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Volumn 413, Issue 2, 2011, Pages 438-450

A new structural form in the SAM/metal-dependent O'methyltransferase family: MycE from the mycinamicin biosynthetic pathway

Author keywords

antibiotic biosynthesis; macrolide antibiotic; metal dependent methyltransfer; methyltransferase; S adenosylmethionine dependent methyltransfer

Indexed keywords

ADENOSYLHOMOCYSTEINASE; HISTIDINE; MAGNESIUM; METAL; METHYLTRANSFERASE; MONOMER; MYCINAMICIN; POLYPEPTIDE; PROTEIN MYCE; TETRAMER; TYROSINE; UNCLASSIFIED DRUG;

EID: 80054746761     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.08.040     Document Type: Article
Times cited : (20)

References (56)
  • 1
    • 34247626294 scopus 로고    scopus 로고
    • Unusual sugar biosynthesis and natural product glycodiversification
    • DOI 10.1038/nature05814, PII NATURE05814
    • Thibodeaux C.J., Melancon C.E., and Liu H.W. Unusual sugar biosynthesis and natural product glycodiversification Nature 446 2007 1008 1016 (Pubitemid 46676062)
    • (2007) Nature , vol.446 , Issue.7139 , pp. 1008-1016
    • Thibodeaux, C.J.1    Melancon, C.E.2    Liu, H.-W.3
  • 2
    • 0035119588 scopus 로고    scopus 로고
    • Structures of two natural product rnethyltransferases reveal the basis for substrate specificity in plant o-methyltransferases
    • DOI 10.1038/85029
    • Zubieta C., He X.Z., Dixon R.A., and Noel J.P. Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases Nat. Struct. Biol. 8 2001 271 279 (Pubitemid 32180056)
    • (2001) Nature Structural Biology , vol.8 , Issue.3 , pp. 271-279
    • Zubieta, C.1    He, X.-Z.2    Dixon, R.A.3    Noel, J.P.4
  • 3
    • 0019177994 scopus 로고
    • Mycinamicins, new macrolide antibiotics. I. Taxonomy, production, isolation, characterization and properties
    • Satoi I., Muto N., Hayashi M., Fujii T., and Otani M. Mycinamicins, new macrolide antibiotics. I. Taxonomy, production, isolation, characterization and properties J. Antibiot. 33 1980 364 376 (Pubitemid 11237732)
    • (1980) Journal of Antibiotics , vol.33 , Issue.4 , pp. 364-376
    • Satoi, S.1    Muto, N.2    Hayashi, M.3
  • 4
    • 0037458152 scopus 로고    scopus 로고
    • Organization of the biosynthetic gene cluster for the polyketide macrolide mycinamicin in Micromonospora griseorubida
    • DOI 10.1016/S0378-1097(02)01123-0, PII S0378109702011230
    • Anzai Y., Saito N., Tanaka M., Kinoshita K., Koyama Y., and Kato F. Organization of the biosynthetic gene cluster for the polyketide macrolide mycinamicin in Micromonospora griseorubida FEMS Microbiol. Lett. 218 2003 135 141 (Pubitemid 36173539)
    • (2003) FEMS Microbiology Letters , vol.218 , Issue.1 , pp. 135-141
    • Anzai, Y.1    Saito, N.2    Tanaka, M.3    Kinoshita, K.4    Koyama, Y.5    Kato, F.6
  • 5
    • 4444369565 scopus 로고    scopus 로고
    • The targeted inactivation of polyketide synthase mycAV in the mycinamicin producer, Micromonospora griseorubida, and a complementation study
    • DOI 10.1016/j.femsle.2004.07.050, PII S0378109704005543
    • Anzai Y., Ishii Y., Yoda Y., Kinoshita K., and Kato F. The targeted inactivation of polyketide synthase mycAV in the mycinamicin producer, Micromonospora griseorubida, and a complementation study FEMS Microbiol. Lett. 238 2004 315 320 (Pubitemid 39195156)
    • (2004) FEMS Microbiology Letters , vol.238 , Issue.2 , pp. 315-320
    • Anzai, Y.1    Ishii, Y.2    Yoda, Y.3    Kinoshita, K.4    Kato, F.5
  • 6
    • 51649100529 scopus 로고    scopus 로고
    • Functional analysis of MycCI and MycG, cytochrome P450 enzymes involved in biosynthesis of mycinamicin macrolide antibiotics
    • Anzai Y., Li S., Chaulagain M.R., Kinoshita K., Kato F., Montgomery J., and Sherman D.H. Functional analysis of MycCI and MycG, cytochrome P450 enzymes involved in biosynthesis of mycinamicin macrolide antibiotics Chem. Biol. 15 2008 950 959
    • (2008) Chem. Biol. , vol.15 , pp. 950-959
    • Anzai, Y.1    Li, S.2    Chaulagain, M.R.3    Kinoshita, K.4    Kato, F.5    Montgomery, J.6    Sherman, D.H.7
  • 7
    • 67651160555 scopus 로고    scopus 로고
    • Functional analysis of MycE and MycF, two O-methyltransferases involved in the biosynthesis of mycinamicin macrolide antibiotics
    • Li S., Anzai Y., Kinoshita K., Kato F., and Sherman D.H. Functional analysis of MycE and MycF, two O-methyltransferases involved in the biosynthesis of mycinamicin macrolide antibiotics ChemBioChem 10 2009 1297 1301
    • (2009) ChemBioChem , vol.10 , pp. 1297-1301
    • Li, S.1    Anzai, Y.2    Kinoshita, K.3    Kato, F.4    Sherman, D.H.5
  • 8
    • 77149179036 scopus 로고    scopus 로고
    • Gene targeting for O-methyltransferase genes, mycE and mycF, on the chromosome of Micromonospora griseorubida producing mycinamicin with a disruption cassette containing the bacteriophage φc31 attB attachment site
    • Tsukada S., Anzai Y., Li S., Kinoshita K., Sherman D.H., and Kato F. Gene targeting for O-methyltransferase genes, mycE and mycF, on the chromosome of Micromonospora griseorubida producing mycinamicin with a disruption cassette containing the bacteriophage φC31 attB attachment site FEMS Microbiol. Lett. 304 2010 148 156
    • (2010) FEMS Microbiol. Lett. , vol.304 , pp. 148-156
    • Tsukada, S.1    Anzai, Y.2    Li, S.3    Kinoshita, K.4    Sherman, D.H.5    Kato, F.6
  • 9
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: A chronicle of convergence
    • DOI 10.1016/S0968-0004(03)00090-2
    • Schubert H.L., Blumenthal R.M., and Cheng X. Many paths to methyltransfer: a chronicle of convergence Trends Biochem. Sci. 28 2003 329 335 (Pubitemid 36776296)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.6 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 10
    • 0036917889 scopus 로고    scopus 로고
    • SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold
    • DOI 10.1016/S0959-440X(02)00391-3
    • Martin J.L., and McMillan F.M. SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold Curr. Opin. Struct. Biol. 12 2002 783 793 (Pubitemid 36009496)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.6 , pp. 783-793
    • Martin, J.L.1    McMillan, F.M.2
  • 11
    • 44649191697 scopus 로고    scopus 로고
    • Crystal structures of human 108V and 108M catechol O-methyltransferase
    • Rutherford K., Le Trong I., Stenkamp R.E., and Parson W.W. Crystal structures of human 108V and 108M catechol O-methyltransferase J. Mol. Biol. 380 2008 120 130
    • (2008) J. Mol. Biol. , vol.380 , pp. 120-130
    • Rutherford, K.1    Le Trong, I.2    Stenkamp, R.E.3    Parson, W.W.4
  • 12
    • 0028210328 scopus 로고
    • Crystal structure of catechol O-methyltransferase
    • DOI 10.1038/368354a0
    • Vidgren J., Svensson L.A., and Liljas A. Crystal structure of catechol O-methyltransferase Nature 368 1994 354 358 (Pubitemid 24104273)
    • (1994) Nature , vol.368 , Issue.6469 , pp. 354-358
    • Vidgren, J.1    Svensson, L.A.2    Liljas, A.3
  • 13
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm L., and Rosenstrom P. Dali server: conservation mapping in 3D Nucleic Acids Res. 38 2010 W545 W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 14
    • 42949154908 scopus 로고    scopus 로고
    • Three-dimensional structure/function analysis of SCP-2-like2 reveals differences among SCP-2 family members
    • Dyer D.H., Wessely V., Forest K.T., and Lan Q. Three-dimensional structure/function analysis of SCP-2-like2 reveals differences among SCP-2 family members J. Lipid Res. 49 2008 644 653
    • (2008) J. Lipid Res. , vol.49 , pp. 644-653
    • Dyer, D.H.1    Wessely, V.2    Forest, K.T.3    Lan, Q.4
  • 18
    • 73149115504 scopus 로고    scopus 로고
    • The crystal structure of the novobiocin biosynthetic enzyme NovP: The first representative structure for the TylF O-methyltransferase superfamily
    • Gomez Garcia I., Stevenson C.E., Uson I., Freel Meyers C.L., Walsh C.T., and Lawson D.M. The crystal structure of the novobiocin biosynthetic enzyme NovP: the first representative structure for the TylF O-methyltransferase superfamily J. Mol. Biol. 395 2010 390 407
    • (2010) J. Mol. Biol. , vol.395 , pp. 390-407
    • Gomez Garcia, I.1    Stevenson, C.E.2    Uson, I.3    Freel Meyers, C.L.4    Walsh, C.T.5    Lawson, D.M.6
  • 19
    • 79551635145 scopus 로고    scopus 로고
    • Structure-function analyses of a caffeic acid O-methyltransferase from perennial ryegrass reveal the molecular basis for substrate preference
    • Louie G.V., Bowman M.E., Tu Y., Mouradov A., Spangenberg G., and Noel J.P. Structure-function analyses of a caffeic acid O-methyltransferase from perennial ryegrass reveal the molecular basis for substrate preference Plant Cell 22 2010 4114 4127
    • (2010) Plant Cell , vol.22 , pp. 4114-4127
    • Louie, G.V.1    Bowman, M.E.2    Tu, Y.3    Mouradov, A.4    Spangenberg, G.5    Noel, J.P.6
  • 20
    • 70349939426 scopus 로고    scopus 로고
    • Structural insights into mechanisms of the small RNA methyltransferase HEN1
    • Huang Y., Ji L., Huang Q., Vassylyev D.G., Chen X., and Ma J.B. Structural insights into mechanisms of the small RNA methyltransferase HEN1 Nature 461 2009 823 827
    • (2009) Nature , vol.461 , pp. 823-827
    • Huang, Y.1    Ji, L.2    Huang, Q.3    Vassylyev, D.G.4    Chen, X.5    Ma, J.B.6
  • 21
    • 33745842198 scopus 로고    scopus 로고
    • Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine methyltransferases
    • DOI 10.1074/jbc.M602257200
    • Couture J.F., Hauk G., Thompson M.J., Blackburn G.M., and Trievel R.C. Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine methyltransferases J. Biol. Chem. 281 2006 19280 19287 (Pubitemid 44035432)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.28 , pp. 19280-19287
    • Couture, J.-F.1    Hauk, G.2    Thompson, M.J.3    Blackburn, G.M.4    Trievel, R.C.5
  • 22
    • 0032948086 scopus 로고    scopus 로고
    • The tylosin biosynthetic cluster from Streptomyces fradiae: Genetic organization of the left region
    • Fouces R., Mellado E., Diez B., and Barredo J.L. The tylosin biosynthetic cluster from Streptomyces fradiae: genetic organization of the left region Microbiology 145 1999 855 868 (Pubitemid 29179202)
    • (1999) Microbiology , vol.145 , Issue.4 , pp. 855-868
    • Fouces, R.1    Mellado, E.2    Diez, B.3    Barredo, J.L.4
  • 24
    • 0035377584 scopus 로고    scopus 로고
    • Deoxysugar methylation during biosynthesis of the antitumor polyketide elloramycin by Streptomyces olivaceus
    • Patallo E.P., Blanco G., Fischer C., Brana A.F., Rohr J., Mendez C., and Salas J.A. Deoxysugar methylation during biosynthesis of the antitumor polyketide elloramycin by Streptomyces olivaceus J. Biol. Chem. 276 2001 18765 18774
    • (2001) J. Biol. Chem. , vol.276 , pp. 18765-18774
    • Patallo, E.P.1    Blanco, G.2    Fischer, C.3    Brana, A.F.4    Rohr, J.5    Mendez, C.6    Salas, J.A.7
  • 25
    • 0034862868 scopus 로고    scopus 로고
    • Functional analysis of OleY L-oleandrosyl 3-O-methyltransferase of the oleandomycin biosynthetic pathway in Streptomyces antibioticus
    • DOI 10.1128/JB.183.18.5358-5363.2001
    • Rodriguez L., Rodriguez D., Olano C., Brana A.F., Mendez C., and Salas J.A. Functional analysis of OleY l-oleandrosyl 3-O-methyltransferase of the oleandomycin biosynthetic pathway in Streptomyces antibioticus J. Bacteriol. 183 2001 5358 5363 (Pubitemid 32802608)
    • (2001) Journal of Bacteriology , vol.183 , Issue.18 , pp. 5358-5363
    • Rodriguez, L.1    Rodriguez, D.2    Olano, C.3    Brana, A.F.4    Mendez, C.5    Salas, J.A.6
  • 26
    • 0030658115 scopus 로고    scopus 로고
    • Characterization of Streptomyces nogalater genes encoding enzymes involved in glycosylation steps in nogalamycin biosynthesis
    • Torkkell S., Ylihonko K., Hakala J., Skurnik M., and Mantsala P. Characterization of Streptomyces nogalater genes encoding enzymes involved in glycosylation steps in nogalamycin biosynthesis Mol. Gen. Genet. 256 1997 203 209
    • (1997) Mol. Gen. Genet. , vol.256 , pp. 203-209
    • Torkkell, S.1    Ylihonko, K.2    Hakala, J.3    Skurnik, M.4    Mantsala, P.5
  • 28
    • 5444249226 scopus 로고    scopus 로고
    • Chalcomycin biosynthesis gene cluster from Streptomyces bikiniensis: Novel features of an unusual ketolide produced through expression of the chm polyketide synthase in Streptomyces fradiae
    • DOI 10.1128/AAC.48.12.4703-4712.2004
    • Ward S.L., Hu Z., Schirmer A., Reid R., Revill W.P., and Reeves C.D. Chalcomycin biosynthesis gene cluster from Streptomyces bikiniensis: novel features of an unusual ketolide produced through expression of the chm polyketide synthase in Streptomyces fradiae Antimicrob. Agents Chemother. 48 2004 4703 4712 (Pubitemid 39577675)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.12 , pp. 4703-4712
    • Ward, S.L.1    Hu, Z.2    Schirmer, A.3    Reid, R.4    Revill, W.P.5    Reeves, C.D.6    Petrakovsky, O.V.7    Dong, S.D.8    Katz, L.9
  • 29
    • 0029937535 scopus 로고    scopus 로고
    • A gene cluster involved in nogalamycin biosynthesis from Streptomyces nogalater: Sequence analysis and complementation of early-block mutations in the anthracycline pathway
    • Ylihonko K., Tuikkanen J., Jussila S., Cong L., and Mantsala P. A gene cluster involved in nogalamycin biosynthesis from Streptomyces nogalater: sequence analysis and complementation of early-block mutations in the anthracycline pathway Mol. Gen. Genet. 251 1996 113 120
    • (1996) Mol. Gen. Genet. , vol.251 , pp. 113-120
    • Ylihonko, K.1    Tuikkanen, J.2    Jussila, S.3    Cong, L.4    Mantsala, P.5
  • 30
    • 58849155679 scopus 로고    scopus 로고
    • Crystal structures of the apo and holo form of rat catechol-O- methyltransferase
    • Tsuji E., Okazaki K., Isaji M., and Takeda K. Crystal structures of the apo and holo form of rat catechol-O-methyltransferase J. Struct. Biol. 165 2009 133 139
    • (2009) J. Struct. Biol. , vol.165 , pp. 133-139
    • Tsuji, E.1    Okazaki, K.2    Isaji, M.3    Takeda, K.4
  • 31
    • 80054735178 scopus 로고    scopus 로고
    • The role of synthesis and biosynthetic logic
    • Elsevier Oxford, UK
    • Ding Y., and Sherman D.H. The role of synthesis and biosynthetic logic Comprehensive Natural Products II 2010 Elsevier Oxford, UK 559 579
    • (2010) Comprehensive Natural Products II , pp. 559-579
    • Ding, Y.1    Sherman, D.H.2
  • 35
    • 33748750539 scopus 로고    scopus 로고
    • The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae
    • DOI 10.1074/jbc.M605478200
    • Sherman D.H., Li S., Yermalitskaya L.V., Kim Y., Smith J.A., Waterman M.R., and Podust L.M. The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae J. Biol. Chem. 281 2006 26289 26297 (Pubitemid 44401837)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.36 , pp. 26289-26297
    • Sherman, D.H.1    Li, S.2    Yermalitskaya, L.V.3    Kim, Y.4    Smith, J.A.5    Waterman, M.R.6    Podust, L.M.7
  • 36
    • 77956013893 scopus 로고    scopus 로고
    • Structure of cytochrome P450 PimD suggests epoxidation of the polyene macrolide pimaricin occurs via a hydroperoxoferric intermediate
    • Kells P.M., Ouellet H., Santos-Aberturas J., Aparicio J.F., and Podust L.M. Structure of cytochrome P450 PimD suggests epoxidation of the polyene macrolide pimaricin occurs via a hydroperoxoferric intermediate Chem. Biol. 17 2010 841 851
    • (2010) Chem. Biol. , vol.17 , pp. 841-851
    • Kells, P.M.1    Ouellet, H.2    Santos-Aberturas, J.3    Aparicio, J.F.4    Podust, L.M.5
  • 37
    • 77952754570 scopus 로고    scopus 로고
    • Regio- and stereospecificity of filipin hydroxylation sites revealed by crystal structures of cytochrome P450 105P1 and 105D6 from Streptomyces avermitilis
    • Xu L.H., Fushinobu S., Takamatsu S., Wakagi T., Ikeda H., and Shoun H. Regio- and stereospecificity of filipin hydroxylation sites revealed by crystal structures of cytochrome P450 105P1 and 105D6 from Streptomyces avermitilis J. Biol. Chem. 285 2010 16844 16853
    • (2010) J. Biol. Chem. , vol.285 , pp. 16844-16853
    • Xu, L.H.1    Fushinobu, S.2    Takamatsu, S.3    Wakagi, T.4    Ikeda, H.5    Shoun, H.6
  • 38
    • 0034798749 scopus 로고    scopus 로고
    • Biosynthesis and combinatorial biosynthesis of pikromycin-related macrolides in Streptomyces venezuelae
    • DOI 10.1006/mben.2000.0167
    • Xue Y., and Sherman D.H. Biosynthesis and combinatorial biosynthesis of pikromycin-related macrolides in Streptomyces venezuelae Metab. Eng. 3 2001 15 26 (Pubitemid 32948855)
    • (2001) Metabolic Engineering , vol.3 , Issue.1 , pp. 15-26
    • Xue, Y.1    Sherman, D.H.2
  • 40
    • 21644437191 scopus 로고    scopus 로고
    • Probing the breadth of macrolide glycosyltransferases: In vitro remodeling of a polyketide antibiotic creates active bacterial uptake and enhances potency
    • DOI 10.1021/ja051482n
    • Yang M., Proctor M.R., Bolam D.N., Errey J.C., Field R.A., Gilbert H.J., and Davis B.G. Probing the breadth of macrolide glycosyltransferases: in vitro remodeling of a polyketide antibiotic creates active bacterial uptake and enhances potency J. Am. Chem. Soc. 127 2005 9336 9337 (Pubitemid 40934725)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.26 , pp. 9336-9337
    • Yang, M.1    Proctor, M.R.2    Bolam, D.N.3    Errey, J.C.4    Field, R.A.5    Gilbert, H.J.6    Davis, B.G.7
  • 41
    • 0034846215 scopus 로고    scopus 로고
    • Production of selenomethionine-labelled proteins using simplified culture conditions and generally applicable host/vector systems
    • DOI 10.1007/s002530100690
    • Guerrero S.A., Hecht H.J., Hofmann B., Biebl H., and Singh M. Production of selenomethionine-labelled proteins using simplified culture conditions and generally applicable host/vector systems Appl. Microbiol. Biotechnol. 56 2001 718 723 (Pubitemid 32831598)
    • (2001) Applied Microbiology and Biotechnology , vol.56 , Issue.5-6 , pp. 718-723
    • Guerrero, S.A.1    Hecht, H.-J.2    Hofmann, B.3    Biebl, H.4    Singh, M.5
  • 42
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z., and Minor V. Processing of X-ray diffraction data collected in oscillation mode Macromolecular Crystalllography, part A 276 1997 Academic Press New York, NY 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 46
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model building by template matching and iterative fragment extension
    • DOI 10.1107/S0907444902018036
    • Terwilliger T.C. Automated main-chain model building by template matching and iterative fragment extension Acta Crystallogr., Sect. D: Biol. Crystallogr. 59 2003 38 44 (Pubitemid 36117204)
    • (2003) Acta Crystallographica Section D: Biological Crystallography , vol.59 , Issue.1 , pp. 38-44
    • Terwilliger, T.C.1
  • 49
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS Refinement in REFMAC at Moderate Resolutions
    • DOI 10.1016/S0076-6879(03)74014-2
    • Winn M.D., Murshudov G.N., and Papiz M.Z. Macromolecular TLS refinement in REFMAC at moderate resolutions Methods Enzymol. 374 2003 300 321 (Pubitemid 37531815)
    • (2003) Methods in Enzymology , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 50
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter J., and Merritt E.A. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion Acta Crystallogr., Sect. D: Biol. Crystallogr. 62 2006 439 450
    • (2006) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 54
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680 (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 55
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2-a multiple sequence alignment editor and analysis workbench
    • Waterhouse A.M., Procter J.B., Martin D.M., Clamp M., and Barton G.J. Jalview Version 2-a multiple sequence alignment editor and analysis workbench Bioinformatics 25 2009 1189 1191
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5


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