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Volumn 7, Issue 7, 2012, Pages

Characterization of Danio rerio mn2+-dependent ADP-Ribose/CDP-alcohol diphosphatase, the structural prototype of the ADPRibase-Mn-like protein family

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC ADENOSINE DIPHOSPHATE RIBOSE; CYTIDINE DIPHOSPHATE ALCOHOL DIPHOSPHATASE; HISTIDINE; MAGNESIUM ION; MUTANT PROTEIN; NUCLEOPHILE; PHOSPHATASE; UNCLASSIFIED DRUG;

EID: 84864413232     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0042249     Document Type: Article
Times cited : (5)

References (51)
  • 1
    • 0030596529 scopus 로고    scopus 로고
    • Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures
    • Klabunde T, Sträter N, Fröhlich R, Witzel H, Krebs B, (1996) Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures. J Mol Biol 259: 737-748.
    • (1996) J Mol Biol , vol.259 , pp. 737-748
    • Klabunde, T.1    Sträter, N.2    Fröhlich, R.3    Witzel, H.4    Krebs, B.5
  • 2
    • 0037083671 scopus 로고    scopus 로고
    • 3′,5′ Cyclic nucleotide phosphodiesterases class III: members, structure, and catalytic mechanism
    • Richter W, (2002) 3′,5′ Cyclic nucleotide phosphodiesterases class III: members, structure, and catalytic mechanism. Proteins 46: 278-286.
    • (2002) Proteins , vol.46 , pp. 278-286
    • Richter, W.1
  • 3
    • 33748502826 scopus 로고    scopus 로고
    • The catalytic mechanisms of binuclear metallohydrolases
    • Mitic N, Smith SJ, Neves A, Guddat LW, Gahan LR, et al. (2006) The catalytic mechanisms of binuclear metallohydrolases. Chem Rev 106: 3338-3363.
    • (2006) Chem Rev , vol.106 , pp. 3338-3363
    • Mitic, N.1    Smith, S.J.2    Neves, A.3    Guddat, L.W.4    Gahan, L.R.5
  • 4
    • 33751515585 scopus 로고    scopus 로고
    • Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis
    • Shenoy AR, Capuder M, Draskovic P, Lamba D, Visweswariah SS, et al. (2007) Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis. J Mol Biol 365: 211-225.
    • (2007) J Mol Biol , vol.365 , pp. 211-225
    • Shenoy, A.R.1    Capuder, M.2    Draskovic, P.3    Lamba, D.4    Visweswariah, S.S.5
  • 5
    • 79952483901 scopus 로고    scopus 로고
    • Structural and functional analysis of the Lmo2642 cyclic nucleotide phosphodiesterase from Listeria monocytogenes
    • Kim YG, Jeong JH, Ha NC, Kim KJ, (2011) Structural and functional analysis of the Lmo2642 cyclic nucleotide phosphodiesterase from Listeria monocytogenes. Proteins 79: 1205-1214.
    • (2011) Proteins , vol.79 , pp. 1205-1214
    • Kim, Y.G.1    Jeong, J.H.2    Ha, N.C.3    Kim, K.J.4
  • 7
    • 84872829687 scopus 로고    scopus 로고
    • Center for Eukaryotic Structural Genomics (CESG) website, University of Wisconsin-Madison Biochemistry Department, Available:
    • Bitto E, Wesenberg GE, Phillips Jr GN, McCoy JG, Bingman CA, (2006) Dimetal phosphatase from Danio rerio LOC 393393. Center for Eukaryotic Structural Genomics (CESG) website, University of Wisconsin-Madison Biochemistry Department. Available:http://www.uwstructuralgenomics.org/gallery/2nxf.pdf. Accessed 2012 July 6.
    • (2006) Dimetal phosphatase from Danio rerio LOC 393393
    • Bitto, E.1    Wesenberg, G.E.2    Phillips Jr, G.N.3    McCoy, J.G.4    Bingman, C.A.5
  • 8
    • 37249055016 scopus 로고    scopus 로고
    • Structures of proteins of biomedical interest from the Center for Eukaryotic Structural Genomics
    • Phillips GN Jr, Fox BG, Markley JL, Volkman BF, Bae E, et al. (2007) Structures of proteins of biomedical interest from the Center for Eukaryotic Structural Genomics. J Struct Funct Genomics 8: 73-84.
    • (2007) J Struct Funct Genomics , vol.8 , pp. 73-84
    • Phillips Jr., G.N.1    Fox, B.G.2    Markley, J.L.3    Volkman, B.F.4    Bae, E.5
  • 9
    • 84872828748 scopus 로고    scopus 로고
    • Crystal structure of a dimetal phosphatase from Danio rerio LOC 393393. RCSB Protein Databank website
    • Available: = 2NXF
    • Bitto E, Wesenberg GE, Phillips Jr GN, McCoy JG, Bingman CA, (2006) Crystal structure of a dimetal phosphatase from Danio rerio LOC 393393. RCSB Protein Databank website. Available:http://www.rcsb.org/pdb/explore.do?structureId = 2NXF. Accesed 2012 July 6.
    • (2006)
    • Bitto, E.1    Wesenberg, G.E.2    Phillips Jr, G.N.3    McCoy, J.G.4    Bingman, C.A.5
  • 10
    • 0028853089 scopus 로고
    • Rat liver nucleoside diphosphosugar or diphosphoalcohol pyrophosphatases different from nucleotide pyrophosphatase or phosphodiesterase I: substrate specificities of Mg2+- and/or Mn2+-dependent hydrolases acting on ADP-ribose
    • Canales J, Pinto RM, Costas MJ, Hernández MT, Miró A, et al. (1995) Rat liver nucleoside diphosphosugar or diphosphoalcohol pyrophosphatases different from nucleotide pyrophosphatase or phosphodiesterase I: substrate specificities of Mg2+- and/or Mn2+-dependent hydrolases acting on ADP-ribose. Biochim Biophys Acta 1246: 167-177.
    • (1995) Biochim Biophys Acta , vol.1246 , pp. 167-177
    • Canales, J.1    Pinto, R.M.2    Costas, M.J.3    Hernández, M.T.4    Miró, A.5
  • 11
    • 46249105799 scopus 로고    scopus 로고
    • Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase: a novel metallophosphoesterase family preferentially expressed in rodent immune cells
    • Canales J, Fernández A, Ribeiro JM, Cabezas A, Rodrigues JR, et al. (2008) Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase: a novel metallophosphoesterase family preferentially expressed in rodent immune cells. Biochem J 413: 103-113.
    • (2008) Biochem J , vol.413 , pp. 103-113
    • Canales, J.1    Fernández, A.2    Ribeiro, J.M.3    Cabezas, A.4    Rodrigues, J.R.5
  • 12
    • 67349103839 scopus 로고    scopus 로고
    • Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase
    • Canales J, Fernández A, Rodrigues JR, Ferreira R, Ribeiro JM, et al. (2009) Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase. FEBS Lett 583: 1593-1598.
    • (2009) FEBS Lett , vol.583 , pp. 1593-1598
    • Canales, J.1    Fernández, A.2    Rodrigues, J.R.3    Ferreira, R.4    Ribeiro, J.M.5
  • 13
    • 0027892021 scopus 로고
    • Synthesis and degradation of cyclic ADP-ribose by NAD glycohydrolases
    • Kim H, Jacobson EL, Jacobson MK, (1993) Synthesis and degradation of cyclic ADP-ribose by NAD glycohydrolases. Science 261: 1330-1333.
    • (1993) Science , vol.261 , pp. 1330-1333
    • Kim, H.1    Jacobson, E.L.2    Jacobson, M.K.3
  • 14
    • 0028026757 scopus 로고
    • Cyclic ADP-Ribose: synthesis and structural assignment
    • Gu Q-M, Sih CJ, (1994) Cyclic ADP-Ribose: synthesis and structural assignment. J Am Chem Soc 116: 7481-7486.
    • (1994) J Am Chem Soc , vol.116 , pp. 7481-7486
    • Gu, Q-M.1    Sih, C.J.2
  • 15
    • 34047231298 scopus 로고    scopus 로고
    • Structural basis for formation and hydrolysis of the calcium messenger cyclic ADP-ribose by human CD38
    • Liu Q, Kriksunov IA, Graeff R, Lee HC, Hao Q, (2007) Structural basis for formation and hydrolysis of the calcium messenger cyclic ADP-ribose by human CD38. J Biol Chem 282: 5853-5861.
    • (2007) J Biol Chem , vol.282 , pp. 5853-5861
    • Liu, Q.1    Kriksunov, I.A.2    Graeff, R.3    Lee, H.C.4    Hao, Q.5
  • 16
    • 0036300516 scopus 로고    scopus 로고
    • Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities
    • Yamamoto-Katayama S, Ariyoshi M, Ishihara K, Hirano T, Jingami H, et al. (2002) Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities. J Mol Biol 316: 711-723.
    • (2002) J Mol Biol , vol.316 , pp. 711-723
    • Yamamoto-Katayama, S.1    Ariyoshi, M.2    Ishihara, K.3    Hirano, T.4    Jingami, H.5
  • 17
    • 0030775072 scopus 로고    scopus 로고
    • Identification of bovine liver mitochondrial NAD+ glycohydrolase as ADP-ribosyl cyclase
    • Ziegler M, Jorcke D, Schweiger M, (1997) Identification of bovine liver mitochondrial NAD+ glycohydrolase as ADP-ribosyl cyclase. Biochem J 326: 401-405.
    • (1997) Biochem J , vol.326 , pp. 401-405
    • Ziegler, M.1    Jorcke, D.2    Schweiger, M.3
  • 18
    • 9444285520 scopus 로고    scopus 로고
    • Microarray and comparative genomics-based identification of genes and gene regulatory regions of the mouse immune system
    • Hutton JJ, Jegga AG, Kong S, Gupta A, Ebert C, et al. (2004) Microarray and comparative genomics-based identification of genes and gene regulatory regions of the mouse immune system. BMC Genomics 5: 82.
    • (2004) BMC Genomics , vol.5 , pp. 82
    • Hutton, J.J.1    Jegga, A.G.2    Kong, S.3    Gupta, A.4    Ebert, C.5
  • 19
    • 26444439972 scopus 로고    scopus 로고
    • TRPM2: a calcium influx pathway regulated by oxidative stress and the novel second messenger ADP-ribose
    • Kühn FJ, Heiner I, Lückhoff A, (2005) TRPM2: a calcium influx pathway regulated by oxidative stress and the novel second messenger ADP-ribose. Pflugers Arch 451: 212-219.
    • (2005) Pflugers Arch , vol.451 , pp. 212-219
    • Kühn, F.J.1    Heiner, I.2    Lückhoff, A.3
  • 20
    • 79953153188 scopus 로고    scopus 로고
    • TRPM2: a multifunctional ion channel for calcium signalling
    • Sumoza-Toledo A, Penner R, (2011) TRPM2: a multifunctional ion channel for calcium signalling. J Physiol 589: 1515-1525.
    • (2011) J Physiol , vol.589 , pp. 1515-1525
    • Sumoza-Toledo, A.1    Penner, R.2
  • 21
    • 15944417442 scopus 로고    scopus 로고
    • Cyclic ADP-ribose and hydrogen peroxide synergize with ADP-ribose in the activation of TRPM2 channels
    • Kolisek M, Beck A, Fleig A, Penner R, (2005) Cyclic ADP-ribose and hydrogen peroxide synergize with ADP-ribose in the activation of TRPM2 channels. Mol Cell 18: 61-69.
    • (2005) Mol Cell , vol.18 , pp. 61-69
    • Kolisek, M.1    Beck, A.2    Fleig, A.3    Penner, R.4
  • 22
    • 77956922681 scopus 로고    scopus 로고
    • Identification of direct and indirect effectors of the transient receptor potential melastatin 2 (TRPM2) cation channel
    • Tóth B, Csanády L, (2010) Identification of direct and indirect effectors of the transient receptor potential melastatin 2 (TRPM2) cation channel. J Biol Chem 285: 30091-30102.
    • (2010) J Biol Chem , vol.285 , pp. 30091-30102
    • Tóth, B.1    Csanády, L.2
  • 24
    • 0014504441 scopus 로고
    • Kinetics of enzyme reactions with interaction between a substrate and a (metal) modifier
    • London WP, Steck TL, (1969) Kinetics of enzyme reactions with interaction between a substrate and a (metal) modifier. Biochemistry 8: 1767-1779.
    • (1969) Biochemistry , vol.8 , pp. 1767-1779
    • London, W.P.1    Steck, T.L.2
  • 25
    • 0033655689 scopus 로고    scopus 로고
    • Inhibition and activation of enzymes. The effect of a modifier on the reaction rate and on kinetic parameters
    • Fontes R, Ribeiro JM, Sillero A, (2000) Inhibition and activation of enzymes. The effect of a modifier on the reaction rate and on kinetic parameters. Acta Biochim Pol 47: 233-257.
    • (2000) Acta Biochim Pol , vol.47 , pp. 233-257
    • Fontes, R.1    Ribeiro, J.M.2    Sillero, A.3
  • 26
    • 0003518480 scopus 로고    scopus 로고
    • New York: John Wiley & Sons, Inc
    • Segel IH (1975, reprinted 1993) Enzyme Kinetics. New York: John Wiley & Sons, Inc.
    • Enzyme Kinetics
    • Segel, I.H.1
  • 27
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL, (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 28
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word JM, Lovell SC, Richardson JS, Richardson DC, (1999) Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation. J Mol Biol 285: 1735-1747.
    • (1999) J Mol Biol , vol.285 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 29
    • 14844293471 scopus 로고    scopus 로고
    • A component-based software environment for visualizing large macromolecular assemblies
    • Sanner MF, (2005) A component-based software environment for visualizing large macromolecular assemblies. Structure 13: 447-462.
    • (2005) Structure , vol.13 , pp. 447-462
    • Sanner, M.F.1
  • 30
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris GM, Goodsell DS, Halliday RS, Huey R, Hart WE, et al. (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J Comput Chem 19: 1639-1662.
    • (1998) J Comput Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5
  • 31
    • 0015680655 scopus 로고
    • Clustering using a similarity measure based on shared near neighbors
    • Jarvis RA, Patrick EA, (1973) Clustering using a similarity measure based on shared near neighbors. IEEE Trans Comput C22: 1025-1034.
    • (1973) IEEE Trans Comput , vol.C22 , pp. 1025-1034
    • Jarvis, R.A.1    Patrick, E.A.2
  • 32
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E, (2008) GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4: 435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 33
    • 57649171118 scopus 로고    scopus 로고
    • A phosphate-binding histidine of binuclear metallophosphodiesterase enzymes is a determinant of 2′,3′-cyclic nucleotide phosphodiesterase activity
    • Keppetipola N, Shuman S, (2008) A phosphate-binding histidine of binuclear metallophosphodiesterase enzymes is a determinant of 2′,3′-cyclic nucleotide phosphodiesterase activity. J Biol Chem 283: 30942-30949.
    • (2008) J Biol Chem , vol.283 , pp. 30942-30949
    • Keppetipola, N.1    Shuman, S.2
  • 34
    • 0027944142 scopus 로고
    • Mutational analysis of a Ser/Thr phosphatase. Identification of residues important in phosphoesterase substrate binding and catalysis
    • Zhuo S, Clemens JC, Stone RL, Dixon JE, (1994) Mutational analysis of a Ser/Thr phosphatase. Identification of residues important in phosphoesterase substrate binding and catalysis. J Biol Chem 269: 26234-26238.
    • (1994) J Biol Chem , vol.269 , pp. 26234-26238
    • Zhuo, S.1    Clemens, J.C.2    Stone, R.L.3    Dixon, J.E.4
  • 35
    • 0029934685 scopus 로고    scopus 로고
    • Mutational analysis of the catalytic subunit of muscle protein phosphatase-1
    • Zhang J, Zhang Z, Brew K, Lee EY, (1996) Mutational analysis of the catalytic subunit of muscle protein phosphatase-1. Biochemistry 35: 6276-6282.
    • (1996) Biochemistry , vol.35 , pp. 6276-6282
    • Zhang, J.1    Zhang, Z.2    Brew, K.3    Lee, E.Y.4
  • 36
    • 0030881845 scopus 로고    scopus 로고
    • Kinetic and spectroscopic analyses of mutants of a conserved histidine in the metallophosphatases calcineurin and λ protein phosphatase
    • Mertz P, Yu L, Sikkink R, Rusnak F, (1997) Kinetic and spectroscopic analyses of mutants of a conserved histidine in the metallophosphatases calcineurin and λ protein phosphatase. J Biol Chem 272: 21296-21302.
    • (1997) J Biol Chem , vol.272 , pp. 21296-21302
    • Mertz, P.1    Yu, L.2    Sikkink, R.3    Rusnak, F.4
  • 37
    • 0032915156 scopus 로고    scopus 로고
    • X-ray structure of the Escherichia coli periplasmic 5′-nucleotidase containing a dimetal catalytic site
    • Knöfel T, Sträter N, (1999) X-ray structure of the Escherichia coli periplasmic 5′-nucleotidase containing a dimetal catalytic site. Nat Struct Biol 6: 448-453.
    • (1999) Nat Struct Biol , vol.6 , pp. 448-453
    • Knöfel, T.1    Sträter, N.2
  • 38
    • 0037662630 scopus 로고    scopus 로고
    • Cobalt activation of Escherichia coli 5′-nucleotidase is due to zinc ion displacement at only one of two metal-ion-binding sites
    • McMillen L, Beacham IR, Burns DM, (2003) Cobalt activation of Escherichia coli 5′-nucleotidase is due to zinc ion displacement at only one of two metal-ion-binding sites. Biochem J 372: 625-630.
    • (2003) Biochem J , vol.372 , pp. 625-630
    • McMillen, L.1    Beacham, I.R.2    Burns, D.M.3
  • 39
    • 77955271184 scopus 로고    scopus 로고
    • 2′,3′-cAMP hydrolysis by metal-dependent phosphodiesterases containing DHH, EAL, and HD domains is non-specific: Implications for PDE screening
    • Rao F, Qi Y, Murugan E, Pasunooti S, Ji Q, (2010) 2′,3′-cAMP hydrolysis by metal-dependent phosphodiesterases containing DHH, EAL, and HD domains is non-specific: Implications for PDE screening. Biochem Biophys Res Commun 398: 500-505.
    • (2010) Biochem Biophys Res Commun , vol.398 , pp. 500-505
    • Rao, F.1    Qi, Y.2    Murugan, E.3    Pasunooti, S.4    Ji, Q.5
  • 40
    • 0035979330 scopus 로고    scopus 로고
    • Identification of the high affinity Mn2+ binding site of bacteriophage λ phosphoprotein phosphatase: effects of metal ligand mutations on electron paramagnetic resonance spectra and phosphatase activities
    • White DJ, Reiter NJ, Sikkink RA, Yu L, Rusnak F, (2001) Identification of the high affinity Mn2+ binding site of bacteriophage λ phosphoprotein phosphatase: effects of metal ligand mutations on electron paramagnetic resonance spectra and phosphatase activities. Biochemistry 40: 8918-8929.
    • (2001) Biochemistry , vol.40 , pp. 8918-8929
    • White, D.J.1    Reiter, N.J.2    Sikkink, R.A.3    Yu, L.4    Rusnak, F.5
  • 41
    • 34250847224 scopus 로고    scopus 로고
    • Structural and biochemical characterization of a novel Mn2+-dependent phosphodiesterase encoded by the yfcE gene
    • Miller DJ, Shuvalova L, Evdokimova E, Savchenko A, Yakunin AF, et al. (2007) Structural and biochemical characterization of a novel Mn2+-dependent phosphodiesterase encoded by the yfcE gene. Protein Sci 16: 1338-1348.
    • (2007) Protein Sci , vol.16 , pp. 1338-1348
    • Miller, D.J.1    Shuvalova, L.2    Evdokimova, E.3    Savchenko, A.4    Yakunin, A.F.5
  • 42
    • 0034035617 scopus 로고    scopus 로고
    • Dimetallic hydrolases and their models
    • Kimura E, (2000) Dimetallic hydrolases and their models. Curr Opin Chem Biol 4: 207-213.
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 207-213
    • Kimura, E.1
  • 43
    • 0037138976 scopus 로고    scopus 로고
    • Electro-nuclear double resonance spectroscopic evidence for a hydroxo-bridge nucleophile involved in catalysis by a dinuclear hydrolase
    • Smoukov SK, Quaroni L, Wang X, Doan PE, Hoffman BM, et al. (2002) Electro-nuclear double resonance spectroscopic evidence for a hydroxo-bridge nucleophile involved in catalysis by a dinuclear hydrolase. J Am Chem Soc 124: 2595-2603.
    • (2002) J Am Chem Soc , vol.124 , pp. 2595-2603
    • Smoukov, S.K.1    Quaroni, L.2    Wang, X.3    Doan, P.E.4    Hoffman, B.M.5
  • 44
    • 4043101125 scopus 로고    scopus 로고
    • Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5
    • Swingle MR, Honkanen RE, Ciszak EM, (2004) Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5. J Biol Chem 279: 33992-33999.
    • (2004) J Biol Chem , vol.279 , pp. 33992-33999
    • Swingle, M.R.1    Honkanen, R.E.2    Ciszak, E.M.3
  • 45
    • 21344442376 scopus 로고    scopus 로고
    • Substrate positioning by His92 is important in catalysis by purple acid phosphatase
    • Funhoff EG, Wang Y, Andersson G, Averill BA, (2005) Substrate positioning by His92 is important in catalysis by purple acid phosphatase. FEBS J 272: 2968-2977.
    • (2005) FEBS J , vol.272 , pp. 2968-2977
    • Funhoff, E.G.1    Wang, Y.2    Andersson, G.3    Averill, B.A.4
  • 46
    • 38049088935 scopus 로고    scopus 로고
    • Characterization of the 2′,3′ cyclic phosphodiesterase activities of Clostridium thermocellum polynucleotide kinase-phosphatase and bacteriophage λ phosphatase
    • Keppetipola N, Shuman S, (2007) Characterization of the 2′,3′ cyclic phosphodiesterase activities of Clostridium thermocellum polynucleotide kinase-phosphatase and bacteriophage λ phosphatase. Nucleic Acids Res 35: 7721-7732.
    • (2007) Nucleic Acids Res , vol.35 , pp. 7721-7732
    • Keppetipola, N.1    Shuman, S.2
  • 47
    • 28544433399 scopus 로고    scopus 로고
    • The Rv0805 gene from Mycobacterium tuberculosis encodes a 3′,5′-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis
    • Shenoy AR, Sreenath N, Podobnik M, Kovacevic M, Visweswariah SS, (2005) The Rv0805 gene from Mycobacterium tuberculosis encodes a 3′,5′-cyclic nucleotide phosphodiesterase: biochemical and mutational analysis. Biochemistry 44: 15695-15704.
    • (2005) Biochemistry , vol.44 , pp. 15695-15704
    • Shenoy, A.R.1    Sreenath, N.2    Podobnik, M.3    Kovacevic, M.4    Visweswariah, S.S.5
  • 48
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L, Rosenström P, (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res 38: W545-549.
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenström, P.2
  • 51


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