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Volumn 347, Issue 2, 2005, Pages 243-255

Dimeric dUTPases, HisE, and MazG belong to a new superfamily of all-α NTP pyrophosphohydrolases with potential "house-cleaning" functions

Author keywords

Gene silencing; Histidine biosynthesis; Mutagenesis; Non canonical nucleotides; Oxidative damage

Indexed keywords

DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; DIMER; INORGANIC PYROPHOSPHATASE; NUCLEOSIDE TRIPHOSPHATASE; PROTEIN HISE; PROTEIN MAGZ; UNCLASSIFIED DRUG;

EID: 14644444463     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.01.030     Document Type: Article
Times cited : (79)

References (71)
  • 1
    • 0029835350 scopus 로고    scopus 로고
    • The MutT proteins or "nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes
    • M.J. Bessman, D.N. Frick, and S.F. O'Handley The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes J. Biol. Chem. 271 1996 25059 25062
    • (1996) J. Biol. Chem. , vol.271 , pp. 25059-25062
    • Bessman, M.J.1    Frick, D.N.2    O'Handley, S.F.3
  • 2
    • 17444398048 scopus 로고    scopus 로고
    • Structure-based identification of a novel NTPase from Methanococcus jannaschii
    • K.Y. Hwang, J.H. Chung, S.H. Kim, Y.S. Han, and Y. Cho Structure-based identification of a novel NTPase from Methanococcus jannaschii Nature Struct. Biol. 6 1999 691 696
    • (1999) Nature Struct. Biol. , vol.6 , pp. 691-696
    • Hwang, K.Y.1    Chung, J.H.2    Kim, S.H.3    Han, Y.S.4    Cho, Y.5
  • 3
    • 0034612280 scopus 로고    scopus 로고
    • Functional implications from crystal structures of the conserved Bacillus subtilis protein Maf with and without dUTP
    • G. Minasov, M. Teplova, G.C. Stewart, E.V. Koonin, W.F. Anderson, and M. Egli Functional implications from crystal structures of the conserved Bacillus subtilis protein Maf with and without dUTP Proc. Natl Acad. Sci. USA 97 2000 6328 6333
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6328-6333
    • Minasov, G.1    Teplova, M.2    Stewart, G.C.3    Koonin, E.V.4    Anderson, W.F.5    Egli, M.6
  • 4
    • 0034744964 scopus 로고    scopus 로고
    • Homotrimeric dUTPases; Structural solutions for specific recognition and hydrolysis of dUTP
    • R. Persson, E.S. Cedergren-Zeppezauer, and K.S. Wilson Homotrimeric dUTPases; structural solutions for specific recognition and hydrolysis of dUTP Curr. Protein Pept. Sci. 2 2001 287 300
    • (2001) Curr. Protein Pept. Sci. , vol.2 , pp. 287-300
    • Persson, R.1    Cedergren-Zeppezauer, E.S.2    Wilson, K.S.3
  • 6
    • 0031571084 scopus 로고    scopus 로고
    • Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: A new family of adenine nucleotide alpha hydrolases
    • H. Savage, G. Montoya, C. Svensson, J.D. Schwenn, and I. Sinning Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases Structure 5 1997 895 906
    • (1997) Structure , vol.5 , pp. 895-906
    • Savage, H.1    Montoya, G.2    Svensson, C.3    Schwenn, J.D.4    Sinning, I.5
  • 7
    • 0035576329 scopus 로고    scopus 로고
    • Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes
    • M.Y. Galperin, and M.J. Jedrzejas Conserved core structure and active site residues in alkaline phosphatase superfamily enzymes Proteins: Struct. Funct. Genet. 45 2001 318 324
    • (2001) Proteins: Struct. Funct. Genet. , vol.45 , pp. 318-324
    • Galperin, M.Y.1    Jedrzejas, M.J.2
  • 8
    • 0030853495 scopus 로고    scopus 로고
    • Description of a novel eukaryotic deoxyuridine 5′-triphosphate nucleotidohydrolase in Leishmania major
    • A. Camacho, R. Arrebola, J. Pena-Diaz, L.M. Ruiz-Perez, and D. Gonzalez-Pacanowska Description of a novel eukaryotic deoxyuridine 5′-triphosphate nucleotidohydrolase in Leishmania major Biochem. J. 325 1997 441 447
    • (1997) Biochem. J. , vol.325 , pp. 441-447
    • Camacho, A.1    Arrebola, R.2    Pena-Diaz, J.3    Ruiz-Perez, L.M.4    Gonzalez-Pacanowska, D.5
  • 10
    • 0034652380 scopus 로고    scopus 로고
    • Properties of Leishmania major dUTP nucleotidohydrolase, a distinct nucleotide-hydrolysing enzyme in kinetoplastids
    • A. Camacho, F. Hidalgo-Zarco, V. Bernier-Villamor, L.M. Ruiz-Perez, and D. Gonzalez-Pacanowska Properties of Leishmania major dUTP nucleotidohydrolase, a distinct nucleotide-hydrolysing enzyme in kinetoplastids Biochem. J. 346 2000 163 168
    • (2000) Biochem. J. , vol.346 , pp. 163-168
    • Camacho, A.1    Hidalgo-Zarco, F.2    Bernier-Villamor, V.3    Ruiz-Perez, L.M.4    Gonzalez-Pacanowska, D.5
  • 12
    • 4444321494 scopus 로고    scopus 로고
    • The crystal structure of a complex of Campylobacter jejuni dUTPase with substrate analogue sheds light on the mechanism and suggests the "basic module" for dimeric d(C/U)TPases
    • O.V. Moroz, M. Harkiolaki, M.Y. Galperin, A.A. Vagin, D. Gonzalez-Pacanowska, and K.S. Wilson The crystal structure of a complex of Campylobacter jejuni dUTPase with substrate analogue sheds light on the mechanism and suggests the "basic module" for dimeric d(C/U)TPases J. Mol. Biol. 342 2004 1583 1597
    • (2004) J. Mol. Biol. , vol.342 , pp. 1583-1597
    • Moroz, O.V.1    Harkiolaki, M.2    Galperin, M.Y.3    Vagin, A.A.4    Gonzalez-Pacanowska, D.5    Wilson, K.S.6
  • 14
    • 4444237887 scopus 로고
    • Deoxycytidine triphosphatase, an enzyme induced by bacteriophage infection
    • J.F. Koerner, M.S. Smith, and J.M. Buchanan Deoxycytidine triphosphatase, an enzyme induced by bacteriophage infection J. Biol. Chem. 235 1960 2691 2697
    • (1960) J. Biol. Chem. , vol.235 , pp. 2691-2697
    • Koerner, J.F.1    Smith, M.S.2    Buchanan, J.M.3
  • 15
    • 0009069474 scopus 로고
    • Deoxycytidine di- and triphosphate cleavage by an enzyme formed in bacteriophage-infected Eschrichia coli
    • S.B. Zimmerman, and A. Kornberg Deoxycytidine di- and triphosphate cleavage by an enzyme formed in bacteriophage-infected Eschrichia coli J. Biol. Chem. 236 1961 1480 1486
    • (1961) J. Biol. Chem. , vol.236 , pp. 1480-1486
    • Zimmerman, S.B.1    Kornberg, A.2
  • 16
    • 0013956438 scopus 로고
    • New dUTPase and dUDPase activites after infection of Escherichia coli by T2 bacteriophage
    • G.R. Greenberg New dUTPase and dUDPase activites after infection of Escherichia coli by T2 bacteriophage Proc. Natl Acad. Sci. USA 56 1966 1226 1232
    • (1966) Proc. Natl Acad. Sci. USA , vol.56 , pp. 1226-1232
    • Greenberg, G.R.1
  • 17
    • 0013959355 scopus 로고
    • Evidence for a dual role for the bacteriophage T4-induced deoxycytidine triphosphate nucleotidohydrolase
    • H.R. Warner, and J.E. Barnes Evidence for a dual role for the bacteriophage T4-induced deoxycytidine triphosphate nucleotidohydrolase Proc. Natl Acad. Sci. USA 56 1966 1233 1240
    • (1966) Proc. Natl Acad. Sci. USA , vol.56 , pp. 1233-1240
    • Warner, H.R.1    Barnes, J.E.2
  • 18
    • 0007853226 scopus 로고
    • Phosphoribosyladenosine monophosphate, an intermediate in histidine biosynthesis
    • D.W.E. Smith, and B.N. Ames Phosphoribosyladenosine monophosphate, an intermediate in histidine biosynthesis J. Biol. Chem. 240 1965 3056 3063
    • (1965) J. Biol. Chem. , vol.240 , pp. 3056-3063
    • Smith, D.W.E.1    Ames, B.N.2
  • 19
    • 0036776766 scopus 로고    scopus 로고
    • MazG, a nucleoside triphosphate pyrophosphohydrolase, interacts with Era, an essential GTPase in Escherichia coli
    • J. Zhang, and M. Inouye MazG, a nucleoside triphosphate pyrophosphohydrolase, interacts with Era, an essential GTPase in Escherichia coli J. Bacteriol. 184 2002 5323 5329
    • (2002) J. Bacteriol. , vol.184 , pp. 5323-5329
    • Zhang, J.1    Inouye, M.2
  • 20
    • 0037485102 scopus 로고    scopus 로고
    • Thermotoga maritima MazG protein has both nucleoside triphosphate pyrophosphohydrolase and pyrophosphatase activities
    • J. Zhang, Y. Zhang, and M. Inouye Thermotoga maritima MazG protein has both nucleoside triphosphate pyrophosphohydrolase and pyrophosphatase activities J. Biol. Chem. 278 2003 21408 21414
    • (2003) J. Biol. Chem. , vol.278 , pp. 21408-21414
    • Zhang, J.1    Zhang, Y.2    Inouye, M.3
  • 21
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • B. Rost, and C. Sander Prediction of protein secondary structure at better than 70% accuracy J. Mol. Biol. 232 1993 584 599
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 22
    • 0030931336 scopus 로고    scopus 로고
    • Seventy-five percent accuracy in protein secondary structure prediction
    • D. Frishman, and P. Argos Seventy-five percent accuracy in protein secondary structure prediction Proteins: Struct. Funct. Genet. 27 1997 329 335
    • (1997) Proteins: Struct. Funct. Genet. , vol.27 , pp. 329-335
    • Frishman, D.1    Argos, P.2
  • 23
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • D.T. Jones Protein secondary structure prediction based on position-specific scoring matrices J. Mol. Biol. 292 1999 195 202
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 24
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • J.A. Cuff, and G.J. Barton Application of multiple sequence alignment profiles to improve protein secondary structure prediction Proteins: Struct. Funct. Genet. 40 2000 502 511
    • (2000) Proteins: Struct. Funct. Genet. , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 25
    • 0036568279 scopus 로고    scopus 로고
    • Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles
    • G. Pollastri, D. Przybylski, B. Rost, and P. Baldi Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles Proteins: Struct. Funct. Genet. 47 2002 228 235
    • (2002) Proteins: Struct. Funct. Genet. , vol.47 , pp. 228-235
    • Pollastri, G.1    Przybylski, D.2    Rost, B.3    Baldi, P.4
  • 26
    • 0032161865 scopus 로고    scopus 로고
    • Isolation and characterization of a histidine biosynthetic gene in Arabidopsis encoding a polypeptide with two separate domains for phosphoribosyl-ATP pyrophosphohydrolase and phosphoribosyl-AMP cyclohydrolase
    • K. Fujimori, and D. Ohta Isolation and characterization of a histidine biosynthetic gene in Arabidopsis encoding a polypeptide with two separate domains for phosphoribosyl-ATP pyrophosphohydrolase and phosphoribosyl-AMP cyclohydrolase Plant Physiol. 118 1998 275 283
    • (1998) Plant Physiol. , vol.118 , pp. 275-283
    • Fujimori, K.1    Ohta, D.2
  • 27
    • 0018288994 scopus 로고
    • The product of the his4 gene cluster in Saccharomyces cerevisiae. A trifunctional polypeptide
    • J.K. Keesey Jr, R. Bigelis, and G.R. Fink The product of the his4 gene cluster in Saccharomyces cerevisiae. a trifunctional polypeptide J. Biol. Chem. 254 1979 7427 7433
    • (1979) J. Biol. Chem. , vol.254 , pp. 7427-7433
    • Keesey Jr., J.K.1    Bigelis, R.2    Fink, G.R.3
  • 28
    • 0033807335 scopus 로고    scopus 로고
    • Cloning of the histidine biosynthetic genes from Corynebacterium glutamicum: Organization and analysis of the hisG and hisE genes
    • J.H. Kwon, J.Y. Chun, H.S. Lee, C.I. Cheon, E.S. Song, K.H. Min, and M.S. Lee Cloning of the histidine biosynthetic genes from Corynebacterium glutamicum: organization and analysis of the hisG and hisE genes Can. J. Microbiol. 46 2000 848 855
    • (2000) Can. J. Microbiol. , vol.46 , pp. 848-855
    • Kwon, J.H.1    Chun, J.Y.2    Lee, H.S.3    Cheon, C.I.4    Song, E.S.5    Min, K.H.6    Lee, M.S.7
  • 33
    • 0029133347 scopus 로고
    • Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerises. Steady-state kinetics of the incorporation
    • H. Kamiya, and H. Kasai Formation of 2-hydroxydeoxyadenosine triphosphate, an oxidatively damaged nucleotide, and its incorporation by DNA polymerises. Steady-state kinetics of the incorporation J. Biol. Chem. 270 1995 19446 19450
    • (1995) J. Biol. Chem. , vol.270 , pp. 19446-19450
    • Kamiya, H.1    Kasai, H.2
  • 34
    • 0037440169 scopus 로고    scopus 로고
    • Mutagenic potentials of damaged nucleic acids produced by reactive oxygen/nitrogen species: Approaches using synthetic oligonucleotides and nucleotides: Survey and summary
    • H. Kamiya Mutagenic potentials of damaged nucleic acids produced by reactive oxygen/nitrogen species: approaches using synthetic oligonucleotides and nucleotides: survey and summary Nucl. Acids Res. 31 2003 517 531
    • (2003) Nucl. Acids Res. , vol.31 , pp. 517-531
    • Kamiya, H.1
  • 35
    • 0034084865 scopus 로고    scopus 로고
    • Who's your neighbor? New computational approaches for functional genomics
    • M.Y. Galperin, and E.V. Koonin Who's your neighbor? New computational approaches for functional genomics Nature Biotechnol. 18 2000 609 613
    • (2000) Nature Biotechnol. , vol.18 , pp. 609-613
    • Galperin, M.Y.1    Koonin, E.V.2
  • 37
    • 0029036695 scopus 로고
    • +-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure
    • +-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure Proc. Natl Acad. Sci. USA 92 1995 5149 5153
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5149-5153
    • York, J.D.1    Ponder, J.W.2    Majerus, P.W.3
  • 40
    • 0034326252 scopus 로고    scopus 로고
    • Effects of estrogen on global gene expression: Identification of novel targets of estrogen action
    • A.H. Charpentier, A.K. Bednarek, R.L. Daniel, K.A. Hawkins, K.J. Laflin, and S. Gaddis Effects of estrogen on global gene expression: identification of novel targets of estrogen action Cancer Res. 60 2000 5977 5983
    • (2000) Cancer Res. , vol.60 , pp. 5977-5983
    • Charpentier, A.H.1    Bednarek, A.K.2    Daniel, R.L.3    Hawkins, K.A.4    Laflin, K.J.5    Gaddis, S.6
  • 41
    • 0034761768 scopus 로고    scopus 로고
    • A comparative molecular analysis of developing mouse forelimbs and hindlimbs using serial analysis of gene expression (SAGE)
    • E.H. Margulies, S.L. Kardia, and J.W. Innis A comparative molecular analysis of developing mouse forelimbs and hindlimbs using serial analysis of gene expression (SAGE) Genome Res. 11 2001 1686 1698
    • (2001) Genome Res. , vol.11 , pp. 1686-1698
    • Margulies, E.H.1    Kardia, S.L.2    Innis, J.W.3
  • 42
    • 0035054441 scopus 로고    scopus 로고
    • Genome and genetic resources from the Cancer Genome Anatomy Project
    • G.J. Riggins, and R.L. Strausberg Genome and genetic resources from the Cancer Genome Anatomy Project Hum. Mol. Genet. 10 2001 663 667
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 663-667
    • Riggins, G.J.1    Strausberg, R.L.2
  • 43
    • 0036768299 scopus 로고    scopus 로고
    • SAGE identification of differentiation responsive genes in P19 embryonic cells induced to form cardiomyocytes in vitro
    • S.V. Anisimov, K.V. Tarasov, D. Riordon, A.M. Wobus, and K.R. Boheler SAGE identification of differentiation responsive genes in P19 embryonic cells induced to form cardiomyocytes in vitro Mech. Dev. 117 2002 25 74
    • (2002) Mech. Dev. , vol.117 , pp. 25-74
    • Anisimov, S.V.1    Tarasov, K.V.2    Riordon, D.3    Wobus, A.M.4    Boheler, K.R.5
  • 47
    • 1942474530 scopus 로고    scopus 로고
    • Gene expression profile of gastric carcinoma: Identification of genes and tags potentially involved in invasion, metastasis, and carcinogenesis by serial analysis of gene expression
    • N. Oue, Y. Hamai, Y. Mitani, S. Matsumura, Y. Oshimo, and P.P. Aung Gene expression profile of gastric carcinoma: identification of genes and tags potentially involved in invasion, metastasis, and carcinogenesis by serial analysis of gene expression Cancer Res. 64 2004 2397 2405
    • (2004) Cancer Res. , vol.64 , pp. 2397-2405
    • Oue, N.1    Hamai, Y.2    Mitani, Y.3    Matsumura, S.4    Oshimo, Y.5    Aung, P.P.6
  • 48
    • 0346250854 scopus 로고    scopus 로고
    • The transcriptome profile of human embryonic stem cells as defined by SAGE
    • M. Richards, S.P. Tan, J.H. Tan, W.K. Chan, and A. Bongso The transcriptome profile of human embryonic stem cells as defined by SAGE Stem Cells 22 2004 51 64
    • (2004) Stem Cells , vol.22 , pp. 51-64
    • Richards, M.1    Tan, S.P.2    Tan, J.H.3    Chan, W.K.4    Bongso, A.5
  • 49
    • 3142769033 scopus 로고    scopus 로고
    • The murine testicular transcriptome: Characterizing gene expression in the testis during the progression of spermatogenesis
    • J.E. Shima, D.J. McLean, J.R. McCarrey, and M.D. Griswold The murine testicular transcriptome: characterizing gene expression in the testis during the progression of spermatogenesis Biol. Reprod. 71 2004 319 330
    • (2004) Biol. Reprod. , vol.71 , pp. 319-330
    • Shima, J.E.1    McLean, D.J.2    McCarrey, J.R.3    Griswold, M.D.4
  • 51
    • 5144231671 scopus 로고    scopus 로고
    • Prokaryotic expression, purification and preparation of polyclonal antibody and immunohistochemistry analysis of RS21-C6 molecule
    • Y. Li, D.D. Jiang, C. Jin, Y.F. Liu, and W.F. Chen Prokaryotic expression, purification and preparation of polyclonal antibody and immunohistochemistry analysis of RS21-C6 molecule Beijing Da Xue Xue Bao (J. Peking Univ. Health Sci.). 36 2004 268 271
    • (2004) Beijing Da Xue Xue Bao (J. Peking Univ. Health Sci.). , vol.36 , pp. 268-271
    • Li, Y.1    Jiang, D.D.2    Jin, C.3    Liu, Y.F.4    Chen, W.F.5
  • 52
    • 0023298691 scopus 로고
    • The loss of CpG dinucleotides from DNA. I. Methylated and non-methylated genome compartments in eukaryotes with different levels of 5-methylcytosine in DNA
    • A.L. Mazin, and B.F. Vaniushin The loss of CpG dinucleotides from DNA. I. Methylated and non-methylated genome compartments in eukaryotes with different levels of 5-methylcytosine in DNA Mol. Biol. (Mosk) 21 1987 543 551
    • (1987) Mol. Biol. (Mosk) , vol.21 , pp. 543-551
    • Mazin, A.L.1    Vaniushin, B.F.2
  • 53
    • 0031027468 scopus 로고    scopus 로고
    • Methylation of genomes and genes at the invertebrate-vertebrate boundary
    • S. Tweedie, J. Charlton, V. Clark, and A. Bird Methylation of genomes and genes at the invertebrate-vertebrate boundary Mol. Cell. Biol. 17 1997 1469 1475
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1469-1475
    • Tweedie, S.1    Charlton, J.2    Clark, V.3    Bird, A.4
  • 54
    • 0037406067 scopus 로고    scopus 로고
    • The methyl-CpG binding domain and the evolving role of DNA methylation in animals
    • B. Hendrich, and S. Tweedie The methyl-CpG binding domain and the evolving role of DNA methylation in animals Trends Genet. 19 2003 269 277
    • (2003) Trends Genet. , vol.19 , pp. 269-277
    • Hendrich, B.1    Tweedie, S.2
  • 55
    • 0026316996 scopus 로고
    • Gene silencing in mammalian cells by direct incorporation of electroporated 5-methyl-2′-deoxycytidine 5′-triphosphate
    • J. Nyce Gene silencing in mammalian cells by direct incorporation of electroporated 5-methyl-2′-deoxycytidine 5′-triphosphate Somat. Cell Mol. Genet. 17 1991 543 550
    • (1991) Somat. Cell Mol. Genet. , vol.17 , pp. 543-550
    • Nyce, J.1
  • 56
    • 0036315387 scopus 로고    scopus 로고
    • DNA methylation and epigenetic inheritance
    • R. Holliday, and T. Ho DNA methylation and epigenetic inheritance Methods 27 2002 179 183
    • (2002) Methods , vol.27 , pp. 179-183
    • Holliday, R.1    Ho, T.2
  • 57
    • 0034856381 scopus 로고    scopus 로고
    • Activation of the maternally preset program of apoptosis by microinjection of 5-aza-2′-deoxycytidine and 5-methyl-2′- deoxycytidine-5′-triphosphate in Xenopus laevis embryos
    • C. Kaito, M. Kai, T. Higo, E. Takayama, H. Fukamachi, K. Sekimizu, and K. Shiokawa Activation of the maternally preset program of apoptosis by microinjection of 5-aza-2′-deoxycytidine and 5-methyl-2′- deoxycytidine-5′-triphosphate in Xenopus laevis embryos Dev. Growth Differ. 43 2001 383 390
    • (2001) Dev. Growth Differ. , vol.43 , pp. 383-390
    • Kaito, C.1    Kai, M.2    Higo, T.3    Takayama, E.4    Fukamachi, H.5    Sekimizu, K.6    Shiokawa, K.7
  • 58
    • 0035937181 scopus 로고    scopus 로고
    • Orf135 from Escherichia coli Is a Nudix hydrolase specific for CTP, dCTP, and 5-methyl-dCTP
    • S.F. O'Handley, C.A. Dunn, and M.J. Bessman Orf135 from Escherichia coli Is a Nudix hydrolase specific for CTP, dCTP, and 5-methyl-dCTP J. Biol. Chem. 276 2001 5421 5426
    • (2001) J. Biol. Chem. , vol.276 , pp. 5421-5426
    • O'Handley, S.F.1    Dunn, C.A.2    Bessman, M.J.3
  • 59
    • 0031970010 scopus 로고    scopus 로고
    • The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold
    • L. Aravind, M.Y. Galperin, and E.V. Koonin The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold Trends Biochem Sci. 23 1998 127 129
    • (1998) Trends Biochem Sci. , vol.23 , pp. 127-129
    • Aravind, L.1    Galperin, M.Y.2    Koonin, E.V.3
  • 61
    • 0024279564 scopus 로고
    • General architecture of the alpha-helical globule
    • A.G. Murzin, and A.V. Finkelstein General architecture of the alpha-helical globule J. Mol. Biol. 204 1988 749 769
    • (1988) J. Mol. Biol. , vol.204 , pp. 749-769
    • Murzin, A.G.1    Finkelstein, A.V.2
  • 64
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • E. Krissinel, and K. Henrick Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallog. sect. D 60 2004 2256 2268
    • (2004) Acta Crystallog. Sect. D , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 65
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • B. Lee, and F.M. Richards The interpretation of protein structures: estimation of static accessibility J. Mol. Biol. 55 1971 379 400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 66
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 67
    • 0028057108 scopus 로고
    • Raster3D Version 2.0. A program for photorealistic molecular graphics
    • E.A. Merritt, and M.E.P. Murphy Raster3D Version 2.0. A program for photorealistic molecular graphics Acta Crystallog. sect. D 50 1994 869 873
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 68
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced colouring capabilities
    • R.M. Esnouf An extensively modified version of MolScript that includes greatly enhanced colouring capabilities J. Mol. Graph. 15 1997 133 138
    • (1997) J. Mol. Graph. , vol.15 , pp. 133-138
    • Esnouf, R.M.1
  • 69
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • R.M. Esnouf Further additions to MolScript version 1.4, including reading and contouring of electron-density maps Acta Crystallog. sect. D 55 1999 938 940
    • (1999) Acta Crystallog. Sect. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 70
    • 0021088248 scopus 로고
    • Enzymes of pyrimidine deoxyribonucleotide metabolism in Mycoplasma mycoides subsp. mycoides
    • G.A. Neale, A. Mitchell, and L.R. Finch Enzymes of pyrimidine deoxyribonucleotide metabolism in Mycoplasma mycoides subsp. mycoides J. Bacteriol. 156 1983 1001 1005
    • (1983) J. Bacteriol. , vol.156 , pp. 1001-1005
    • Neale, G.A.1    Mitchell, A.2    Finch, L.R.3
  • 71
    • 0020584389 scopus 로고
    • T4 phage deoxyribonucleotide-synthesizing enzyme complex. Further studies on enzyme composition and regulation
    • J.R. Allen, G.W. Lasser, D.A. Goldman, J.W. Booth, and C.K. Mathews T4 phage deoxyribonucleotide-synthesizing enzyme complex. Further studies on enzyme composition and regulation J. Biol. Chem. 258 1983 5746 5753
    • (1983) J. Biol. Chem. , vol.258 , pp. 5746-5753
    • Allen, J.R.1    Lasser, G.W.2    Goldman, D.A.3    Booth, J.W.4    Mathews, C.K.5


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