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Volumn 7, Issue , 2007, Pages

Phylogenetic analysis of condensation domains in NRPS sheds light on their functional evolution

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA AMANITIN; AMINO ACID DERIVATIVE; BETA HYDROXYCARBOXYLIC ACID; BETA HYDROXYL FATTY ACID; BLEOMYCIN; CYCLOSPORIN A; CYSTEINE; NON RIBOSOMAL PEPTIDE SYNTHASE; PENICILLIN G; PEPTIDE SYNTHASE; SERINE; THREONINE; UNCLASSIFIED DRUG; VANCOMYCIN; NON-RIBOSOMAL PEPTIDE SYNTHASE;

EID: 34250710858     PISSN: None     EISSN: 14712148     Source Type: Journal    
DOI: 10.1186/1471-2148-7-78     Document Type: Article
Times cited : (257)

References (72)
  • 1
    • 0037036464 scopus 로고    scopus 로고
    • Identification of peptaibols from Trichoderma virens and cloning of a peptaibol synthetase
    • 10.1074/jbc.M201654200. 11909873
    • Identification of peptaibols from Trichoderma virens and cloning of a peptaibol synthetase. A Wiest D Grzegorski BW Xu C Goulard S Rebuffat DJ Ebbole B Bodo C Kenerley, J Biol Chem 2002 277 23 20862 20868 10.1074/jbc.M201654200 11909873
    • (2002) J Biol Chem , vol.277 , Issue.23 , pp. 20862-20868
    • Wiest, A.1    Grzegorski, D.2    Xu, B.W.3    Goulard, C.4    Rebuffat, S.5    Ebbole, D.J.6    Bodo, B.7    Kenerley, C.8
  • 2
    • 14844362054 scopus 로고    scopus 로고
    • Molecular mechanisms underlying nonribosomal peptide synthesis: Approaches to new antibiotics
    • 15700962. 10.1021/cr0301191
    • Molecular mechanisms underlying nonribosomal peptide synthesis: approaches to new antibiotics. SA Sieber MA Marahiel, Chem Rev 2005 105 2 715 738 15700962 10.1021/cr0301191
    • (2005) Chem Rev , vol.105 , Issue.2 , pp. 715-738
    • Sieber, S.A.1    Marahiel, M.A.2
  • 3
    • 3142672123 scopus 로고    scopus 로고
    • Substrate recognition by nonribosomal peptide synthetase multi-enzymes
    • 15184549. 10.1099/mic.0.26837-0
    • Substrate recognition by nonribosomal peptide synthetase multi-enzymes. S Lautru GL Challis, Microbiology 2004 150 Pt 6 1629 1636 15184549 10.1099/mic.0.26837-0
    • (2004) Microbiology , vol.150 , Issue.PART 6 , pp. 1629-1636
    • Lautru, S.1    Challis, G.L.2
  • 4
    • 33744830630 scopus 로고    scopus 로고
    • The thioesterase domain of the fengycin biosynthesis cluster: A structural base for the macrocyclization of a non-ribosomal lipopeptide
    • 16697411. 10.1016/j.jmb.2006.03.062
    • The thioesterase domain of the fengycin biosynthesis cluster: a structural base for the macrocyclization of a non-ribosomal lipopeptide. SA Samel B Wagner MA Marahiel LO Essen, J Mol Biol 2006 359 4 876 889 16697411 10.1016/j.jmb.2006.03.062
    • (2006) J Mol Biol , vol.359 , Issue.4 , pp. 876-889
    • Samel, S.A.1    Wagner, B.2    Marahiel, M.A.3    Essen, L.O.4
  • 5
    • 34250771295 scopus 로고    scopus 로고
    • Bioactive microbial metabolites
    • 15813176
    • Bioactive microbial metabolites. J Brédy, J Antibiot (Tokyo) 2005 58 1 26 15813176
    • (2005) J Antibiot (Tokyo) , vol.58 , pp. 1-26
    • Brédy, J.1
  • 6
    • 0033780306 scopus 로고    scopus 로고
    • Structural organization of microcystin biosynthesis in Microcystis aeruginosa PCC7806: An integrated peptide-polyketide synthetase system
    • 10.1016/S1074-5521(00)00021-1. 11033079
    • Structural organization of microcystin biosynthesis in Microcystis aeruginosa PCC7806: an integrated peptide-polyketide synthetase system. D Tillett E Dittmann M Erhard H von Döhren T Börner BA Neilan, Chem Biol 2000 7 10 753 764 10.1016/S1074-5521(00)00021-1 11033079
    • (2000) Chem Biol , vol.7 , Issue.10 , pp. 753-764
    • Tillett, D.1    Dittmann, E.2    Erhard, M.3    Von Döhren, H.4    Börner, T.5    Neilan, B.A.6
  • 7
    • 0029034197 scopus 로고
    • Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains
    • 10.1126/science.7604280. 7604280
    • Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains. T Stachelhaus A Schneider MA Marahiel, Science 1995 269 5220 69 72 10.1126/science.7604280 7604280
    • (1995) Science , vol.269 , Issue.5220 , pp. 69-72
    • Stachelhaus, T.1    Schneider, A.2    Marahiel, M.A.3
  • 8
    • 0034705130 scopus 로고    scopus 로고
    • Construction of hybrid peptide synthetases by module and domain fusions
    • 10811885. 10.1073/pnas.100075897
    • Construction of hybrid peptide synthetases by module and domain fusions. HD Mootz D Schwarzer MA Marahiel, Proc Natl Acad Sci USA 2000 97 11 5848 5853 10811885 10.1073/pnas.100075897
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.11 , pp. 5848-5853
    • Mootz, H.D.1    Schwarzer, D.2    Marahiel, M.A.3
  • 9
    • 0037130634 scopus 로고    scopus 로고
    • Decreasing the ring size of a cyclic nonribosomal peptide antibiotic by in-frame module deletion in the biosynthetic genes
    • 10.1021/ja027276m. 12224936
    • Decreasing the ring size of a cyclic nonribosomal peptide antibiotic by in-frame module deletion in the biosynthetic genes. HD Mootz N Kessler U Linne K Eppelmann D Schwarzer MA Marahiel, J Am Chem Soc 2002 124 37 10980 10981 10.1021/ja027276m 12224936
    • (2002) J Am Chem Soc , vol.124 , Issue.37 , pp. 10980-10981
    • Mootz, H.D.1    Kessler, N.2    Linne, U.3    Eppelmann, K.4    Schwarzer, D.5    Marahiel, M.A.6
  • 10
    • 0037199494 scopus 로고    scopus 로고
    • Exploitation of the selectivity-conferring code of nonribosomal peptide synthetases for the rational design of novel peptide antibiotics
    • 10.1021/bi0259406. 12135394
    • Exploitation of the selectivity-conferring code of nonribosomal peptide synthetases for the rational design of novel peptide antibiotics. K Eppelmann T Stachelhaus MA Marahiel, Biochemistry 2002 41 30 9718 9726 10.1021/bi0259406 12135394
    • (2002) Biochemistry , vol.41 , Issue.30 , pp. 9718-9726
    • Eppelmann, K.1    Stachelhaus, T.2    Marahiel, M.A.3
  • 11
    • 9244234513 scopus 로고    scopus 로고
    • Biosynthesis of nonribosomal peptides
    • 15487945. 10.1146/annurev.micro.58.030603.123615
    • Biosynthesis of nonribosomal peptides. R Finking MA Marahiel, Annu Rev Microbiol 2004 58 453 488 15487945 10.1146/annurev.micro.58.030603.123615
    • (2004) Annu Rev Microbiol , vol.58 , pp. 453-488
    • Finking, R.1    Marahiel, M.A.2
  • 13
    • 27744519951 scopus 로고    scopus 로고
    • Generation of D amino acid residues in assembly of arthrofactin by dual condensation/epimerization domains
    • 16298298. 10.1016/j.chembiol.2005.08.010
    • Generation of D amino acid residues in assembly of arthrofactin by dual condensation/epimerization domains. CJ Balibar FH Vaillancourt CT Walsh, Chem Biol 2005 12 11 1189 1200 16298298 10.1016/j.chembiol.2005.08.010
    • (2005) Chem Biol , vol.12 , Issue.11 , pp. 1189-1200
    • Balibar, C.J.1    Vaillancourt, F.H.2    Walsh, C.T.3
  • 14
    • 0036295033 scopus 로고    scopus 로고
    • The structure of VibH represents nonribosomal peptide synthetase condensation, cyclization and epimerization domains
    • 12055621
    • The structure of VibH represents nonribosomal peptide synthetase condensation, cyclization and epimerization domains. TA Keating CG Marshall CT Walsh AE Keating, Nat Struct Biol 2002 9 7 522 526 12055621
    • (2002) Nat Struct Biol , vol.9 , Issue.7 , pp. 522-526
    • Keating, T.A.1    Marshall, C.G.2    Walsh, C.T.3    Keating, A.E.4
  • 15
    • 0014409012 scopus 로고
    • Surfactin, a crystalline peptidelipid surfactant produced by Bacillus subtilis : iisolation, characterization and its inhibition of fibrin clot formation
    • 10.1016/0006-291X(68)90503-2. 4968234
    • Surfactin, a crystalline peptidelipid surfactant produced by Bacillus subtilis : isolation, characterization and its inhibition of fibrin clot formation. K Arima A Kakinuma G Tamura, Biochem Biophys Res Commun 1968 31 3 488 494 10.1016/0006-291X(68)90503-2 4968234
    • (1968) Biochem Biophys Res Commun , vol.31 , Issue.3 , pp. 488-494
    • Arima, K.1    Kakinuma, A.2    Tamura, G.3
  • 16
    • 0026020738 scopus 로고
    • Structural analysis of Bacillus licheniformis 86 surfactant
    • 10.1007/BF01575602. 1367206
    • Structural analysis of Bacillus licheniformis 86 surfactant. S Horowitz W Griffin, J Ind Microbiol 1991 7 45 52 10.1007/BF01575602 1367206
    • (1991) J Ind Microbiol , vol.7 , pp. 45-52
    • Horowitz, S.1    Griffin, W.2
  • 17
    • 0030663849 scopus 로고    scopus 로고
    • Sequence completion, identification and definition of the fengycin operon in Bacillus subtilis 168
    • 9387222
    • Sequence completion, identification and definition of the fengycin operon in Bacillus subtilis 168. V Tosato A Albertini M Zotti S Sonda C Bruschi, Microbiology 1997 143 Pt 11 3443 3450 9387222
    • (1997) Microbiology , vol.143 , Issue.PART 11 , pp. 3443-3450
    • Tosato, V.1    Albertini, A.2    Zotti, M.3    Sonda, S.4    Bruschi, C.5
  • 18
    • 0027362067 scopus 로고
    • A new lipopeptide biosurfactant produced by Arthrobacter sp. strain MIS38
    • 8407822
    • A new lipopeptide biosurfactant produced by Arthrobacter sp. strain MIS38. M Morikawa H Daido T Takao SM ra ta YS moni shi T Imanaka, J Bacteriol 1993 175 20 6459 6466 8407822
    • (1993) J Bacteriol , vol.175 , Issue.20 , pp. 6459-6466
    • Morikawa, M.1    Daido, H.2    Takao, T.3    Ra Ta, S.M.4    Moni Shi, Y.S.5    Imanaka, T.6
  • 19
    • 0032955583 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of the protein template controlling biosynthesis of the lipopeptide lichenysin
    • 9864322
    • Molecular and biochemical characterization of the protein template controlling biosynthesis of the lipopeptide lichenysin. D Konz S Doekel M Marahiel, J Bacteriol 1999 181 133 140 9864322
    • (1999) J Bacteriol , vol.181 , pp. 133-140
    • Konz, D.1    Doekel, S.2    Marahiel, M.3
  • 20
    • 0027289507 scopus 로고
    • Sequence and analysis of the genetic locus responsible for surfactin synthesis in Bacillus subtilis
    • 10.1111/j.1365-2958.1993.tb01629.x. 8355609
    • Sequence and analysis of the genetic locus responsible for surfactin synthesis in Bacillus subtilis. P Cosmina F Rodriguez F de Ferra G Grandi M Perego G Venema D van Sinderen, Mol Microbiol 1993 8 5 821 831 10.1111/j.1365-2958.1993.tb01629.x 8355609
    • (1993) Mol Microbiol , vol.8 , Issue.5 , pp. 821-831
    • Cosmina, P.1    Rodriguez, F.2    De Ferra, F.3    Grandi, G.4    Perego, M.5    Venema, G.6    Van Sinderen, D.7
  • 21
    • 0028959563 scopus 로고
    • A putative new peptide synthase operon in Bacillus subtilis : ppartial characterization
    • 7711903
    • A putative new peptide synthase operon in Bacillus subtilis : partial characterization. A Tognoni E Franchi C Magistrelli E Colombo P Cosmina G Grandi, Microbiology 1995 141 Pt 3 645 648 7711903
    • (1995) Microbiology , vol.141 , Issue.PART 3 , pp. 645-648
    • Tognoni, A.1    Franchi, E.2    Magistrelli, C.3    Colombo, E.4    Cosmina, P.5    Grandi, G.6
  • 24
    • 0031024022 scopus 로고    scopus 로고
    • Pristinamycin I biosynthesis in Streptomyces pristinaespiralis : mmolecular characterization of the first two structural peptide synthetase genes
    • 9006024
    • Pristinamycin I biosynthesis in Streptomyces pristinaespiralis : molecular characterization of the first two structural peptide synthetase genes. V de Créecy-Lagard V Blanc P Gil L Naudin S Lorenzon A Famechon N Bamas-Jacques J Crouzet D Thibaut, J Bacteriol 1997 179 3 705 713 9006024
    • (1997) J Bacteriol , vol.179 , Issue.3 , pp. 705-713
    • De Créecy-Lagard, V.1    Blanc, V.2    Gil, P.3    Naudin, L.4    Lorenzon, S.5    Famechon, A.6    Bamas-Jacques, N.7    Crouzet, J.8    Thibaut, D.9
  • 25
    • 0024420904 scopus 로고
    • Subcloning, expression, and purification of the enterobactin biosynthetic enzyme 2,3-dihydroxybenzoate-AMP ligase: Demonstration of enzyme-bound (2,3-dihydroxybenzoyl)adenylate product
    • 10.1021/bi00443a008. 2531000
    • Subcloning, expression, and purification of the enterobactin biosynthetic enzyme 2,3-dihydroxybenzoate-AMP ligase: demonstration of enzyme-bound (2,3-dihydroxybenzoyl)adenylate product. FW Rusnak S Faraci CT Walsh, Biochemistry 1989 28 17 6827 6835 10.1021/bi00443a008 2531000
    • (1989) Biochemistry , vol.28 , Issue.17 , pp. 6827-6835
    • Rusnak, F.W.1    Faraci, S.2    Walsh, C.T.3
  • 26
    • 0031958021 scopus 로고    scopus 로고
    • Molecular cloning of the actinomycin synthetase gene cluster from Streptomyces chrysomallus and functional heterologous expression of the gene encoding actinomycin synthetase II
    • 9573200
    • Molecular cloning of the actinomycin synthetase gene cluster from Streptomyces chrysomallus and functional heterologous expression of the gene encoding actinomycin synthetase II. F Schauwecker F Pfennig W Schroder U Keller, J Bacteriol 1998 180 9 2468 2474 9573200
    • (1998) J Bacteriol , vol.180 , Issue.9 , pp. 2468-2474
    • Schauwecker, F.1    Pfennig, F.2    Schroder, W.3    Keller, U.4
  • 27
    • 33745017396 scopus 로고    scopus 로고
    • Formylation domain: An essential modifying enzyme for the nonribosomal biosynthesis of linear gramicidin
    • 16756271. 10.1021/ja0611240
    • Formylation domain: an essential modifying enzyme for the nonribosomal biosynthesis of linear gramicidin. G Schoenafinger N Schracke U Linne MA Marahiel, J Am Chem Soc 2006 128 23 7406 7407 16756271 10.1021/ja0611240
    • (2006) J Am Chem Soc , vol.128 , Issue.23 , pp. 7406-7407
    • Schoenafinger, G.1    Schracke, N.2    Linne, U.3    Marahiel, M.A.4
  • 28
    • 0028807689 scopus 로고
    • Multienzymatic non ribosomal peptide biosynthesis: Identification of the functional domains catalysing peptide elongation and epimerisation
    • 8521076
    • Multienzymatic non ribosomal peptide biosynthesis: identification of the functional domains catalysing peptide elongation and epimerisation. V de Crécy-Lagard P Marlière W Saurin, C R Acad Sci III 1995 318 9 927 936 8521076
    • (1995) C R Acad Sci III , vol.318 , Issue.9 , pp. 927-936
    • De Crécy-Lagard, V.1    Marlière, P.2    Saurin, W.3
  • 29
    • 9444278428 scopus 로고    scopus 로고
    • Modular Peptide Synthetases Involved in Nonribosomal Peptide Synthesis
    • 10.1021/cr960029e. 11851476
    • Modular Peptide Synthetases Involved in Nonribosomal Peptide Synthesis. M Marahiel T Stachelhaus H Mootz, Chem Rev 1997 97 7 2651 2674 10.1021/cr960029e 11851476
    • (1997) Chem Rev , vol.97 , Issue.7 , pp. 2651-2674
    • Marahiel, M.1    Stachelhaus, T.2    Mootz, H.3
  • 30
    • 0037162408 scopus 로고    scopus 로고
    • Timing of epimerization and condensation reactions in nonribosomal peptide assembly lines: Kinetic analysis of phenylalanine activating elongation modules of tyrocidine synthetase B
    • 10.1021/bi026047+. 12119033
    • Timing of epimerization and condensation reactions in nonribosomal peptide assembly lines: kinetic analysis of phenylalanine activating elongation modules of tyrocidine synthetase B. L Luo RM Kohli M Onishi U Linne MA Marahiel CT Walsh, Biochemistry 2002 41 29 9184 9196 10.1021/bi026047+ 12119033
    • (2002) Biochemistry , vol.41 , Issue.29 , pp. 9184-9196
    • Luo, L.1    Kohli, R.M.2    Onishi, M.3    Linne, U.4    Marahiel, M.A.5    Walsh, C.T.6
  • 31
    • 2142738304 scopus 로고    scopus 로고
    • WebLogo: A sequence logo generator
    • 15173120. 10.1101/gr.849004
    • WebLogo: a sequence logo generator. GE Crooks G Hon JM Chandonia SE Brenner, Genome Res 2004 14 6 1188 1190 15173120 10.1101/gr.849004
    • (2004) Genome Res , vol.14 , Issue.6 , pp. 1188-1190
    • Crooks, G.E.1    Hon, G.2    Chandonia, J.M.3    Brenner, S.E.4
  • 32
    • 0032575648 scopus 로고    scopus 로고
    • Peptide bond formation in nonribosomal peptide biosynthesis. Catalytic role of the condensation domain
    • 10.1074/jbc.273.35.22773. 9712910
    • Peptide bond formation in nonribosomal peptide biosynthesis. Catalytic role of the condensation domain. T Stachelhaus H Mootz V Bergendahl M Marahiel, J Biol Chem 1998 273 35 22773 22781 10.1074/jbc.273.35.22773 9712910
    • (1998) J Biol Chem , vol.273 , Issue.35 , pp. 22773-22781
    • Stachelhaus, T.1    Mootz, H.2    Bergendahl, V.3    Marahiel, M.4
  • 33
    • 0037431961 scopus 로고    scopus 로고
    • Dissection of the EntF condensation domain boundary and active site residues in nonribosomal peptide synthesis
    • 12564937. 10.1021/bi026867m
    • Dissection of the EntF condensation domain boundary and active site residues in nonribosomal peptide synthesis. ED Roche CT Walsh, Biochemistry 2003 42 5 1334 1344 12564937 10.1021/bi026867m
    • (2003) Biochemistry , vol.42 , Issue.5 , pp. 1334-1344
    • Roche, E.D.1    Walsh, C.T.2
  • 34
    • 0036161991 scopus 로고    scopus 로고
    • Mutational analysis of the C-domain in nonribosomal peptide synthesis
    • 10.1046/j.0014-2956.2001.02691.x. 11856321
    • Mutational analysis of the C-domain in nonribosomal peptide synthesis. V Bergendahl U Linne MA Marahiel, Eur J Biochem 2002 269 2 620 629 10.1046/j.0014-2956.2001.02691.x 11856321
    • (2002) Eur J Biochem , vol.269 , Issue.2 , pp. 620-629
    • Bergendahl, V.1    Linne, U.2    Marahiel, M.A.3
  • 35
    • 1642452921 scopus 로고    scopus 로고
    • Automated selection of positions determining functional specificity of proteins by comparative analysis of orthologous groups in protein families
    • 14739328. 10.1110/ps.03191704
    • Automated selection of positions determining functional specificity of proteins by comparative analysis of orthologous groups in protein families. OV Kalinina AA Mironov MS Gelfand AB Rakhmaninova, Protein Sci 2004 13 2 443 456 14739328 10.1110/ps.03191704
    • (2004) Protein Sci , vol.13 , Issue.2 , pp. 443-456
    • Kalinina, O.V.1    Mironov, A.A.2    Gelfand, M.S.3    Rakhmaninova, A.B.4
  • 37
    • 0032945593 scopus 로고    scopus 로고
    • DIALIGN 2: Improvement of the segment-to-segment approach to multiple sequence alignment
    • 10222408. 10.1093/bioinformatics/15.3.211
    • DIALIGN 2: improvement of the segment-to-segment approach to multiple sequence alignment. B Morgenstern, Bioinformatics 1999 15 3 211 218 10222408 10.1093/bioinformatics/15.3.211
    • (1999) Bioinformatics , vol.15 , Issue.3 , pp. 211-218
    • Morgenstern, B.1
  • 38
    • 26944502019 scopus 로고    scopus 로고
    • Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVMs)
    • 16221976. 10.1093/nar/gki885
    • Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVMs). C Rausch T Weber O Kohlbacher W Wohlleben DH Huson, Nucleic Acids Res 2005 33 18 5799 5808 16221976 10.1093/nar/gki885
    • (2005) Nucleic Acids Res , vol.33 , Issue.18 , pp. 5799-5808
    • Rausch, C.1    Weber, T.2    Kohlbacher, O.3    Wohlleben, W.4    Huson, D.H.5
  • 39
    • 0035905507 scopus 로고    scopus 로고
    • The Biosynthesis of Vancomycin-Type Glycopeptide Antibiotics-The Order of the Cyclization Steps
    • 10.1002/1521-3773(20011217)40:24<4688::AID-ANIE4688>3.0.CO;2-M. 12404385
    • The Biosynthesis of Vancomycin-Type Glycopeptide Antibiotics-The Order of the Cyclization Steps. D Bischoff S Pelzer B Bister GJ Nicholson S Stockert M Schirle W Wohlleben G Jung RD Süssmuth, Angew Chem Int Ed Engl 2001 40 24 4688 4691 10.1002/1521-3773(20011217)40:24<4688::AID-ANIE4688>3.0.CO;2-M 12404385
    • (2001) Angew Chem Int Ed Engl , vol.40 , Issue.24 , pp. 4688-4691
    • Bischoff, D.1    Pelzer, S.2    Bister, B.3    Nicholson, G.J.4    Stockert, S.5    Schirle, M.6    Wohlleben, W.7    Jung, G.8    Süssmuth, R.D.9
  • 40
    • 0035805265 scopus 로고    scopus 로고
    • The Biosynthesis of Vancomycin-Type Glycopeptide Antibiotics - New Insights into the Cyclization Steps
    • 10.1002/1521-3773(20010504)40:9<1693::AID-ANIE16930>3.0.CO;2-8. 11353482
    • The Biosynthesis of Vancomycin-Type Glycopeptide Antibiotics - New Insights into the Cyclization Steps. D Bischoff S Pelzer A Höltzel GJ Nicholson S Stockert W Wohlleben G Jung RD Süssmuth, Angew Chem Int Ed Engl 2001 40 9 1693 1696 10.1002/1521-3773(20010504)40:9<1693::AID- ANIE16930>3.0.CO;2-8 11353482
    • (2001) Angew Chem Int Ed Engl , vol.40 , Issue.9 , pp. 1693-1696
    • Bischoff, D.1    Pelzer, S.2    Höltzel, A.3    Nicholson, G.J.4    Stockert, S.5    Wohlleben, W.6    Jung, G.7    Süssmuth, R.D.8
  • 41
    • 0038167479 scopus 로고    scopus 로고
    • The gene cluster for the biosynthesis of the glycopeptide antibiotic A40926 by Nonomuraea species
    • 10.1016/S1074-5521(03)00120-0. 12837387
    • The gene cluster for the biosynthesis of the glycopeptide antibiotic A40926 by Nonomuraea species. M Sosio S Stinchi F Beltrametti A Lazzarini S Donadio, Chem Biol 2003 10 6 541 549 10.1016/S1074-5521(03)00120-0 12837387
    • (2003) Chem Biol , vol.10 , Issue.6 , pp. 541-549
    • Sosio, M.1    Stinchi, S.2    Beltrametti, F.3    Lazzarini, A.4    Donadio, S.5
  • 42
    • 0034724272 scopus 로고    scopus 로고
    • Heterologous expression in Escherichia coli of the first module of the nonribosomal peptide synthetase for chloroeremomycin, a vancomycin-type glycopeptide antibiotic
    • 10716695. 10.1073/pnas.040560597
    • Heterologous expression in Escherichia coli of the first module of the nonribosomal peptide synthetase for chloroeremomycin, a vancomycin-type glycopeptide antibiotic. JW Trauger CT Walsh, Proc Natl Acad Sci USA 2000 97 7 3112 3117 10716695 10.1073/pnas.040560597
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.7 , pp. 3112-3117
    • Trauger, J.W.1    Walsh, C.T.2
  • 43
    • 0028272082 scopus 로고
    • Purification and characterization of eucaryotic alanine racemase acting as key enzyme in cyclosporin biosynthesis
    • 8175682
    • Purification and characterization of eucaryotic alanine racemase acting as key enzyme in cyclosporin biosynthesis. K Hoffmann E Schneider-Scherzer H Kleinkauf R Zocher, J Biol Chem 1994 269 17 12710 12714 8175682
    • (1994) J Biol Chem , vol.269 , Issue.17 , pp. 12710-12714
    • Hoffmann, K.1    Schneider-Scherzer, E.2    Kleinkauf, H.3    Zocher, R.4
  • 44
    • 26844571878 scopus 로고    scopus 로고
    • Phylogenetic analysis of condensation domains in the nonribosomal peptide synthetases
    • 16182472. 10.1016/j.femsle.2005.08.041
    • Phylogenetic analysis of condensation domains in the nonribosomal peptide synthetases. N Roongsawang SP Lim K Washio K Takano S Kanaya M Morikawa, FEMS Microbiol Lett 2005 252 143 151 16182472 10.1016/j.femsle.2005.08.041
    • (2005) FEMS Microbiol Lett , vol.252 , pp. 143-151
    • Roongsawang, N.1    Lim, S.P.2    Washio, K.3    Takano, K.4    Kanaya, S.5    Morikawa, M.6
  • 47
    • 0037249633 scopus 로고    scopus 로고
    • The TIGRFAMs database of protein families
    • 12520025. 10.1093/nar/gkg128
    • The TIGRFAMs database of protein families. DH Haft JD Selengut O White, Nucleic Acids Res 2003 31 371 373 12520025 10.1093/nar/gkg128
    • (2003) Nucleic Acids Res , vol.31 , pp. 371-373
    • Haft, D.H.1    Selengut, J.D.2    White, O.3
  • 52
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: A multiple sequence alignment method with reduced time and space complexity
    • 15318951. 10.1186/1471-2105-5-113
    • MUSCLE: a multiple sequence alignment method with reduced time and space complexity. RC Edgar, BMC Bioinformatics 2004 5 113 15318951 10.1186/1471-2105-5-113
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1
  • 53
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • 15034147. 10.1093/nar/gkh340
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput. RC Edgar, Nucleic Acids Res 2004 32 5 1792 1797 15034147 10.1093/nar/gkh340
    • (2004) Nucleic Acids Res , vol.32 , Issue.5 , pp. 1792-1797
    • Edgar, R.C.1
  • 54
    • 34250693829 scopus 로고    scopus 로고
    • Quick2D. http://toolkit.tuebingen.mpg.de/quick2_d
    • Quick2D
  • 55
    • 33747856166 scopus 로고    scopus 로고
    • The MPI Bioinformatics Toolkit for protein sequence analysis
    • 16845021. 10.1093/nar/gkl217
    • The MPI Bioinformatics Toolkit for protein sequence analysis. A Biegert C Mayer M Remmert J Söding AN Lupas, Nucleic Acids Res 2006 34 Web Server W335 W339 16845021 10.1093/nar/gkl217
    • (2006) Nucleic Acids Res , Issue.34 WEB SERVER
    • Biegert, A.1    Mayer, C.2    Remmert, M.3    Söding, J.4    Lupas, A.N.5
  • 56
    • 0037447059 scopus 로고    scopus 로고
    • Amino acids determining enzyme-substrate specificity in prokaryotic and eukaryotic protein kinases
    • 12679523. 10.1073/pnas.0737647100
    • Amino acids determining enzyme-substrate specificity in prokaryotic and eukaryotic protein kinases. L Li EI Shakhnovich LA Mirny, Proc Natl Acad Sci USA 2003 100 8 4463 4468 12679523 10.1073/pnas.0737647100
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.8 , pp. 4463-4468
    • Li, L.1    Shakhnovich, E.I.2    Mirny, L.A.3
  • 59
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • 1633570
    • The rapid generation of mutation data matrices from protein sequences. DT Jones WR Taylor JM Thornton, Comput Appl Biosci 1992 8 3 275 282 1633570
    • (1992) Comput Appl Biosci , vol.8 , Issue.3 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 60
    • 0030734575 scopus 로고    scopus 로고
    • A simple method for estimating the parameter of substitution rate variation among sites
    • 9364768
    • A simple method for estimating the parameter of substitution rate variation among sites. X Gu J Zhang, Mol Biol Evol 1997 14 11 1106 1113 9364768
    • (1997) Mol Biol Evol , vol.14 , Issue.11 , pp. 1106-1113
    • Gu, X.1    Zhang, J.2
  • 62
    • 0023375195 scopus 로고
    • The Neighbor-Joining method: A new method for reconstructing phylogenetic trees
    • 3447015
    • The Neighbor-Joining method: a new method for reconstructing phylogenetic trees. N Saitou M Nei, Mol Biol Evol 1987 4 4 406 425 3447015
    • (1987) Mol Biol Evol , vol.4 , Issue.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 63
    • 3242801484 scopus 로고    scopus 로고
    • IQPNNI: Moving fast through tree space and stopping in time
    • 15163768. 10.1093/molbev/msh176
    • IQPNNI: moving fast through tree space and stopping in time. LS Vinh A von Haeseler, Mol Biol Evol 2004 21 8 1565 71 15163768 10.1093/molbev/msh176
    • (2004) Mol Biol Evol , vol.21 , Issue.8 , pp. 1565-71
    • Vinh, L.S.1    Von Haeseler, A.2
  • 64
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • 10.1080/10635150390235520. 14530136
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. S Guindon O Gascuel, Syst Biol 2003 52 5 696 704 10.1080/10635150390235520 14530136
    • (2003) Syst Biol , vol.52 , Issue.5 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 65
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • 10.2307/2408678
    • Confidence limits on phylogenies: An approach using the bootstrap. J Felsenstein, Evolution 1985 39 783 791 10.2307/2408678
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 66
    • 12044253190 scopus 로고
    • An Empirical Test of Bootstrapping as a Method for Assessing Confidence in Phylogenetic Analysis
    • 10.2307/2992540
    • An Empirical Test of Bootstrapping as a Method for Assessing Confidence in Phylogenetic Analysis. DM Hillis JJ Bull, Syst Biol 1993 42 2 182 192 10.2307/2992540
    • (1993) Syst Biol , vol.42 , Issue.2 , pp. 182-192
    • Hillis, D.M.1    Bull, J.J.2
  • 67
    • 30744470609 scopus 로고    scopus 로고
    • Application of phylogenetic networks in evolutionary studies
    • 16221896. 10.1093/molbev/msj030
    • Application of phylogenetic networks in evolutionary studies. DH Huson D Bryant, Mol Biol Evol 2006 23 2 254 267 16221896 10.1093/molbev/msj030
    • (2006) Mol Biol Evol , vol.23 , Issue.2 , pp. 254-267
    • Huson, D.H.1    Bryant, D.2
  • 68
    • 0028685490 scopus 로고
    • Fitting a mixture model by expectation maximization to discover motifs in biopolymers
    • 7584402
    • Fitting a mixture model by expectation maximization to discover motifs in biopolymers. TL Bailey C Elkan, Proc Int Conf Intell Syst Mol Biol 1994 2 28 36 7584402
    • (1994) Proc Int Conf Intell Syst Mol Biol , vol.2 , pp. 28-36
    • Bailey, T.L.1    Elkan, C.2
  • 70
    • 1342288004 scopus 로고    scopus 로고
    • The Jalview Java alignment editor
    • 14960472. 10.1093/bioinformatics/btg430
    • The Jalview Java alignment editor. M Clamp J Cuff SM Searle GJ Barton, Bioinformatics 2004 20 3 426 427 14960472 10.1093/bioinformatics/btg430
    • (2004) Bioinformatics , vol.20 , Issue.3 , pp. 426-427
    • Clamp, M.1    Cuff, J.2    Searle, S.M.3    Barton, G.J.4
  • 71
    • 34250738083 scopus 로고    scopus 로고
    • SplitsTree4. http://www.splitstree.org
    • SplitsTree4
  • 72
    • 2442525077 scopus 로고    scopus 로고
    • HMM Logos for visualization of protein families
    • 14736340. 10.1186/1471-2105-5-7
    • HMM Logos for visualization of protein families. B Schuster-Böckler J Schultz S Rahmann, BMC Bioinformatics 2004 5 7 14736340 10.1186/1471-2105-5-7
    • (2004) BMC Bioinformatics , vol.5 , pp. 7
    • Schuster-Böckler, B.1    Schultz, J.2    Rahmann, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.