) Science , vol.257 , pp. 1653-1659
    • Georgiadis, M.M.1    Komiya, H.2    Chakrabarti, P.3    Woo, D.4    Kornuc, J.J.5    Rees, D.C.6
  • 55
    • 0029974453 scopus 로고    scopus 로고
    • Extraribosomal functions of ribosomal proteins
    • Wool, I.G. (1996). Extraribosomal functions of ribosomal proteins. Trends Biochem. Sci. 21, 164-165.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 164-165
    • Wool, I.G.1
  • 57
    • 0021008435 scopus 로고
    • Nucleotide sequence of the structura gene for dUTPase of Escherichia coli K-12
    • Lundberg, L.G., Thoressen, H.-O., Karlstrom, O.H. & Nyman, P.O. (1983). Nucleotide sequence of the structura gene for dUTPase of Escherichia coli K-12. EMBO J. 2, 967-971.
    • (1983) EMBO J. , vol.2 , pp. 967-971
    • Lundberg, L.G.1    Thoressen, H.-O.2    Karlstrom, O.H.3    Nyman, P.O.4
  • 58
    • 0026570966 scopus 로고
    • Channel catfish virus: A new type of herpesvirus
    • Davison, A.J. (1992). Channel catfish virus: a new type of herpesvirus. Virology 186, 9-14.
    • (1992) Virology , vol.186 , pp. 9-14
    • Davison, A.J.1
  • 59
    • 0026815647 scopus 로고
    • A meristem-related gene from tomato encodes a dUTPase: Analysis of expression in vegetative and flora meristems
    • Pri-Hadash, A., Harevan, D. & Lifschitz, E. (1992). A meristem-related gene from tomato encodes a dUTPase: analysis of expression in vegetative and flora meristems. Plant Cell. 4, 149-159.
    • (1992) Plant Cell. , vol.4 , pp. 149-159
    • Pri-Hadash, A.1    Harevan, D.2    Lifschitz, E.3
  • 60
    • 0024320604 scopus 로고
    • Retroviral protease-like gene in the vaccinia virus genome
    • Slabaugh, M.B. & Roseman, N.A. (1989). Retroviral protease-like gene in the vaccinia virus genome. Proc. Natl. Acad. Sci. USA 86, 4152-4155.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4152-4155
    • Slabaugh, M.B.1    Roseman, N.A.2
  • 61
  • 62
    • 0024378577 scopus 로고
    • A homologue of retroviral pseudoproteases in the parapoxvirus, orf virus
    • Mercer, A.A., Fraser, K.M., Stockwell, P.A. & Robinson, A.J. (1989). A homologue of retroviral pseudoproteases in the parapoxvirus, orf virus. Virology 172, 665-668.
    • (1989) Virology , vol.172 , pp. 665-668
    • Mercer, A.A.1    Fraser, K.M.2    Stockwell, P.A.3    Robinson, A.J.4
  • 63
    • 0027501113 scopus 로고
    • DNA sequence analysis of conserved and unique regions of swinepox virus: Identification of genetic elements supporting phenotypic observations including a novel G protein-coupled receptor homologue
    • Massung, R.F., Jayarama, V. & Moyer, R.W. (1993). DNA sequence analysis of conserved and unique regions of swinepox virus: identification of genetic elements supporting phenotypic observations including a novel G protein-coupled receptor homologue. Virology 197, 511-528.
    • (1993) Virology , vol.197 , pp. 511-528
    • Massung, R.F.1    Jayarama, V.2    Moyer, R.W.3
  • 64
    • 0014432781 scopus 로고
    • Solvent content in protein crystals
    • Matthews, B.W. (1968). Solvent content in protein crystals. J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 65
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • Sawyer, L., Issac, N. & Bailey, S., ed, SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend. (Sawyer, L., Issac, N. & Bailey, S., ed), pp. 56-62, SERC Daresbury Laboratory, Warrington, UK.
    • (1993) Proceedings of the CCP4 Study Weekend , pp. 56-62
    • Otwinowski, Z.1
  • 66
    • 0002351177 scopus 로고
    • AMoRe: A new package for molecular replacement
    • Dodson, E.J., Grower, S. & Wolf, W., eds, SERC, Daresbury Laboratory, Warrington, UK
    • Navaza, J. (1992). AMoRe: A new package for molecular replacement. In Proceedings of the CCP4 Study Weekend. (Dodson, E.J., Grower, S. & Wolf, W., eds), pp. 87-91, SERC, Daresbury Laboratory, Warrington, UK.
    • (1992) Proceedings of the CCP4 Study Weekend , pp. 87-91
    • Navaza, J.1
  • 67
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, J. & Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 68
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 69
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140-149.
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 70
    • 0002705842 scopus 로고
    • XtalView: A visual protein crystallographic software system for X11/XView
    • McRee, D.E. (1992). XtalView: a visual protein crystallographic software system for X11/XView. J. Mol. Graphics 10, 44-47.
    • (1992) J. Mol. Graphics , vol.10 , pp. 44-47
    • McRee, D.E.1
  • 72
    • 0014381393 scopus 로고
    • Conformation of polypeptides and proteins
    • Anfinsen, C.B Jr., Anson, M.L., Edsall, J.T. & Richards, F.M., eds, Academic Press, NY, USA
    • Ramachandran, G.N. & Sasisekharan, V. (1968). Conformation of polypeptides and proteins. In Advances in Protein Chemistry, Vol 23. (Anfinsen, C.B Jr., Anson, M.L., Edsall, J.T. & Richards, F.M., eds), pp 283-438, Academic Press, NY, USA.
    • (1968) Advances in Protein Chemistry , vol.23 , pp. 283-438
    • Ramachandran, G.N.1    Sasisekharan, V.2
  • 73
    • 84913050729 scopus 로고
    • An efficient genera-purpose least-squares refinement program for macromolecular structures
    • Tronrud, D.E., Ten Eyck, L.F. & Matthews, B.W. (1987). An efficient genera-purpose least-squares refinement program for macromolecular structures. Acta Crystallogr. A 43, 489-501.
    • (1987) Acta Crystallogr. A , vol.43 , pp. 489-501
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 74
    • 0029882967 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP)
    • Larsson, G., Svensson, L.A. & Nyman, P.O. (1996). Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP). Nat. Struct. Biol. 3, 532-538.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 532-538
    • Larsson, G.1    Svensson, L.A.2    Nyman, P.O.3


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