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Volumn 16, Issue 1, 2015, Pages

The genomic landscape of ribosomal peptides containing thiazole and oxazole heterocycles

Author keywords

Genome mining; Natural products; Oxazole; Post translational modification; Ribosomal peptide; Secondary metabolites; Thiazole

Indexed keywords

ANABAENASIN; BOTTROMYCIN; CORYNEAZOLISIN TYPE 1; CORYNEAZOLISIN TYPE 2; CYANOBACTIN; FAECALISIN; GALLOLYTISIN; GOADSPORIN; HAKACIN; HALOAZOLISIN; HELICOBACTIN; HETEROCYCLOANTHRACIN; MICROCIN B17; MOBILISIN; NIF11 RELATED PRECURSOR PEPTIDE; NITRILE HYDRATASE RELATED LEADER PEPTIDE; PEPTIDE; PLANTAZOLICIN; PROPIONISIN; STREPTOLYSIN S; THERMOACIDOPHISIN; THIAZOLE OXAZOLE MODIFIED MICROCIN; THIOPEPTIDE; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; YCAO DOMAIN CONTAINING PROTEIN; OXAZOLE DERIVATIVE; RIBOSOME PROTEIN; THIAZOLE DERIVATIVE;

EID: 84945232182     PISSN: None     EISSN: 14712164     Source Type: Journal    
DOI: 10.1186/s12864-015-2008-0     Document Type: Article
Times cited : (56)

References (58)
  • 1
    • 84870918230 scopus 로고    scopus 로고
    • Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature
    • Arnison PG, Bibb MJ, Bierbaum G, Bowers AA, Bugni TS, Bulaj G, et al. Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature. Nat Prod Rep. 2013;30(1):108-60
    • (2013) Nat Prod Rep , vol.30 , Issue.1 , pp. 108-160
    • Arnison, P.G.1    Bibb, M.J.2    Bierbaum, G.3    Bowers, A.A.4    Bugni, T.S.5    Bulaj, G.6
  • 2
    • 65149101910 scopus 로고    scopus 로고
    • A strain-variable bacteriocin in Bacillus anthracis and Bacillus cereus with repeated Cys-Xaa-Xaa motifs
    • Haft DH. A strain-variable bacteriocin in Bacillus anthracis and Bacillus cereus with repeated Cys-Xaa-Xaa motifs. Biol Direct. 2009;4:15
    • (2009) Biol Direct , vol.4 , pp. 15
    • Haft, D.H.1
  • 3
    • 77953742146 scopus 로고    scopus 로고
    • Catalytic promiscuity in the biosynthesis of cyclic peptide secondary metabolites in planktonic marine cyanobacteria
    • Li B, Sher D, Kelly L, Shi Y, Huang K, Knerr PJ, et al. Catalytic promiscuity in the biosynthesis of cyclic peptide secondary metabolites in planktonic marine cyanobacteria. Proc Natl Acad Sci U S A. 2010;107(23):10430-5
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.23 , pp. 10430-10435
    • Li, B.1    Sher, D.2    Kelly, L.3    Shi, Y.4    Huang, K.5    Knerr, P.J.6
  • 4
    • 84914150307 scopus 로고    scopus 로고
    • High divergence of the precursor peptides in combinatorial lanthipeptide biosynthesis
    • Zhang Q, Yang X, Wang H, van der Donk WA. High divergence of the precursor peptides in combinatorial lanthipeptide biosynthesis. ACS Chem Biol. 2014;9(11):2686-94
    • (2014) ACS Chem Biol , vol.9 , Issue.11 , pp. 2686-2694
    • Zhang, Q.1    Yang, X.2    Wang, H.3    van der Donk, W.A.4
  • 5
    • 74049115080 scopus 로고    scopus 로고
    • Follow the leader: the use of leader peptides to guide natural product biosynthesis
    • Oman TJ, van der Donk WA. Follow the leader: the use of leader peptides to guide natural product biosynthesis. Nat Chem Biol. 2010;6(1):9-18
    • (2010) Nat Chem Biol , vol.6 , Issue.1 , pp. 9-18
    • Oman, T.J.1    van der Donk, W.A.2
  • 6
    • 79851508812 scopus 로고    scopus 로고
    • Genome mining for ribosomally synthesized natural products
    • Velasquez JE, van der Donk WA. Genome mining for ribosomally synthesized natural products. Curr Opin Chem Biol. 2011;15(1):11-21
    • (2011) Curr Opin Chem Biol , vol.15 , Issue.1 , pp. 11-21
    • Velasquez, J.E.1    van der Donk, W.A.2
  • 7
    • 79957973597 scopus 로고    scopus 로고
    • Thiazole/oxazole-modified microcins: complex natural products from ribosomal templates
    • Melby JO, Nard NJ, Mitchell DA. Thiazole/oxazole-modified microcins: complex natural products from ribosomal templates. Curr Opin Chem Biol. 2011;15(3):369-78
    • (2011) Curr Opin Chem Biol , vol.15 , Issue.3 , pp. 369-378
    • Melby, J.O.1    Nard, N.J.2    Mitchell, D.A.3
  • 8
    • 84875126202 scopus 로고    scopus 로고
    • Revealing nature's synthetic potential through the study of ribosomal natural product biosynthesis
    • Dunbar KL, Mitchell DA. Revealing nature's synthetic potential through the study of ribosomal natural product biosynthesis. ACS Chem Biol. 2013;8(3):473-87
    • (2013) ACS Chem Biol , vol.8 , Issue.3 , pp. 473-487
    • Dunbar, K.L.1    Mitchell, D.A.2
  • 9
    • 84861308350 scopus 로고    scopus 로고
    • YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations
    • Dunbar KL, Melby JO, Mitchell DA. YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations. Nat Chem Biol. 2012;8(6):569-75
    • (2012) Nat Chem Biol , vol.8 , Issue.6 , pp. 569-575
    • Dunbar, K.L.1    Melby, J.O.2    Mitchell, D.A.3
  • 10
    • 84858602406 scopus 로고    scopus 로고
    • InterPro in 2011: new developments in the family and domain prediction database
    • Hunter S, Jones P, Mitchell A, Apweiler R, Attwood TK, Bateman A, et al. InterPro in 2011: new developments in the family and domain prediction database. Nucleic Acids Res. 2012;40(Database issue):D306-12
    • (2012) Nucleic Acids Res , vol.40 , Issue.DATABASE ISSUE , pp. D306-D312
    • Hunter, S.1    Jones, P.2    Mitchell, A.3    Apweiler, R.4    Attwood, T.K.5    Bateman, A.6
  • 12
    • 84876587454 scopus 로고    scopus 로고
    • Detecting sequence homology at the gene cluster level with MultiGeneBlast
    • Medema MH, Takano E, Breitling R. Detecting sequence homology at the gene cluster level with MultiGeneBlast. Mol Biol Evol. 2013;30(5):1218-23
    • (2013) Mol Biol Evol , vol.30 , Issue.5 , pp. 1218-1223
    • Medema, M.H.1    Takano, E.2    Breitling, R.3
  • 13
    • 84892704003 scopus 로고    scopus 로고
    • Insights into the evolution of lanthipeptide biosynthesis
    • Yu Y, Zhang Q, van der Donk WA. Insights into the evolution of lanthipeptide biosynthesis. Protein Sci. 2013;22(11):1478-89
    • (2013) Protein Sci , vol.22 , Issue.11 , pp. 1478-1489
    • Yu, Y.1    Zhang, Q.2    van der Donk, W.A.3
  • 14
    • 84895076771 scopus 로고    scopus 로고
    • Genomics-enabled discovery of phosphonate natural products and their biosynthetic pathways
    • Ju KS, Doroghazi JR, Metcalf WW. Genomics-enabled discovery of phosphonate natural products and their biosynthetic pathways. J Ind Microbiol Biotechnol. 2014;41(2):345-56
    • (2014) J Ind Microbiol Biotechnol , vol.41 , Issue.2 , pp. 345-356
    • Ju, K.S.1    Doroghazi, J.R.2    Metcalf, W.W.3
  • 15
    • 84883615133 scopus 로고    scopus 로고
    • Comparative genomics of actinomycetes with a focus on natural product biosynthetic genes
    • Doroghazi JR, Metcalf WW. Comparative genomics of actinomycetes with a focus on natural product biosynthetic genes. BMC Genomics. 2013;14:611
    • (2013) BMC Genomics , vol.14 , pp. 611
    • Doroghazi, J.R.1    Metcalf, W.W.2
  • 17
    • 84883261261 scopus 로고    scopus 로고
    • Structure of microcin B-like compounds produced by Pseudomonas syringae and species specificity of their antibacterial action
    • Metelev M, Serebryakova M, Ghilarov D, Zhao Y, Severinov K. Structure of microcin B-like compounds produced by Pseudomonas syringae and species specificity of their antibacterial action. J Bacteriol. 2013;195(18):4129-37
    • (2013) J Bacteriol , vol.195 , Issue.18 , pp. 4129-4137
    • Metelev, M.1    Serebryakova, M.2    Ghilarov, D.3    Zhao, Y.4    Severinov, K.5
  • 19
    • 84937855626 scopus 로고    scopus 로고
    • Identification of the minimal cytolytic unit for streptolysin S and an expansion of the toxin family
    • Molloy EM, Casjens SR, Cox CL, Maxson T, Ethridge NA, Margos G, et al. Identification of the minimal cytolytic unit for streptolysin S and an expansion of the toxin family. BMC Microbiol. 2015;15:141
    • (2015) BMC Microbiol , vol.15 , pp. 141
    • Molloy, E.M.1    Casjens, S.R.2    Cox, C.L.3    Maxson, T.4    Ethridge, N.A.5    Margos, G.6
  • 20
    • 79958720098 scopus 로고    scopus 로고
    • Expansion of type II CAAX proteases reveals evolutionary origin of gamma-secretase subunit APH-1
    • Pei J, Mitchell DA, Dixon JE, Grishin NV. Expansion of type II CAAX proteases reveals evolutionary origin of gamma-secretase subunit APH-1. J Mol Biol. 2011;410(1):18-26
    • (2011) J Mol Biol , vol.410 , Issue.1 , pp. 18-26
    • Pei, J.1    Mitchell, D.A.2    Dixon, J.E.3    Grishin, N.V.4
  • 22
    • 84873563996 scopus 로고    scopus 로고
    • Novel twin streptolysin S-like peptides encoded in the sag operon homologue of beta-hemolytic Streptococcus anginosus
    • Tabata A, Nakano K, Ohkura K, Tomoyasu T, Kikuchi K, Whiley RA, et al. Novel twin streptolysin S-like peptides encoded in the sag operon homologue of beta-hemolytic Streptococcus anginosus. J Bacteriol. 2013;195(5):1090-9
    • (2013) J Bacteriol , vol.195 , Issue.5 , pp. 1090-1099
    • Tabata, A.1    Nakano, K.2    Ohkura, K.3    Tomoyasu, T.4    Kikuchi, K.5    Whiley, R.A.6
  • 23
    • 67649730080 scopus 로고    scopus 로고
    • Structural and functional dissection of the heterocyclic peptide cytotoxin streptolysin S
    • Mitchell DA, Lee SW, Pence MA, Markley AL, Limm JD, Nizet V, et al. Structural and functional dissection of the heterocyclic peptide cytotoxin streptolysin S. J Biol Chem. 2009;284(19):13004-12
    • (2009) J Biol Chem , vol.284 , Issue.19 , pp. 13004-13012
    • Mitchell, D.A.1    Lee, S.W.2    Pence, M.A.3    Markley, A.L.4    Limm, J.D.5    Nizet, V.6
  • 24
    • 33751096434 scopus 로고    scopus 로고
    • Natural combinatorial peptide libraries in cyanobacterial symbionts of marine ascidians
    • Donia MS, Hathaway BJ, Sudek S, Haygood MG, Rosovitz MJ, Ravel J, et al. Natural combinatorial peptide libraries in cyanobacterial symbionts of marine ascidians. Nat Chem Biol. 2006;2(12):729-35
    • (2006) Nat Chem Biol , vol.2 , Issue.12 , pp. 729-735
    • Donia, M.S.1    Hathaway, B.J.2    Sudek, S.3    Haygood, M.G.4    Rosovitz, M.J.5    Ravel, J.6
  • 25
    • 84864709843 scopus 로고    scopus 로고
    • The mechanism of patellamide macrocyclization revealed by the characterization of the PatG macrocyclase domain
    • Koehnke J, Bent A, Houssen WE, Zollman D, Morawitz F, Shirran S, et al. The mechanism of patellamide macrocyclization revealed by the characterization of the PatG macrocyclase domain. Nat Struct Mol Biol. 2012;19(8):767-72
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.8 , pp. 767-772
    • Koehnke, J.1    Bent, A.2    Houssen, W.E.3    Zollman, D.4    Morawitz, F.5    Shirran, S.6
  • 26
    • 84870039217 scopus 로고    scopus 로고
    • Structures of Cyanobactin Maturation Enzymes Define a Family of Transamidating Proteases
    • Agarwal V, Pierce E, McIntosh J, Schmidt EW, Nair SK. Structures of Cyanobactin Maturation Enzymes Define a Family of Transamidating Proteases. Chem Biol. 2012;19(11):1411-22
    • (2012) Chem Biol , vol.19 , Issue.11 , pp. 1411-1422
    • Agarwal, V.1    Pierce, E.2    McIntosh, J.3    Schmidt, E.W.4    Nair, S.K.5
  • 27
    • 67749142086 scopus 로고    scopus 로고
    • Using marine natural products to discover a protease that catalyzes peptide macrocyclization of diverse substrates
    • Lee J, McIntosh J, Hathaway BJ, Schmidt EW. Using marine natural products to discover a protease that catalyzes peptide macrocyclization of diverse substrates. J Am Chem Soc. 2009;131(6):2122-4
    • (2009) J Am Chem Soc , vol.131 , Issue.6 , pp. 2122-2124
    • Lee, J.1    McIntosh, J.2    Hathaway, B.J.3    Schmidt, E.W.4
  • 28
    • 43749113148 scopus 로고    scopus 로고
    • A global assembly line for cyanobactins
    • Donia MS, Ravel J, Schmidt EW. A global assembly line for cyanobactins. Nat Chem Biol. 2008;4(6):341-3
    • (2008) Nat Chem Biol , vol.4 , Issue.6 , pp. 341-343
    • Donia, M.S.1    Ravel, J.2    Schmidt, E.W.3
  • 29
    • 64249133292 scopus 로고    scopus 로고
    • Chapter 23. Cyanobactin ribosomally synthesized peptides-a case of deep metagenome mining
    • Schmidt EW, Donia MS. Chapter 23. Cyanobactin ribosomally synthesized peptides-a case of deep metagenome mining. Methods Enzymol. 2009;458:575-96
    • (2009) Methods Enzymol , vol.458 , pp. 575-596
    • Schmidt, E.W.1    Donia, M.S.2
  • 30
  • 31
    • 79955401110 scopus 로고    scopus 로고
    • Linking chemistry and genetics in the growing cyanobactin natural products family
    • Donia MS, Schmidt EW. Linking chemistry and genetics in the growing cyanobactin natural products family. Chem Biol. 2011;18(4):508-19
    • (2011) Chem Biol , vol.18 , Issue.4 , pp. 508-519
    • Donia, M.S.1    Schmidt, E.W.2
  • 32
    • 77952511174 scopus 로고    scopus 로고
    • Expansion of ribosomally produced natural products: a nitrile hydratase-and Nif11-related precursor family
    • Haft DH, Basu MK, Mitchell DA. Expansion of ribosomally produced natural products: a nitrile hydratase-and Nif11-related precursor family. BMC Biol. 2010;8:70
    • (2010) BMC Biol , vol.8 , pp. 70
    • Haft, D.H.1    Basu, M.K.2    Mitchell, D.A.3
  • 33
    • 29244470531 scopus 로고    scopus 로고
    • Cloning and characterization of the goadsporin biosynthetic gene cluster from Streptomyces sp. TP-A0584
    • Onaka H, Nakaho M, Hayashi K, Igarashi Y, Furumai T. Cloning and characterization of the goadsporin biosynthetic gene cluster from Streptomyces sp. TP-A0584. Microbiology. 2005;151(Pt 12):3923-33
    • (2005) Microbiology , vol.151 , pp. 3923-3933
    • Onaka, H.1    Nakaho, M.2    Hayashi, K.3    Igarashi, Y.4    Furumai, T.5
  • 35
    • 84934925970 scopus 로고    scopus 로고
    • Identification of an Auxiliary Leader Peptide-Binding Protein Required for Azoline Formation in Ribosomal Natural Products
    • Dunbar KL, Tietz JI, Cox CL, Burkhart BJ, Mitchell DA. Identification of an Auxiliary Leader Peptide-Binding Protein Required for Azoline Formation in Ribosomal Natural Products. J Am Chem Soc. 2015;137(24):7672-7
    • (2015) J Am Chem Soc , vol.137 , Issue.24 , pp. 7672-7677
    • Dunbar, K.L.1    Tietz, J.I.2    Cox, C.L.3    Burkhart, B.J.4    Mitchell, D.A.5
  • 37
    • 78149447364 scopus 로고    scopus 로고
    • Isolation and characterization of the gene cluster for biosynthesis of the thiopeptide antibiotic TP-1161
    • Engelhardt K, Degnes KF, Zotchev SB. Isolation and characterization of the gene cluster for biosynthesis of the thiopeptide antibiotic TP-1161. Appl Environ Microbiol. 2010;76(21):7093-101
    • (2010) Appl Environ Microbiol , vol.76 , Issue.21 , pp. 7093-7101
    • Engelhardt, K.1    Degnes, K.F.2    Zotchev, S.B.3
  • 38
    • 84878120464 scopus 로고    scopus 로고
    • The posttranslational modification cascade to the thiopeptide berninamycin generates linear forms and altered macrocyclic scaffolds
    • Malcolmson SJ, Young TS, Ruby JG, Skewes-Cox P, Walsh CT. The posttranslational modification cascade to the thiopeptide berninamycin generates linear forms and altered macrocyclic scaffolds. Proc Natl Acad Sci U S A. 2013;110(21):8483-8
    • (2013) Proc Natl Acad Sci U S A , vol.110 , Issue.21 , pp. 8483-8488
    • Malcolmson, S.J.1    Young, T.S.2    Ruby, J.G.3    Skewes-Cox, P.4    Walsh, C.T.5
  • 39
    • 77956244429 scopus 로고    scopus 로고
    • Genetic interception and structural characterization of thiopeptide cyclization precursors from Bacillus cereus
    • Bowers AA, Walsh CT, Acker MG. Genetic interception and structural characterization of thiopeptide cyclization precursors from Bacillus cereus. J Am Chem Soc. 2010;132(35):12182-4
    • (2010) J Am Chem Soc , vol.132 , Issue.35 , pp. 12182-12184
    • Bowers, A.A.1    Walsh, C.T.2    Acker, M.G.3
  • 40
    • 84925252380 scopus 로고    scopus 로고
    • Chemoenzymatic Synthesis of Thiazolyl Peptide Natural Products Featuring an Enzyme-Catalyzed Formal [4 + 2] Cycloaddition
    • Wever WJ, Bogart JW, Baccile JA, Chan A, Schroeder FC, Bowers AA. Chemoenzymatic Synthesis of Thiazolyl Peptide Natural Products Featuring an Enzyme-Catalyzed Formal [4 + 2] Cycloaddition. J Am Chem Soc. 2015;137(10):3494-7
    • (2015) J Am Chem Soc , vol.137 , Issue.10 , pp. 3494-3497
    • Wever, W.J.1    Bogart, J.W.2    Baccile, J.A.3    Chan, A.4    Schroeder, F.C.5    Bowers, A.A.6
  • 41
    • 84858656036 scopus 로고    scopus 로고
    • Structure determination and interception of biosynthetic intermediates for the plantazolicin class of highly discriminating antibiotics
    • Molohon KJ, Melby JO, Lee J, Evans BS, Dunbar KL, Bumpus SB, et al. Structure determination and interception of biosynthetic intermediates for the plantazolicin class of highly discriminating antibiotics. ACS Chem Biol. 2011;6(12):1307-13
    • (2011) ACS Chem Biol , vol.6 , Issue.12 , pp. 1307-1313
    • Molohon, K.J.1    Melby, J.O.2    Lee, J.3    Evans, B.S.4    Dunbar, K.L.5    Bumpus, S.B.6
  • 42
    • 78650083538 scopus 로고    scopus 로고
    • Plantazolicin, a novel microcin B17/streptolysin S-like natural product from Bacillus amyloliquefaciens FZB42
    • Scholz R, Molohon KJ, Nachtigall J, Vater J, Markley AL, Sussmuth RD, et al. Plantazolicin, a novel microcin B17/streptolysin S-like natural product from Bacillus amyloliquefaciens FZB42. J Bacteriol. 2011;193(1):215-24
    • (2011) J Bacteriol , vol.193 , Issue.1 , pp. 215-224
    • Scholz, R.1    Molohon, K.J.2    Nachtigall, J.3    Vater, J.4    Markley, A.L.5    Sussmuth, R.D.6
  • 43
    • 84881397081 scopus 로고    scopus 로고
    • Structural and functional insight into an unexpectedly selective N-methyltransferase involved in plantazolicin biosynthesis
    • Lee J, Hao Y, Blair PM, Melby JO, Agarwal V, Burkhart BJ, et al. Structural and functional insight into an unexpectedly selective N-methyltransferase involved in plantazolicin biosynthesis. Proc Natl Acad Sci U S A. 2013;110(32):12954-9
    • (2013) Proc Natl Acad Sci U S A , vol.110 , Issue.32 , pp. 12954-12959
    • Lee, J.1    Hao, Y.2    Blair, P.M.3    Melby, J.O.4    Agarwal, V.5    Burkhart, B.J.6
  • 44
    • 84929576090 scopus 로고    scopus 로고
    • Insights into Methyltransferase Specificity and Bioactivity of Derivatives of the Antibiotic Plantazolicin
    • Hao Y, Blair PM, Sharma A, Mitchell DA, Nair SK. Insights into Methyltransferase Specificity and Bioactivity of Derivatives of the Antibiotic Plantazolicin. ACS Chem Biol. 2015;10(5):1209-16
    • (2015) ACS Chem Biol , vol.10 , Issue.5 , pp. 1209-1216
    • Hao, Y.1    Blair, P.M.2    Sharma, A.3    Mitchell, D.A.4    Nair, S.K.5
  • 45
    • 84886404774 scopus 로고    scopus 로고
    • Arg-Thz is a minimal substrate for the N(alpha), N(alpha)-arginyl methyltransferase involved in the biosynthesis of plantazolicin
    • Piwowarska NA, Banala S, Overkleeft HS, Sussmuth RD. Arg-Thz is a minimal substrate for the N(alpha), N(alpha)-arginyl methyltransferase involved in the biosynthesis of plantazolicin. Chem Commun (Camb). 2013;49(91):10703-5
    • (2013) Chem Commun (Camb) , vol.49 , Issue.91 , pp. 10703-10705
    • Piwowarska, N.A.1    Banala, S.2    Overkleeft, H.S.3    Sussmuth, R.D.4
  • 46
    • 84858665499 scopus 로고    scopus 로고
    • Selectivity, directionality, and promiscuity in peptide processing from a Bacillus sp. Al Hakam cyclodehydratase
    • Melby JO, Dunbar KL, Trinh NQ, Mitchell DA. Selectivity, directionality, and promiscuity in peptide processing from a Bacillus sp. Al Hakam cyclodehydratase. J Am Chem Soc. 2012;134(11):5309-16
    • (2012) J Am Chem Soc , vol.134 , Issue.11 , pp. 5309-5316
    • Melby, J.O.1    Dunbar, K.L.2    Trinh, N.Q.3    Mitchell, D.A.4
  • 47
    • 84937438220 scopus 로고    scopus 로고
    • A prevalent peptidebinding domain guides ribosomal natural product biosynthesis
    • Burkhart BJ, Hudson GA, Dunbar KL, Mitchell DA. A prevalent peptidebinding domain guides ribosomal natural product biosynthesis. Nat Chem Biol. 2015;11(8):564-70
    • (2015) Nat Chem Biol , vol.11 , Issue.8 , pp. 564-570
    • Burkhart, B.J.1    Hudson, G.A.2    Dunbar, K.L.3    Mitchell, D.A.4
  • 48
    • 0030015322 scopus 로고    scopus 로고
    • A newly discovered gene, tfuA, involved in the production of the ribosomally synthesized peptide antibiotic trifolitoxin
    • Breil B, Borneman J, Triplett EW. A newly discovered gene, tfuA, involved in the production of the ribosomally synthesized peptide antibiotic trifolitoxin. J Bacteriol. 1996;178(14):4150-6
    • (1996) J Bacteriol , vol.178 , Issue.14 , pp. 4150-4156
    • Breil, B.1    Borneman, J.2    Triplett, E.W.3
  • 50
    • 84883353135 scopus 로고    scopus 로고
    • antiSMASH 2.0-a versatile platform for genome mining of secondary metabolite producers
    • Blin K, Medema MH, Kazempour D, Fischbach MA, Breitling R, Takano E, et al. antiSMASH 2.0-a versatile platform for genome mining of secondary metabolite producers. Nucleic Acids Res. 2013;41(Web Server issue):W204-12
    • (2013) Nucleic Acids Res , vol.41 , Issue.WEB SERVER ISSUE , pp. W204-W212
    • Blin, K.1    Medema, M.H.2    Kazempour, D.3    Fischbach, M.A.4    Breitling, R.5    Takano, E.6
  • 51
    • 79959920872 scopus 로고    scopus 로고
    • antiSMASH: rapid identification, annotation and analysis of secondary metabolite biosynthesis gene clusters in bacterial and fungal genome sequences
    • Medema MH, Blin K, Cimermancic P, de Jager V, Zakrzewski P, Fischbach MA, et al. antiSMASH: rapid identification, annotation and analysis of secondary metabolite biosynthesis gene clusters in bacterial and fungal genome sequences. Nucleic Acids Res. 2011;39(Web Server issue): W339-46
    • (2011) Nucleic Acids Res , vol.39 , Issue.WEB SERVER ISSUE , pp. W339-W346
    • Medema, M.H.1    Blin, K.2    Cimermancic, P.3    de Jager, V.4    Zakrzewski, P.5    Fischbach, M.A.6
  • 52
    • 79959931985 scopus 로고    scopus 로고
    • HMMER web server: interactive sequence similarity searching
    • Finn RD, Clements J, Eddy SR. HMMER web server: interactive sequence similarity searching. Nucleic Acids Res. 2011;39(Web Server issue):W29-37
    • (2011) Nucleic Acids Res , vol.39 , Issue.WEB SERVER ISSUE , pp. W29-W37
    • Finn, R.D.1    Clements, J.2    Eddy, S.R.3
  • 53
    • 84929376894 scopus 로고    scopus 로고
    • Enzyme Function Initiative-Enzyme Similarity Tool (EFI-EST): A web tool for generating protein sequence similarity networks
    • Gerlt JA, Bouvier JT, Davidson DB, Imker HJ, Sadkhin B, Slater DR, et al. Enzyme Function Initiative-Enzyme Similarity Tool (EFI-EST): A web tool for generating protein sequence similarity networks. Biochim Biophys Acta. 2015;1854(8):1019-37
    • (2015) Biochim Biophys Acta , vol.1854 , Issue.8 , pp. 1019-1037
    • Gerlt, J.A.1    Bouvier, J.T.2    Davidson, D.B.3    Imker, H.J.4    Sadkhin, B.5    Slater, D.R.6
  • 54
    • 79952202448 scopus 로고    scopus 로고
    • Cytoscape: software for visualization and analysis of biological networks
    • Kohl M, Wiese S, Warscheid B. Cytoscape: software for visualization and analysis of biological networks. Methods Mol Biol. 2011;696:291-303
    • (2011) Methods Mol Biol , vol.696 , pp. 291-303
    • Kohl, M.1    Wiese, S.2    Warscheid, B.3
  • 55
    • 37549027613 scopus 로고    scopus 로고
    • SILVA: a comprehensive online resource for quality checked and aligned ribosomal RNA sequence data compatible with ARB
    • Pruesse E, Quast C, Knittel K, Fuchs BM, Ludwig W, Peplies J, et al. SILVA: a comprehensive online resource for quality checked and aligned ribosomal RNA sequence data compatible with ARB. Nucleic Acids Res. 2007;35(21):7188-96
    • (2007) Nucleic Acids Res , vol.35 , Issue.21 , pp. 7188-7196
    • Pruesse, E.1    Quast, C.2    Knittel, K.3    Fuchs, B.M.4    Ludwig, W.5    Peplies, J.6
  • 56
  • 57
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: a multiple sequence alignment method with reduced time and space complexity
    • Edgar RC. MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinform. 2004;5:113
    • (2004) BMC Bioinform , vol.5 , pp. 113
    • Edgar, R.C.1
  • 58
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 2004;32(5):1792-7
    • (2004) Nucleic Acids Res , vol.32 , Issue.5 , pp. 1792-1797
    • Edgar, R.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.