메뉴 건너뛰기




Volumn 76, Issue 4, 2013, Pages 615-626

Crystal structure and biochemical analyses reveal that the Arabidopsis triphosphate tunnel metalloenzyme AtTTM3 is a tripolyphosphatase involved in root development

Author keywords

adenylate cyclase; Arabidopsis thaliana; CYTH domain; RNA triphosphatase; root; triphosphate tunnel metalloenzyme; tripolyphosphatase

Indexed keywords

ADENYLATE CYCLASE; ARABIDOPSIS THALIANA; CYTH DOMAIN; METALLOENZYMES; RNA TRIPHOSPHATASE; ROOT; TRIPOLYPHOSPHATASE;

EID: 84886798108     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/tpj.12325     Document Type: Article
Times cited : (29)

References (54)
  • 1
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P.D., Afonine, P.V., Bunkoczi, G., et al. (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221.
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1    Afonine, P.V.2    Bunkoczi, G.3
  • 2
    • 0042768158 scopus 로고    scopus 로고
    • Genome-wide insertional mutagenesis of Arabidopsis thaliana
    • Alonso, J.M., Stepanova, A.N., Leisse, T.J., et al. (2003) Genome-wide insertional mutagenesis of Arabidopsis thaliana. Science, 301, 653-657.
    • (2003) Science , vol.301 , pp. 653-657
    • Alonso, J.M.1    Stepanova, A.N.2    Leisse, T.J.3
  • 3
    • 41449108933 scopus 로고    scopus 로고
    • Characterization of a trifunctional mimivirus mRNA capping enzyme and crystal structure of the RNA triphosphatase domain
    • Benarroch, D., Smith, P., and, Shuman, S., (2008) Characterization of a trifunctional mimivirus mRNA capping enzyme and crystal structure of the RNA triphosphatase domain. Structure, 16, 501-512.
    • (2008) Structure , vol.16 , pp. 501-512
    • Benarroch, D.1    Smith, P.2    Shuman, S.3
  • 4
    • 77955505992 scopus 로고    scopus 로고
    • Root development: Two meristems for the price of one
    • Bennett, T., and, Scheres, B., (2010) Root development: two meristems for the price of one. Curr. Top. Dev. Biol. 91, 67-102.
    • (2010) Curr. Top. Dev. Biol. , vol.91 , pp. 67-102
    • Bennett, T.1    Scheres, B.2
  • 5
    • 11844301664 scopus 로고    scopus 로고
    • A colorimetric assay for the determination of 4-diphosphocytidyl-2-C- methyl-D-erythritol 4-phosphate synthase activity
    • Bernal, C., Palacin, C., Boronat, A., and, Imperial, S., (2005) A colorimetric assay for the determination of 4-diphosphocytidyl-2-C-methyl-D- erythritol 4-phosphate synthase activity. Anal. Biochem. 337, 55-61.
    • (2005) Anal. Biochem. , vol.337 , pp. 55-61
    • Bernal, C.1    Palacin, C.2    Boronat, A.3    Imperial, S.4
  • 7
    • 0035873620 scopus 로고    scopus 로고
    • Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme
    • Changela, A., Ho, C.K., Martins, A., Shuman, S., and, Mondragon, A., (2001) Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme. EMBO J. 20, 2575-2586.
    • (2001) EMBO J. , vol.20 , pp. 2575-2586
    • Changela, A.1    Ho, C.K.2    Martins, A.3    Shuman, S.4    Mondragon, A.5
  • 8
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough, S.J., and, Bent, A.F., (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16, 735-743.
    • (1998) Plant J. , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 9
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4.
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 10
    • 35848958805 scopus 로고    scopus 로고
    • PORE: A modular binary vector series suited for both monocot and dicot plant transformation
    • Coutu, C., Brandle, J., Brown, D., Brown, K., Miki, B., Simmonds, J., and, Hegedus, D., (2007) pORE: a modular binary vector series suited for both monocot and dicot plant transformation. Transgenic Res. 16, 771-781.
    • (2007) Transgenic Res. , vol.16 , pp. 771-781
    • Coutu, C.1    Brandle, J.2    Brown, D.3    Brown, K.4    Miki, B.5    Simmonds, J.6    Hegedus, D.7
  • 11
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis, I.W., Leaver-Fay, A., Chen, V.B., et al. (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35, W375-W383.
    • (2007) Nucleic Acids Res. , vol.35
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3
  • 12
    • 80053206909 scopus 로고    scopus 로고
    • A specific inorganic triphosphatase from Nitrosomonas europaea: Structure and catalytic mechanism
    • Delvaux, D., Murty, M.R.V.S., Gabelica, V., et al. (2011) A specific inorganic triphosphatase from Nitrosomonas europaea: structure and catalytic mechanism. J. Biol. Chem. 286, 34023-34035.
    • (2011) J. Biol. Chem. , vol.286 , pp. 34023-34035
    • Delvaux, D.1    Murty, M.R.V.S.2    Gabelica, V.3
  • 13
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P., and, Cowtan, K., (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 15
    • 78650731892 scopus 로고    scopus 로고
    • Adenyl cyclases and cAMP in plant signaling - Past and present
    • Gehring, C., (2010) Adenyl cyclases and cAMP in plant signaling-past and present. Cell Comm. Signal, 8, 15.
    • (2010) Cell Comm. Signal , vol.8 , pp. 15
    • Gehring, C.1
  • 16
    • 0037013218 scopus 로고    scopus 로고
    • Chlorella virus RNA triphosphatase. Mutational analysis and mechanism of inhibition by tripolyphosphate
    • Gong, C., and, Shuman, S., (2002) Chlorella virus RNA triphosphatase. Mutational analysis and mechanism of inhibition by tripolyphosphate. J. Biol. Chem. 277, 15317-15324.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15317-15324
    • Gong, C.1    Shuman, S.2
  • 17
    • 0347065370 scopus 로고    scopus 로고
    • Structure-function analysis of Trypanosoma brucei RNA triphosphatase and evidence for a two-metal mechanism
    • Gong, C., Martins, A., and, Shuman, S., (2003) Structure-function analysis of Trypanosoma brucei RNA triphosphatase and evidence for a two-metal mechanism. J. Biol. Chem. 278, 50843-50852.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50843-50852
    • Gong, C.1    Martins, A.2    Shuman, S.3
  • 18
    • 33746571989 scopus 로고    scopus 로고
    • Structure-function analysis of Plasmodium RNA triphosphatase and description of a triphosphate tunnel metalloenzyme superfamily that includes Cet1-like RNA triphosphatases and CYTH proteins
    • Gong, C., Smith, P., and, Shuman, S., (2006) Structure-function analysis of Plasmodium RNA triphosphatase and description of a triphosphate tunnel metalloenzyme superfamily that includes Cet1-like RNA triphosphatases and CYTH proteins. RNA, 12, 1468-1474.
    • (2006) RNA , vol.12 , pp. 1468-1474
    • Gong, C.1    Smith, P.2    Shuman, S.3
  • 19
    • 0032545284 scopus 로고    scopus 로고
    • Yeast and viral RNA 5′ triphosphatases comprise a new nucleoside triphosphatase family
    • Ho, C.K., Pei, Y., and, Shuman, S., (1998a) Yeast and viral RNA 5′ triphosphatases comprise a new nucleoside triphosphatase family. J. Biol. Chem. 273, 34151-34156.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34151-34156
    • Ho, C.K.1    Pei, Y.2    Shuman, S.3
  • 20
    • 3543026832 scopus 로고    scopus 로고
    • Genetic, physical and functional interactions between the triphosphatase and the guanylyltransferase components of the yeast mRNA capping apparatus
    • Ho, C.K., Schwer, B., and, Shuman, S., (1998b) Genetic, physical and functional interactions between the triphosphatase and the guanylyltransferase components of the yeast mRNA capping apparatus. Mol. Cell. Biol. 18, 5189-5198.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5189-5198
    • Ho, C.K.1    Schwer, B.2    Shuman, S.3
  • 21
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L., and, Rosenstrom, P., (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res. 38 (Suppl), W545-W549.
    • (2010) Nucleic Acids Res. , vol.38 , Issue.SUPPL.
    • Holm, L.1    Rosenstrom, P.2
  • 22
    • 65449179270 scopus 로고    scopus 로고
    • Catalytic core of a membrane-associated eukaryotic polyphosphate polymerase
    • Hothorn, M., Neumann, H., Lenherr, E.D., et al. (2009) Catalytic core of a membrane-associated eukaryotic polyphosphate polymerase. Science, 324, 513-516.
    • (2009) Science , vol.324 , pp. 513-516
    • Hothorn, M.1    Neumann, H.2    Lenherr, E.D.3
  • 23
    • 67649884096 scopus 로고    scopus 로고
    • Nucleotide analogs and molecular modeling studies reveal key interactions involved in substrate recognition by the yeast RNA triphosphatase
    • Issur, M., Despins, S., Bougie, I., and, Bisaillon, M., (2009) Nucleotide analogs and molecular modeling studies reveal key interactions involved in substrate recognition by the yeast RNA triphosphatase. Nucleic Acids Res. 37, 3714-3722.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3714-3722
    • Issur, M.1    Despins, S.2    Bougie, I.3    Bisaillon, M.4
  • 24
    • 0042076040 scopus 로고    scopus 로고
    • The catalytic domains of thiamine triphosphatase and CyaB-like adenylyl cyclase define a novel superfamily of domains that bind organic phosphates
    • Iyer, L.M., and, Aravind, L., (2002) The catalytic domains of thiamine triphosphatase and CyaB-like adenylyl cyclase define a novel superfamily of domains that bind organic phosphates. BMC Genomics, 3, 33.
    • (2002) BMC Genomics , vol.3 , pp. 33
    • Iyer, L.M.1    Aravind, L.2
  • 25
    • 57649155902 scopus 로고    scopus 로고
    • Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme
    • Jain, R., and, Shuman, S., (2008) Polyphosphatase activity of CthTTM, a bacterial triphosphate tunnel metalloenzyme. J. Biol. Chem. 283, 31047-31057.
    • (2008) J. Biol. Chem. , vol.283 , pp. 31047-31057
    • Jain, R.1    Shuman, S.2
  • 26
    • 0031775225 scopus 로고    scopus 로고
    • The LEF-4 subunit of baculovirus RNA polymerase has RNA 5′-triphosphatase and ATPase activities
    • Jin, J., Dong, W., and, Guarino, L.A., (1998) The LEF-4 subunit of baculovirus RNA polymerase has RNA 5′-triphosphatase and ATPase activities. J. Virol. 72, 10011-10019.
    • (1998) J. Virol. , vol.72 , pp. 10011-10019
    • Jin, J.1    Dong, W.2    Guarino, L.A.3
  • 27
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W., (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 28
    • 34249748419 scopus 로고    scopus 로고
    • Novel triphosphate phosphohydrolase activity of Clostridium thermocellum TTM, a member of the triphosphate tunnel metalloenzyme superfamily
    • Keppetipola, N., Jain, R., and, Shuman, S., (2007) Novel triphosphate phosphohydrolase activity of Clostridium thermocellum TTM, a member of the triphosphate tunnel metalloenzyme superfamily. J. Biol. Chem. 282, 11941-11949.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11941-11949
    • Keppetipola, N.1    Jain, R.2    Shuman, S.3
  • 29
    • 84866314876 scopus 로고    scopus 로고
    • High inorganic triphosphatase activities in bacteria and mammalian cells: Identification of the enzymes involved
    • Kohn, G., Delvaux, D., Lakaye, B., et al. (2012) High inorganic triphosphatase activities in bacteria and mammalian cells: identification of the enzymes involved. PLoS One, 7 (9), e43879.
    • (2012) PLoS One , vol.7 , Issue.9
    • Kohn, G.1    Delvaux, D.2    Lakaye, B.3
  • 30
    • 11144354607 scopus 로고    scopus 로고
    • Human recombinant thiamine triphosphatase: Purification, secondary structure and catalytic properties
    • Lakaye, B., Makarchikov, A.F., Wins, P., et al. (2004) Human recombinant thiamine triphosphatase: purification, secondary structure and catalytic properties. Int. J. Biochem. Cell Biol. 36, 1348-1364.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 1348-1364
    • Lakaye, B.1    Makarchikov, A.F.2    Wins, P.3
  • 31
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer, G., Cohen, S.X., Lamzin, V.S., and, Perrakis, A., (2008) Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc. 3, 1171-1179.
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 34
    • 0033601125 scopus 로고    scopus 로고
    • Structure and mechanism of yeast RNA triphosphatase: An essential component of the mRNA capping apparatus
    • Lima, C.D., Wang, L.K., and, Shuman, S., (1999) Structure and mechanism of yeast RNA triphosphatase: an essential component of the mRNA capping apparatus. Cell, 99, 533-543.
    • (1999) Cell , vol.99 , pp. 533-543
    • Lima, C.D.1    Wang, L.K.2    Shuman, S.3
  • 35
    • 0031027182 scopus 로고    scopus 로고
    • Organization and cell differentiation in lateral roots of Arabidopsis thaliana
    • Malamy, J.E., and, Benfey, P.N., (1997) Organization and cell differentiation in lateral roots of Arabidopsis thaliana. Development, 124, 33-44.
    • (1997) Development , vol.124 , pp. 33-44
    • Malamy, J.E.1    Benfey, P.N.2
  • 36
    • 27844556005 scopus 로고    scopus 로고
    • Cellular organisation in meiotic and early post-meiotic rice anthers
    • Mamun, E.A., Cantrill, L.C., Overall, R.L., and, Sutton, B.G., (2005) Cellular organisation in meiotic and early post-meiotic rice anthers. Cell Biol. Int. 29, 903-913.
    • (2005) Cell Biol. Int. , vol.29 , pp. 903-913
    • Mamun, E.A.1    Cantrill, L.C.2    Overall, R.L.3    Sutton, B.G.4
  • 37
    • 0034664251 scopus 로고    scopus 로고
    • 31P NMR spectroscopy of Trypanosoma brucei, Trypanosoma cruzi, and Leishmania major. Evidence for high levels of condensed inorganic phosphates
    • Moreno, B., Urbina, J.A., Oldfield, E., Bailey, B.N., Rodrigues, C.O., and, Docampo, R., (2000) 31P NMR spectroscopy of Trypanosoma brucei, Trypanosoma cruzi, and Leishmania major. Evidence for high levels of condensed inorganic phosphates. J. Biol. Chem. 275, 28356-28362.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28356-28362
    • Moreno, B.1    Urbina, J.A.2    Oldfield, E.3    Bailey, B.N.4    Rodrigues, C.O.5    Docampo, R.6
  • 38
    • 37249085076 scopus 로고    scopus 로고
    • Newly formed vacuoles in root meristems of barley and pea seedlings have characteristics of both protein storage and lytic vacuoles
    • Olbrich, A., Hillmer, S., Hinz, G., Oliviusson, P., and, Robinson, D.G., (2007) Newly formed vacuoles in root meristems of barley and pea seedlings have characteristics of both protein storage and lytic vacuoles. Plant Physiol. 145, 1383-1394.
    • (2007) Plant Physiol. , vol.145 , pp. 1383-1394
    • Olbrich, A.1    Hillmer, S.2    Hinz, G.3    Oliviusson, P.4    Robinson, D.G.5
  • 39
    • 0032849895 scopus 로고    scopus 로고
    • Mutational analyses of yeast RNA triphosphatases highlight a common mechanism of metal-dependent NTP hydrolysis and a means of targeting enzymes to pre-mRNAs in vivo by fusion to the guanylyltransferase component of the capping apparatus
    • Pei, Y., Ho, C.K., Schwer, B., and, Shuman, S., (1999) Mutational analyses of yeast RNA triphosphatases highlight a common mechanism of metal-dependent NTP hydrolysis and a means of targeting enzymes to pre-mRNAs in vivo by fusion to the guanylyltransferase component of the capping apparatus. J. Biol. Chem. 274, 28865-28874.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28865-28874
    • Pei, Y.1    Ho, C.K.2    Schwer, B.3    Shuman, S.4
  • 40
    • 0033562339 scopus 로고    scopus 로고
    • A Saccharomyces cerevisiae RNA 5′-triphosphatase related to mRNA capping enzyme
    • Rodriguez, C.R., Tagaki, T., Cho, E.J., and, Buratowski, S., (1999) A Saccharomyces cerevisiae RNA 5′-triphosphatase related to mRNA capping enzyme. Nucleic Acids Res. 27, 2181-2188.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2181-2188
    • Rodriguez, C.R.1    Tagaki, T.2    Cho, E.J.3    Buratowski, S.4
  • 41
    • 0035854697 scopus 로고    scopus 로고
    • Rapid changes in polyphosphate content within acidocalcisomes in response to cell growth, differentiation, and environmental stress in Trypanosoma cruzi
    • Ruiz, F.A., Rodrigues, C.O., and, Docampo, R., (2001) Rapid changes in polyphosphate content within acidocalcisomes in response to cell growth, differentiation, and environmental stress in Trypanosoma cruzi. J. Biol. Chem. 276, 26114-26121.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26114-26121
    • Ruiz, F.A.1    Rodrigues, C.O.2    Docampo, R.3
  • 42
    • 70849134876 scopus 로고    scopus 로고
    • Cellular pathways regulating responses to compatible and self-incompatible pollen in Brassica and Arabidopsis stigmas intersect at Exo70A1, a putative component of the exocyst complex
    • Samuel, M.A., Chong, Y.T., Haasen, K.E., Aldea-Brydges, M.G., Stone, S.L., and, Goring, D.R., (2009) Cellular pathways regulating responses to compatible and self-incompatible pollen in Brassica and Arabidopsis stigmas intersect at Exo70A1, a putative component of the exocyst complex. Plant Cell, 21, 2655-2671.
    • (2009) Plant Cell , vol.21 , pp. 2655-2671
    • Samuel, M.A.1    Chong, Y.T.2    Haasen, K.E.3    Aldea-Brydges, M.G.4    Stone, S.L.5    Goring, D.R.6
  • 43
    • 77954426175 scopus 로고    scopus 로고
    • Recent discoveries on the roles of polyphosphates in plants
    • Seufferheld, M.J., and, Curzi, M.J., (2010) Recent discoveries on the roles of polyphosphates in plants. Plant Mol. Biol. Rep. 28, 549-559.
    • (2010) Plant Mol. Biol. Rep. , vol.28 , pp. 549-559
    • Seufferheld, M.J.1    Curzi, M.J.2
  • 45
    • 0036347305 scopus 로고    scopus 로고
    • What messenger RNA capping tells us about eukaryotic evolution
    • Shuman, S., (2002) What messenger RNA capping tells us about eukaryotic evolution. Nat. Rev. Mol. Cell Biol. 3, 619-625.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 619-625
    • Shuman, S.1
  • 46
    • 0019205794 scopus 로고
    • Purification and characterization of a GTP-pyrophosphate exchange activity from vaccinia virions
    • Shuman, S., Surks, M., Furneaux, H., and, Hurwitz, J., (1980) Purification and characterization of a GTP-pyrophosphate exchange activity from vaccinia virions. J. Biol. Chem. 255, 11588-11598.
    • (1980) J. Biol. Chem. , vol.255 , pp. 11588-11598
    • Shuman, S.1    Surks, M.2    Furneaux, H.3    Hurwitz, J.4
  • 47
    • 0031801223 scopus 로고    scopus 로고
    • Aeromonas hydrophila adenylyl cyclase 2: A new class of adenylyl cyclases with thermophilic properties and sequence similarities to proteins from hyperthermophilic Archaebacteria
    • Sismeiro, O., Trotot, P., Bivillem, F., Vivares, C., and, Danchin, A., (1998) Aeromonas hydrophila adenylyl cyclase 2: a new class of adenylyl cyclases with thermophilic properties and sequence similarities to proteins from hyperthermophilic Archaebacteria. J. Bacteriol. 180, 3339-3344.
    • (1998) J. Bacteriol. , vol.180 , pp. 3339-3344
    • Sismeiro, O.1    Trotot, P.2    Bivillem, F.3    Vivares, C.4    Danchin, A.5
  • 48
    • 44849109378 scopus 로고    scopus 로고
    • Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase
    • Song, J., Bettendorff, L., Tonelli, M., and, Markley, J.L., (2008) Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase. J. Biol. Chem. 283, 10939-10948.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10939-10948
    • Song, J.1    Bettendorff, L.2    Tonelli, M.3    Markley, J.L.4
  • 49
    • 0030807902 scopus 로고    scopus 로고
    • An RNA 5′-triphosphatase related to the protein tyrosine phosphatases
    • Takagi, T., Moore, C.R., Diehn, F., and, Buratowski, S., (1997) An RNA 5′-triphosphatase related to the protein tyrosine phosphatases. Cell, 89, 867-873.
    • (1997) Cell , vol.89 , pp. 867-873
    • Takagi, T.1    Moore, C.R.2    Diehn, F.3    Buratowski, S.4
  • 52
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M.D., Isupov, M.N., and, Murshudov, G.N., (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D Biol. Crystallogr. 57, 122-133.
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 53
    • 40349091686 scopus 로고    scopus 로고
    • An 'electronic fluorescent pictograph' browser for exploring and analyzing large-scale biological data sets
    • Winter, D., Vinegar, B., Nahal, H., Ammar, R., Wilson, G.V., and, Provart, N.J., (2007) An 'electronic fluorescent pictograph' browser for exploring and analyzing large-scale biological data sets. PLoS One, 8, e718.
    • (2007) PLoS One , vol.8
    • Winter, D.1    Vinegar, B.2    Nahal, H.3    Ammar, R.4    Wilson, G.V.5    Provart, N.J.6
  • 54
    • 0030728958 scopus 로고    scopus 로고
    • Structure-function analysis of the triphosphatase component of vaccinia virus mRNA capping enzyme
    • Yu, L., Martins, A., Deng, L., and, Shuman, S., (1997) Structure-function analysis of the triphosphatase component of vaccinia virus mRNA capping enzyme. J. Virol. 71, 9837-9843.
    • (1997) J. Virol. , vol.71 , pp. 9837-9843
    • Yu, L.1    Martins, A.2    Deng, L.3    Shuman, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.