메뉴 건너뛰기




Volumn 8, Issue 3, 2013, Pages 473-487

Erratum: Revealing nature's synthetic potential through the study of ribosomal natural product biosynthesis (ACS Chemical Biology (2013) 8 (473-487) DOI: 10.1021/cb3005325);Revealing nature's synthetic potential through the study of ribosomal natural product biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

NATURAL PRODUCT; BIOLOGICAL PRODUCT; PEPTIDE;

EID: 84875126202     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb4002359     Document Type: Erratum
Times cited : (32)

References (117)
  • 1
    • 52049109838 scopus 로고    scopus 로고
    • Natural products in drug discovery
    • Harvey, A. L. (2008) Natural products in drug discovery Drug Discovery Today 13, 894-901
    • (2008) Drug Discovery Today , vol.13 , pp. 894-901
    • Harvey, A.L.1
  • 2
    • 84858308226 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the 30 years from 1981 to 2010
    • Newman, D. J. and Cragg, G. M. (2012) Natural products as sources of new drugs over the 30 years from 1981 to 2010 J. Nat. Prod. 75, 311-335
    • (2012) J. Nat. Prod. , vol.75 , pp. 311-335
    • Newman, D.J.1    Cragg, G.M.2
  • 3
    • 33750464876 scopus 로고    scopus 로고
    • Small molecule natural products in the discovery of therapeutic agents: The synthesis connection
    • Wilson, R. M. and Danishefsky, S. J. (2006) Small molecule natural products in the discovery of therapeutic agents: the synthesis connection J. Org. Chem. 71, 8329-8351
    • (2006) J. Org. Chem. , vol.71 , pp. 8329-8351
    • Wilson, R.M.1    Danishefsky, S.J.2
  • 4
    • 81355123306 scopus 로고    scopus 로고
    • Lessons and revelations from biomimetic syntheses
    • Razzak, M. and De Brabander, J. K. (2011) Lessons and revelations from biomimetic syntheses Nat. Chem. Biol. 7, 865-875
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 865-875
    • Razzak, M.1    De Brabander, J.K.2
  • 5
    • 79959448080 scopus 로고    scopus 로고
    • Antibiotics as probes of biological complexity
    • Falconer, S. B., Czarny, T. L., and Brown, E. D. (2011) Antibiotics as probes of biological complexity Nat. Chem. Biol. 7, 415-423
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 415-423
    • Falconer, S.B.1    Czarny, T.L.2    Brown, E.D.3
  • 8
    • 0025776523 scopus 로고
    • Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast
    • Heitman, J., Movva, N. R., and Hall, M. N. (1991) Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast Science 253, 905-909
    • (1991) Science , vol.253 , pp. 905-909
    • Heitman, J.1    Movva, N.R.2    Hall, M.N.3
  • 9
    • 0037133038 scopus 로고    scopus 로고
    • Direct long-term observation of kinesin processivity at low load
    • Yajima, J., Alonso, M. C., Cross, R. A., and Toyoshima, Y. Y. (2002) Direct long-term observation of kinesin processivity at low load Curr. Biol. 12, 301-306
    • (2002) Curr. Biol. , vol.12 , pp. 301-306
    • Yajima, J.1    Alonso, M.C.2    Cross, R.A.3    Toyoshima, Y.Y.4
  • 10
    • 67649210440 scopus 로고    scopus 로고
    • Chemical Tools for Inhibiting Glycosylation
    • 2 nd ed. pp, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • Esko, J. D. and Bertozzi, C. R. (2009) Chemical Tools for Inhibiting Glycosylation, in Essentials of Glycobiology, 2 nd ed., pp 705-719, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2009) Essentials of Glycobiology , pp. 705-719
    • Esko, J.D.1    Bertozzi, C.R.2
  • 11
    • 33745019553 scopus 로고    scopus 로고
    • Marcel Faber Roundtable: Is our antibiotic pipeline unproductive because of starvation, constipation or lack of inspiration?
    • Baltz, R. H. (2006) Marcel Faber Roundtable: is our antibiotic pipeline unproductive because of starvation, constipation or lack of inspiration? J. Ind. Microbiol. Biotechnol. 33, 507-513
    • (2006) J. Ind. Microbiol. Biotechnol. , vol.33 , pp. 507-513
    • Baltz, R.H.1
  • 13
    • 79851508812 scopus 로고    scopus 로고
    • Genome mining for ribosomally synthesized natural products
    • Velasquez, J. E. and van der Donk, W. A. (2011) Genome mining for ribosomally synthesized natural products Curr. Opin. Chem. Biol. 15, 11-21
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 11-21
    • Velasquez, J.E.1    Van Der Donk, W.A.2
  • 15
    • 79955401110 scopus 로고    scopus 로고
    • Linking chemistry and genetics in the growing cyanobactin natural products family
    • Donia, M. S. and Schmidt, E. W. (2011) Linking chemistry and genetics in the growing cyanobactin natural products family Chem. Biol. 18, 508-519
    • (2011) Chem. Biol. , vol.18 , pp. 508-519
    • Donia, M.S.1    Schmidt, E.W.2
  • 16
    • 43749113148 scopus 로고    scopus 로고
    • A global assembly line for cyanobactins
    • Donia, M. S., Ravel, J., and Schmidt, E. W. (2008) A global assembly line for cyanobactins Nat. Chem. Biol. 4, 341-343
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 341-343
    • Donia, M.S.1    Ravel, J.2    Schmidt, E.W.3
  • 18
    • 74049115080 scopus 로고    scopus 로고
    • Follow the leader: The use of leader peptides to guide natural product biosynthesis
    • Oman, T. J. and van der Donk, W. A. (2010) Follow the leader: the use of leader peptides to guide natural product biosynthesis Nat. Chem. Biol. 6, 9-18
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 9-18
    • Oman, T.J.1    Van Der Donk, W.A.2
  • 20
    • 77952511174 scopus 로고    scopus 로고
    • Expansion of ribosomally produced natural products: A nitrile hydratase- and Nif11-related precursor family
    • Haft, D. H., Basu, M. K., and Mitchell, D. A. (2010) Expansion of ribosomally produced natural products: a nitrile hydratase- and Nif11-related precursor family BMC Biol. 8, 70
    • (2010) BMC Biol. , vol.8 , pp. 70
    • Haft, D.H.1    Basu, M.K.2    Mitchell, D.A.3
  • 21
    • 79957973597 scopus 로고    scopus 로고
    • Thiazole/oxazole-modified microcins: Complex natural products from ribosomal templates
    • Melby, J. O., Nard, N. J., and Mitchell, D. A. (2011) Thiazole/oxazole-modified microcins: complex natural products from ribosomal templates Curr. Opin. Chem. Biol. 15, 369-378
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 369-378
    • Melby, J.O.1    Nard, N.J.2    Mitchell, D.A.3
  • 23
    • 84858665499 scopus 로고    scopus 로고
    • Selectivity, directionality, and promiscuity in peptide processing from a Bacillus sp. Al Hakam cyclodehydratase
    • Melby, J. O., Dunbar, K. L., Trinh, N. Q., and Mitchell, D. A. (2012) Selectivity, directionality, and promiscuity in peptide processing from a Bacillus sp. Al Hakam cyclodehydratase J. Am. Chem. Soc. 134, 5309-5316
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 5309-5316
    • Melby, J.O.1    Dunbar, K.L.2    Trinh, N.Q.3    Mitchell, D.A.4
  • 24
    • 78649556678 scopus 로고    scopus 로고
    • The dawning of a 'Golden era' in lantibiotic bioengineering
    • Field, D., Hill, C., Cotter, P. D., and Ross, R. P. (2010) The dawning of a 'Golden era' in lantibiotic bioengineering Mol. Microbiol. 78, 1077-1087
    • (2010) Mol. Microbiol. , vol.78 , pp. 1077-1087
    • Field, D.1    Hill, C.2    Cotter, P.D.3    Ross, R.P.4
  • 25
    • 84864344468 scopus 로고    scopus 로고
    • Biochemical and biosynthetic preparation of natural product-like cyclic peptide libraries
    • Bowers, A. A. (2012) Biochemical and biosynthetic preparation of natural product-like cyclic peptide libraries MedChemComm 3, 905-915
    • (2012) MedChemComm , vol.3 , pp. 905-915
    • Bowers, A.A.1
  • 27
    • 0029923954 scopus 로고    scopus 로고
    • From peptide precursors to oxazole and thiazole-containing peptide antibiotics: Microcin B17 synthase
    • Li, Y. M., Milne, J. C., Madison, L. L., Kolter, R., and Walsh, C. T. (1996) From peptide precursors to oxazole and thiazole-containing peptide antibiotics: microcin B17 synthase Science 274, 1188-1193
    • (1996) Science , vol.274 , pp. 1188-1193
    • Li, Y.M.1    Milne, J.C.2    Madison, L.L.3    Kolter, R.4    Walsh, C.T.5
  • 29
    • 18844410256 scopus 로고    scopus 로고
    • Patellamide A and C biosynthesis by a microcin-like pathway in Prochloron didemni, the cyanobacterial symbiont of Lissoclinum patella
    • Schmidt, E. W., Nelson, J. T., Rasko, D. A., Sudek, S., Eisen, J. A., Haygood, M. G., and Ravel, J. (2005) Patellamide A and C biosynthesis by a microcin-like pathway in Prochloron didemni, the cyanobacterial symbiont of Lissoclinum patella Proc. Natl. Acad. Sci. U.S.A. 102, 7315-7320
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 7315-7320
    • Schmidt, E.W.1    Nelson, J.T.2    Rasko, D.A.3    Sudek, S.4    Eisen, J.A.5    Haygood, M.G.6    Ravel, J.7
  • 30
    • 0039130745 scopus 로고    scopus 로고
    • Cofactor requirements and reconstitution of Microcin B17 synthetase: A multienzyme complex that catalyzes the formation of oxazoles and thiazoles in the antibiotic Microcin B17
    • Milne, J. C., Roy, R. S., Eliot, A. C., Kelleher, N. L., Wokhlu, A., Nickels, B., and Walsh, C. T. (1999) Cofactor requirements and reconstitution of Microcin B17 synthetase: A multienzyme complex that catalyzes the formation of oxazoles and thiazoles in the antibiotic Microcin B17 Biochemistry 38, 4768-4781
    • (1999) Biochemistry , vol.38 , pp. 4768-4781
    • Milne, J.C.1    Roy, R.S.2    Eliot, A.C.3    Kelleher, N.L.4    Wokhlu, A.5    Nickels, B.6    Walsh, C.T.7
  • 31
    • 0033598801 scopus 로고    scopus 로고
    • Posttranslational heterocyclization of cysteine and serine residues in the antibiotic Microcin B17: Distributivity and directionality
    • Kelleher, N. L., Hendrickson, C. L., and Walsh, C. T. (1999) Posttranslational heterocyclization of cysteine and serine residues in the antibiotic Microcin B17: Distributivity and directionality Biochemistry 38, 15623-15630
    • (1999) Biochemistry , vol.38 , pp. 15623-15630
    • Kelleher, N.L.1    Hendrickson, C.L.2    Walsh, C.T.3
  • 32
    • 0032054255 scopus 로고    scopus 로고
    • Role of the microcin B17 propeptide in substrate recognition: Solution structure and mutational analysis of McbA1-26
    • Roy, R. S., Kim, S., Baleja, J. D., and Walsh, C. T. (1998) Role of the microcin B17 propeptide in substrate recognition: solution structure and mutational analysis of McbA1-26 Chem. Biol. 5, 217-228
    • (1998) Chem. Biol. , vol.5 , pp. 217-228
    • Roy, R.S.1    Kim, S.2    Baleja, J.D.3    Walsh, C.T.4
  • 33
    • 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, B. J., and Schmidt, E. W. (2009) Using marine natural products to discover a protease that catalyzes peptide macrocyclization of diverse substrates J. Am. Chem. Soc. 131, 2122-2124
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2122-2124
    • Lee, J.1    McIntosh, J.2    Hathaway, B.J.3    Schmidt, E.W.4
  • 34
    • 79951845926 scopus 로고    scopus 로고
    • Radical-mediated enzymatic carbon chain fragmentation-recombination
    • Zhang, Q., Li, Y., Chen, D., Yu, Y., Duan, L., Shen, B., and Liu, W. (2011) Radical-mediated enzymatic carbon chain fragmentation-recombination Nat. Chem. Biol. 7, 154-160
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 154-160
    • Zhang, Q.1    Li, Y.2    Chen, D.3    Yu, Y.4    Duan, L.5    Shen, B.6    Liu, W.7
  • 35
    • 80052087588 scopus 로고    scopus 로고
    • Enzymatic basis of ribosomal peptide prenylation in cyanobacteria
    • McIntosh, J. A., Donia, M. S., Nair, S. K., and Schmidt, E. W. (2011) Enzymatic basis of ribosomal peptide prenylation in cyanobacteria J. Am. Chem. Soc. 133, 13698-13705
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 13698-13705
    • McIntosh, J.A.1    Donia, M.S.2    Nair, S.K.3    Schmidt, E.W.4
  • 36
    • 79952262668 scopus 로고    scopus 로고
    • Thiostrepton maturation involving a deesterification-amidation way to process the C-terminally methylated peptide backbone
    • Liao, R. and Liu, W. (2011) Thiostrepton maturation involving a deesterification-amidation way to process the C-terminally methylated peptide backbone J. Am. Chem. Soc. 133, 2852-2855
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2852-2855
    • Liao, R.1    Liu, W.2
  • 37
    • 78649262383 scopus 로고    scopus 로고
    • NosA catalyzing carboxyl-terminal amide formation in nosiheptide maturation via an enamine dealkylation on the serine-extended precursor peptide
    • Yu, Y., Guo, H., Zhang, Q., Duan, L., Ding, Y., Liao, R., Lei, C., Shen, B., and Liu, W. (2010) NosA catalyzing carboxyl-terminal amide formation in nosiheptide maturation via an enamine dealkylation on the serine-extended precursor peptide J. Am. Chem. Soc. 132, 16324-16326
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 16324-16326
    • Yu, Y.1    Guo, H.2    Zhang, Q.3    Duan, L.4    Ding, Y.5    Liao, R.6    Lei, C.7    Shen, B.8    Liu, W.9
  • 38
    • 84861308350 scopus 로고    scopus 로고
    • YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations
    • Dunbar, K. L., Melby, J. O., and Mitchell, D. A. (2012) YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations Nat. Chem. Biol. 8, 569-575
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 569-575
    • Dunbar, K.L.1    Melby, J.O.2    Mitchell, D.A.3
  • 39
    • 54449093009 scopus 로고    scopus 로고
    • Interaction studies and alanine scanning analysis of a semi-synthetic split intein reveal thiazoline ring formation from an intermediate of the protein splicing reaction
    • Ludwig, C., Schwarzer, D., and Mootz, H. D. (2008) Interaction studies and alanine scanning analysis of a semi-synthetic split intein reveal thiazoline ring formation from an intermediate of the protein splicing reaction J. Biol. Chem. 283, 25264-25272
    • (2008) J. Biol. Chem. , vol.283 , pp. 25264-25272
    • Ludwig, C.1    Schwarzer, D.2    Mootz, H.D.3
  • 40
    • 79960686713 scopus 로고    scopus 로고
    • A major portion of DNA gyrase inhibitor microcin B17 undergoes an N,O-peptidyl shift during synthesis
    • Ghilarov, D., Serebryakova, M., Shkundina, I., and Severinov, K. (2011) A major portion of DNA gyrase inhibitor microcin B17 undergoes an N,O-peptidyl shift during synthesis J. Biol. Chem. 286, 26308-26318
    • (2011) J. Biol. Chem. , vol.286 , pp. 26308-26318
    • Ghilarov, D.1    Serebryakova, M.2    Shkundina, I.3    Severinov, K.4
  • 41
    • 0031244525 scopus 로고    scopus 로고
    • Protein splicing and autoproteolysis mechanisms
    • Perler, F. B., Xu, M. Q., and Paulus, H. (1997) Protein splicing and autoproteolysis mechanisms Curr. Opin. Chem. Biol. 1, 292-299
    • (1997) Curr. Opin. Chem. Biol. , vol.1 , pp. 292-299
    • Perler, F.B.1    Xu, M.Q.2    Paulus, H.3
  • 42
    • 57349119221 scopus 로고    scopus 로고
    • Structural biology of the purine biosynthetic pathway
    • Zhang, Y., Morar, M., and Ealick, S. E. (2008) Structural biology of the purine biosynthetic pathway Cell. Mol. Life Sci. 65, 3699-3724
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3699-3724
    • Zhang, Y.1    Morar, M.2    Ealick, S.E.3
  • 43
    • 84864447599 scopus 로고    scopus 로고
    • Structure and biosynthesis of the unusual polyketide alkaloid coelimycin P1, a metabolic product of the cpk gene cluster of Streptomyces coelicolor M145
    • Gomez-Escribano, J. P., Song, L., Bibb, M. J., and Challis, G. L. (2012) Structure and biosynthesis of the unusual polyketide alkaloid coelimycin P1, a metabolic product of the cpk gene cluster of Streptomyces coelicolor M145 Chem. Sci. 3, 2716-2720
    • (2012) Chem. Sci. , vol.3 , pp. 2716-2720
    • Gomez-Escribano, J.P.1    Song, L.2    Bibb, M.J.3    Challis, G.L.4
  • 44
    • 84868118472 scopus 로고    scopus 로고
    • Identification and characterisation of the gene cluster for the anti-MRSA antibiotic bottromycin: Expanding the biosynthetic diversity of ribosomal peptides
    • Crone, W. J. K., Leeper, F. J., and Truman, A. W. (2012) Identification and characterisation of the gene cluster for the anti-MRSA antibiotic bottromycin: expanding the biosynthetic diversity of ribosomal peptides Chem. Sci. 3, 3516-3521
    • (2012) Chem. Sci. , vol.3 , pp. 3516-3521
    • Crone, W.J.K.1    Leeper, F.J.2    Truman, A.W.3
  • 46
    • 84868104639 scopus 로고    scopus 로고
    • Synthetic biotechnology to study and engineer ribosomal bottromycin biosynthesis
    • Huo, L., Rachid, S., Stradler, M., Wenzel, S. C., and Müller, R. (2012) Synthetic biotechnology to study and engineer ribosomal bottromycin biosynthesis Chem. Biol. 19, 1278-1287
    • (2012) Chem. Biol. , vol.19 , pp. 1278-1287
    • Huo, L.1    Rachid, S.2    Stradler, M.3    Wenzel, S.C.4    Müller, R.5
  • 47
    • 84861511784 scopus 로고    scopus 로고
    • Thiamin biosynthesis: Still yielding fascinating biological chemistry
    • Begley, T. P., Ealick, S. E., and McLafferty, F. W. (2012) Thiamin biosynthesis: still yielding fascinating biological chemistry Biochem. Soc. Trans. 40, 555-560
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 555-560
    • Begley, T.P.1    Ealick, S.E.2    McLafferty, F.W.3
  • 49
    • 0036295033 scopus 로고    scopus 로고
    • The structure of VibH represents nonribosomal peptide synthetase condensation, cyclization and epimerization domains
    • Keating, T. A., Marshall, C. G., Walsh, C. T., and Keating, A. E. (2002) The structure of VibH represents nonribosomal peptide synthetase condensation, cyclization and epimerization domains Nat. Struct. Biol. 9, 522-526
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 522-526
    • Keating, T.A.1    Marshall, C.G.2    Walsh, C.T.3    Keating, A.E.4
  • 50
    • 67649604461 scopus 로고    scopus 로고
    • Ribosomal peptide natural products: Bridging the ribosomal and nonribosomal worlds
    • McIntosh, J. A., Donia, M. S., and Schmidt, E. W. (2009) Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds Nat. Prod. Rep. 26, 537-559
    • (2009) Nat. Prod. Rep. , vol.26 , pp. 537-559
    • McIntosh, J.A.1    Donia, M.S.2    Schmidt, E.W.3
  • 51
    • 0021945764 scopus 로고
    • Structure and mode of action of microcin 7, an antibacterial peptide produced by Escherichia coli
    • Garcia-Bustos, J. F., Pezzi, N., and Mendez, E. (1985) Structure and mode of action of microcin 7, an antibacterial peptide produced by Escherichia coli Antimicrob. Agents Chemother. 27, 791-797
    • (1985) Antimicrob. Agents Chemother. , vol.27 , pp. 791-797
    • Garcia-Bustos, J.F.1    Pezzi, N.2    Mendez, E.3
  • 54
    • 0028868830 scopus 로고
    • Structure and organization of plasmid genes required to produce the translation inhibitor microcin C7
    • Gonzalez-Pastor, J. E., San Millan, J. L., Castilla, M. A., and Moreno, F. (1995) Structure and organization of plasmid genes required to produce the translation inhibitor microcin C7 J. Bacteriol. 177, 7131-7140
    • (1995) J. Bacteriol. , vol.177 , pp. 7131-7140
    • Gonzalez-Pastor, J.E.1    San Millan, J.L.2    Castilla, M.A.3    Moreno, F.4
  • 55
    • 36549033355 scopus 로고    scopus 로고
    • The Escherichia coli Yej transporter is required for the uptake of translation inhibitor microcin C
    • Novikova, M., Metlitskaya, A., Datsenko, K., Kazakov, T., Kazakov, A., Wanner, B., and Severinov, K. (2007) The Escherichia coli Yej transporter is required for the uptake of translation inhibitor microcin C J. Bacteriol. 189, 8361-8365
    • (2007) J. Bacteriol. , vol.189 , pp. 8361-8365
    • Novikova, M.1    Metlitskaya, A.2    Datsenko, K.3    Kazakov, T.4    Kazakov, A.5    Wanner, B.6    Severinov, K.7
  • 57
    • 41449111223 scopus 로고    scopus 로고
    • Maturation of an Escherichia coli ribosomal peptide antibiotic by ATP-consuming N-P bond formation in microcin C7
    • Roush, R. F., Nolan, E. M., Lohr, F., and Walsh, C. T. (2008) Maturation of an Escherichia coli ribosomal peptide antibiotic by ATP-consuming N-P bond formation in microcin C7 J. Am. Chem. Soc. 130, 3603-3609
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 3603-3609
    • Roush, R.F.1    Nolan, E.M.2    Lohr, F.3    Walsh, C.T.4
  • 58
    • 67650450156 scopus 로고    scopus 로고
    • How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic
    • Regni, C. A., Roush, R. F., Miller, D. J., Nourse, A., Walsh, C. T., and Schulman, B. A. (2009) How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic EMBO J. 28, 1953-1964
    • (2009) EMBO J. , vol.28 , pp. 1953-1964
    • Regni, C.A.1    Roush, R.F.2    Miller, D.J.3    Nourse, A.4    Walsh, C.T.5    Schulman, B.A.6
  • 61
    • 84861649020 scopus 로고    scopus 로고
    • Discovery, biosynthesis, and engineering of lantipeptides
    • Knerr, P. J. and van der Donk, W. A. (2012) Discovery, biosynthesis, and engineering of lantipeptides Annu. Rev. Biochem. 81, 479-505
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 479-505
    • Knerr, P.J.1    Van Der Donk, W.A.2
  • 63
    • 77953528770 scopus 로고    scopus 로고
    • In vitro biosynthesis of the prepeptide of type-III lantibiotic labyrinthopeptin A2 including formation of a C-C bond as a post-translational modification
    • Muller, W. M., Schmiederer, T., Ensle, P., and Sussmuth, R. D. (2010) In vitro biosynthesis of the prepeptide of type-III lantibiotic labyrinthopeptin A2 including formation of a C-C bond as a post-translational modification Angew. Chem., Int. Ed. 49, 2436-2440
    • (2010) Angew. Chem., Int. Ed. , vol.49 , pp. 2436-2440
    • Muller, W.M.1    Schmiederer, T.2    Ensle, P.3    Sussmuth, R.D.4
  • 64
    • 59649107063 scopus 로고    scopus 로고
    • Widespread occurrence and lateral transfer of the cyanobactin biosynthesis gene cluster in cyanobacteria
    • Leikoski, N., Fewer, D. P., and Sivonen, K. (2009) Widespread occurrence and lateral transfer of the cyanobactin biosynthesis gene cluster in cyanobacteria Appl. Environ. Microbiol. 75, 853-857
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 853-857
    • Leikoski, N.1    Fewer, D.P.2    Sivonen, K.3
  • 66
    • 77950269149 scopus 로고    scopus 로고
    • Insights into heterocyclization from two highly similar enzymes
    • McIntosh, J. A., Donia, M. S., and Schmidt, E. W. (2010) Insights into heterocyclization from two highly similar enzymes J. Am. Chem. Soc. 132, 4089-4091
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 4089-4091
    • McIntosh, J.A.1    Donia, M.S.2    Schmidt, E.W.3
  • 67
    • 78149276862 scopus 로고    scopus 로고
    • Circular logic: Nonribosomal peptide-like macrocyclization with a ribosomal peptide catalyst
    • McIntosh, J. A., Robertson, C. R., Agarwal, V., Nair, S. K., Bulaj, G. W., and Schmidt, E. W. (2010) Circular logic: nonribosomal peptide-like macrocyclization with a ribosomal peptide catalyst J. Am. Chem. Soc. 132, 15499-15501
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15499-15501
    • McIntosh, J.A.1    Robertson, C.R.2    Agarwal, V.3    Nair, S.K.4    Bulaj, G.W.5    Schmidt, E.W.6
  • 68
    • 77954377341 scopus 로고    scopus 로고
    • Marine molecular machines: Heterocyclization in cyanobactin biosynthesis
    • McIntosh, J. A. and Schmidt, E. W. (2010) Marine molecular machines: heterocyclization in cyanobactin biosynthesis ChemBioChem 11, 1413-1421
    • (2010) ChemBioChem , vol.11 , pp. 1413-1421
    • McIntosh, J.A.1    Schmidt, E.W.2
  • 70
    • 41549163979 scopus 로고    scopus 로고
    • Translational regulation via L11: Molecular switches on the ribosome turned on and off by thiostrepton and micrococcin
    • Harms, J. M., Wilson, D. N., Schluenzen, F., Connell, S. R., Stachelhaus, T., Zaborowska, Z., Spahn, C. M., and Fucini, P. (2008) Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin Mol. Cell 30, 26-38
    • (2008) Mol. Cell , vol.30 , pp. 26-38
    • Harms, J.M.1    Wilson, D.N.2    Schluenzen, F.3    Connell, S.R.4    Stachelhaus, T.5    Zaborowska, Z.6    Spahn, C.M.7    Fucini, P.8
  • 71
    • 62449284698 scopus 로고    scopus 로고
    • Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin
    • Wieland Brown, L. C., Acker, M. G., Clardy, J., Walsh, C. T., and Fischbach, M. A. (2009) Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin Proc. Natl. Acad. Sci. U.S.A. 106, 2549-2553
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 2549-2553
    • Wieland Brown, L.C.1    Acker, M.G.2    Clardy, J.3    Walsh, C.T.4    Fischbach, M.A.5
  • 72
    • 77956244429 scopus 로고    scopus 로고
    • Genetic interception and structural characterization of thiopeptide cyclization precursors from Bacillus cereus
    • Bowers, A. A., Walsh, C. T., and Acker, M. G. (2010) Genetic interception and structural characterization of thiopeptide cyclization precursors from Bacillus cereus J. Am. Chem. Soc. 132, 12182-12184
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 12182-12184
    • Bowers, A.A.1    Walsh, C.T.2    Acker, M.G.3
  • 73
    • 84862786646 scopus 로고    scopus 로고
    • Current developments and challenges in the search for a naturally selected Diels-Alderase
    • Kim, H. J., Ruszczycky, M. W., and Liu, H. W. (2012) Current developments and challenges in the search for a naturally selected Diels-Alderase Curr. Opin. Chem. Biol. 16, 124-131
    • (2012) Curr. Opin. Chem. Biol. , vol.16 , pp. 124-131
    • Kim, H.J.1    Ruszczycky, M.W.2    Liu, H.W.3
  • 74
    • 33751095311 scopus 로고
    • The use of isotope effects to elucidate enzyme mechanisms
    • Schowen, K. B. and Schowen, R. L. (1981) The use of isotope effects to elucidate enzyme mechanisms Bioscience 31, 826-831
    • (1981) Bioscience , vol.31 , pp. 826-831
    • Schowen, K.B.1    Schowen, R.L.2
  • 75
    • 79955642774 scopus 로고    scopus 로고
    • Enzyme-catalysed [4 + 2] cycloaddition is a key step in the biosynthesis of spinosyn A
    • Kim, H. J., Ruszczycky, M. W., Choi, S. H., Liu, Y. N., and Liu, H. W. (2011) Enzyme-catalysed [4 + 2] cycloaddition is a key step in the biosynthesis of spinosyn A Nature 473, 109-112
    • (2011) Nature , vol.473 , pp. 109-112
    • Kim, H.J.1    Ruszczycky, M.W.2    Choi, S.H.3    Liu, Y.N.4    Liu, H.W.5
  • 77
    • 79953302584 scopus 로고    scopus 로고
    • Radicals from S-adenosylmethionine and their application to biosynthesis
    • Roach, P. L. (2011) Radicals from S-adenosylmethionine and their application to biosynthesis Curr. Opin. Chem. Biol. 15, 267-275
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 267-275
    • Roach, P.L.1
  • 78
    • 65249142024 scopus 로고    scopus 로고
    • Anaerobic functionalization of unactivated C-H bonds
    • Booker, S. J. (2009) Anaerobic functionalization of unactivated C-H bonds Curr. Opin. Chem. Biol. 13, 58-73
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 58-73
    • Booker, S.J.1
  • 79
    • 77949870163 scopus 로고    scopus 로고
    • Adenosyl radical: Reagent and catalyst in enzyme reactions
    • Marsh, E. N., Patterson, D. P., and Li, L. (2010) Adenosyl radical: reagent and catalyst in enzyme reactions ChemBioChem 11, 604-621
    • (2010) ChemBioChem , vol.11 , pp. 604-621
    • Marsh, E.N.1    Patterson, D.P.2    Li, L.3
  • 80
    • 70350170631 scopus 로고    scopus 로고
    • Nosiheptide biosynthesis featuring a unique indole side ring formation on the characteristic thiopeptide framework
    • Yu, Y., Duan, L., Zhang, Q., Liao, R., Ding, Y., Pan, H., Wendt-Pienkowski, E., Tang, G., Shen, B., and Liu, W. (2009) Nosiheptide biosynthesis featuring a unique indole side ring formation on the characteristic thiopeptide framework ACS Chem. Biol. 4, 855-864
    • (2009) ACS Chem. Biol. , vol.4 , pp. 855-864
    • Yu, Y.1    Duan, L.2    Zhang, Q.3    Liao, R.4    Ding, Y.5    Pan, H.6    Wendt-Pienkowski, E.7    Tang, G.8    Shen, B.9    Liu, W.10
  • 81
    • 60549109637 scopus 로고    scopus 로고
    • Thiopeptide biosynthesis featuring ribosomally synthesized precursor peptides and conserved posttranslational modifications
    • Liao, R., Duan, L., Lei, C., Pan, H., Ding, Y., Zhang, Q., Chen, D., Shen, B., Yu, Y., and Liu, W. (2009) Thiopeptide biosynthesis featuring ribosomally synthesized precursor peptides and conserved posttranslational modifications Chem. Biol. 16, 141-147
    • (2009) Chem. Biol. , vol.16 , pp. 141-147
    • Liao, R.1    Duan, L.2    Lei, C.3    Pan, H.4    Ding, Y.5    Zhang, Q.6    Chen, D.7    Shen, B.8    Yu, Y.9    Liu, W.10
  • 82
    • 67749113468 scopus 로고    scopus 로고
    • Thiostrepton biosynthesis: Prototype for a new family of bacteriocins
    • Kelly, W. L., Pan, L., and Li, C. (2009) Thiostrepton biosynthesis: prototype for a new family of bacteriocins J. Am. Chem. Soc. 131, 4327-4334
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 4327-4334
    • Kelly, W.L.1    Pan, L.2    Li, C.3
  • 83
    • 0027521129 scopus 로고
    • Biosynthesis of the modified peptide antibiotic thiostrepton in Streptomyces azureus and Streptomyces laurentii
    • Mocek, U., Zeng, Z. P., Ohagan, D., Zhou, P., Fan, L. D. G., Beale, J. M., and Floss, H. G. (1993) Biosynthesis of the modified peptide antibiotic thiostrepton in Streptomyces azureus and Streptomyces laurentii J. Am. Chem. Soc. 115, 7992-8001
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 7992-8001
    • Mocek, U.1    Zeng, Z.P.2    Ohagan, D.3    Zhou, P.4    Fan, L.D.G.5    Beale, J.M.6    Floss, H.G.7
  • 84
    • 0027442564 scopus 로고
    • Biosynthesis of the modified peptide antibiotic nosiheptide in Streptomyces actuosus
    • Mocek, U., Knaggs, A. R., Tsuchiya, R., Nguyen, T., Beale, J. M., and Floss, H. G. (1993) Biosynthesis of the modified peptide antibiotic nosiheptide in Streptomyces actuosus J. Am. Chem. Soc. 115, 7557-7568
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 7557-7568
    • Mocek, U.1    Knaggs, A.R.2    Tsuchiya, R.3    Nguyen, T.4    Beale, J.M.5    Floss, H.G.6
  • 85
    • 84860180048 scopus 로고    scopus 로고
    • Insights into quinaldic acid moiety formation in thiostrepton biosynthesis facilitating fluorinated thiopeptide generation
    • Duan, L., Wang, S., Liao, R., and Liu, W. (2012) Insights into quinaldic acid moiety formation in thiostrepton biosynthesis facilitating fluorinated thiopeptide generation Chem. Biol. 19, 443-448
    • (2012) Chem. Biol. , vol.19 , pp. 443-448
    • Duan, L.1    Wang, S.2    Liao, R.3    Liu, W.4
  • 86
    • 79958752675 scopus 로고    scopus 로고
    • Characterization of NocL involved in thiopeptide nocathiacin i biosynthesis: A [4Fe-4S] cluster and the catalysis of a radical S-adenosylmethionine enzyme
    • Zhang, Q., Chen, D., Lin, J., Liao, R., Tong, W., Xu, Z., and Liu, W. (2011) Characterization of NocL involved in thiopeptide nocathiacin I biosynthesis: a [4Fe-4S] cluster and the catalysis of a radical S-adenosylmethionine enzyme J. Biol. Chem. 286, 21287-21294
    • (2011) J. Biol. Chem. , vol.286 , pp. 21287-21294
    • Zhang, Q.1    Chen, D.2    Lin, J.3    Liao, R.4    Tong, W.5    Xu, Z.6    Liu, W.7
  • 87
    • 0037899473 scopus 로고    scopus 로고
    • Radical carbon skeleton rearrangements: Catalysis by coenzyme B12-dependent mutases
    • Banerjee, R. (2003) Radical carbon skeleton rearrangements: catalysis by coenzyme B12-dependent mutases Chem. Rev. 103, 2083-2094
    • (2003) Chem. Rev. , vol.103 , pp. 2083-2094
    • Banerjee, R.1
  • 88
    • 0022413987 scopus 로고
    • Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: Isolation, structural analysis, and biogenesis
    • Babasaki, K., Takao, T., Shimonishi, Y., and Kurahashi, K. (1985) Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: isolation, structural analysis, and biogenesis J. Biochem. 98, 585-603
    • (1985) J. Biochem. , vol.98 , pp. 585-603
    • Babasaki, K.1    Takao, T.2    Shimonishi, Y.3    Kurahashi, K.4
  • 90
    • 0037462081 scopus 로고    scopus 로고
    • Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to alpha-carbons of phenylalanine and threonine
    • Kawulka, K., Sprules, T., McKay, R. T., Mercier, P., Diaper, C. M., Zuber, P., and Vederas, J. C. (2003) Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to alpha-carbons of phenylalanine and threonine J. Am. Chem. Soc. 125, 4726-4727
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4726-4727
    • Kawulka, K.1    Sprules, T.2    McKay, R.T.3    Mercier, P.4    Diaper, C.M.5    Zuber, P.6    Vederas, J.C.7
  • 91
    • 80052485163 scopus 로고    scopus 로고
    • The 3D solution structure of thurincin H, a bacteriocin with four sulfur to alpha-carbon crosslinks
    • Sit, C. S., van Belkum, M. J., McKay, R. T., Worobo, R. W., and Vederas, J. C. (2011) The 3D solution structure of thurincin H, a bacteriocin with four sulfur to alpha-carbon crosslinks Angew. Chem., Int. Ed. 50, 8718-8721
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 8718-8721
    • Sit, C.S.1    Van Belkum, M.J.2    McKay, R.T.3    Worobo, R.W.4    Vederas, J.C.5
  • 93
    • 79957690316 scopus 로고    scopus 로고
    • The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to alpha-carbon cross-links
    • Sit, C. S., McKay, R. T., Hill, C., Ross, R. P., and Vederas, J. C. (2011) The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to alpha-carbon cross-links J. Am. Chem. Soc. 133, 7680-7683
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 7680-7683
    • Sit, C.S.1    McKay, R.T.2    Hill, C.3    Ross, R.P.4    Vederas, J.C.5
  • 94
    • 79960080501 scopus 로고    scopus 로고
    • Genome mining for radical SAM protein determinants reveals multiple sactibiotic-like gene clusters
    • Murphy, K., O'Sullivan, O., Rea, M. C., Cotter, P. D., Ross, R. P., and Hill, C. (2011) Genome mining for radical SAM protein determinants reveals multiple sactibiotic-like gene clusters PLoS ONE 6, e20852
    • (2011) PLoS ONE , vol.6 , pp. 20852
    • Murphy, K.1    O'Sullivan, O.2    Rea, M.C.3    Cotter, P.D.4    Ross, R.P.5    Hill, C.6
  • 95
    • 0034039083 scopus 로고    scopus 로고
    • Mutational analysis of the sbo-alb locus of Bacillus subtilis: Identification of genes required for subtilosin production and immunity
    • Zheng, G., Hehn, R., and Zuber, P. (2000) Mutational analysis of the sbo-alb locus of Bacillus subtilis: identification of genes required for subtilosin production and immunity J. Bacteriol. 182, 3266-3273
    • (2000) J. Bacteriol. , vol.182 , pp. 3266-3273
    • Zheng, G.1    Hehn, R.2    Zuber, P.3
  • 96
    • 0032726081 scopus 로고    scopus 로고
    • Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin
    • Zheng, G., Yan, L. Z., Vederas, J. C., and Zuber, P. (1999) Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin J. Bacteriol. 181, 7346-7355
    • (1999) J. Bacteriol. , vol.181 , pp. 7346-7355
    • Zheng, G.1    Yan, L.Z.2    Vederas, J.C.3    Zuber, P.4
  • 98
    • 0346727529 scopus 로고    scopus 로고
    • Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme
    • Berkovitch, F., Nicolet, Y., Wan, J. T., Jarrett, J. T., and Drennan, C. L. (2004) Crystal structure of biotin synthase, an S-adenosylmethionine- dependent radical enzyme Science 303, 76-79
    • (2004) Science , vol.303 , pp. 76-79
    • Berkovitch, F.1    Nicolet, Y.2    Wan, J.T.3    Jarrett, J.T.4    Drennan, C.L.5
  • 99
    • 77951930923 scopus 로고    scopus 로고
    • A consensus mechanism for Radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters
    • Grove, T. L., Ahlum, J. H., Sharma, P., Krebs, C., and Booker, S. J. (2010) A consensus mechanism for Radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters Biochemistry 49, 3783-3785
    • (2010) Biochemistry , vol.49 , pp. 3783-3785
    • Grove, T.L.1    Ahlum, J.H.2    Sharma, P.3    Krebs, C.4    Booker, S.J.5
  • 100
    • 84866011930 scopus 로고    scopus 로고
    • Identification and function of auxiliary iron-sulfur clusters in radical SAM enzymes
    • Lanz, N. D. and Booker, S. J. (2012) Identification and function of auxiliary iron-sulfur clusters in radical SAM enzymes Biochim. Biophys. Acta 1824, 1196-1212
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 1196-1212
    • Lanz, N.D.1    Booker, S.J.2
  • 101
    • 84859891708 scopus 로고    scopus 로고
    • Radical-mediated enzymatic methylation: A tale of two SAMS
    • Zhang, Q., van der Donk, W. A., and Liu, W. (2012) Radical-mediated enzymatic methylation: a tale of two SAMS Acc. Chem. Res. 45, 555-564
    • (2012) Acc. Chem. Res. , vol.45 , pp. 555-564
    • Zhang, Q.1    Van Der Donk, W.A.2    Liu, W.3
  • 103
    • 0023677320 scopus 로고
    • Biosynthesis of the modified peptide antibiotic nosiheptide in Streptomyces actuosus
    • Houck, D. R., Chen, L. C., Keller, P. J., Beale, J. M., and Floss, H. G. (1988) Biosynthesis of the modified peptide antibiotic nosiheptide in Streptomyces actuosus J. Am. Chem. Soc. 110, 5800-5806
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 5800-5806
    • Houck, D.R.1    Chen, L.C.2    Keller, P.J.3    Beale, J.M.4    Floss, H.G.5
  • 104
    • 0011116189 scopus 로고
    • Biosynthesis of the antibiotic thiostrepton - Methylation of tryptophan in the formation of the quinaldic acid moiety by transfer of the methionine methyl-group with net retention of configuration
    • Zhou, P., Ohagan, D., Mocek, U., Zeng, Z. P., Yuen, L. D., Frenzel, T., Unkefer, C. J., Beale, J. M., and Floss, H. G. (1989) Biosynthesis of the antibiotic thiostrepton-methylation of tryptophan in the formation of the quinaldic acid moiety by transfer of the methionine methyl-group with net retention of configuration J. Am. Chem. Soc. 111, 7274-7276
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 7274-7276
    • Zhou, P.1    Ohagan, D.2    Mocek, U.3    Zeng, Z.P.4    Yuen, L.D.5    Frenzel, T.6    Unkefer, C.J.7    Beale, J.M.8    Floss, H.G.9
  • 105
    • 79955526574 scopus 로고    scopus 로고
    • A radically different mechanism for S-adenosylmethionine-dependent methyltransferases
    • Grove, T. L., Benner, J. S., Radle, M. I., Ahlum, J. H., Landgraf, B. J., Krebs, C., and Booker, S. J. (2011) A radically different mechanism for S-adenosylmethionine-dependent methyltransferases Science 332, 604-607
    • (2011) Science , vol.332 , pp. 604-607
    • Grove, T.L.1    Benner, J.S.2    Radle, M.I.3    Ahlum, J.H.4    Landgraf, B.J.5    Krebs, C.6    Booker, S.J.7
  • 107
    • 84870323306 scopus 로고    scopus 로고
    • Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes
    • Pierre, S., Guillot, A., Benjdia, A., Sandstrom, C., Langella, P., and Berteau, O. (2012) Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes Nat. Chem. Biol. 8, 957-959
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 957-959
    • Pierre, S.1    Guillot, A.2    Benjdia, A.3    Sandstrom, C.4    Langella, P.5    Berteau, O.6
  • 109
    • 0347504850 scopus 로고    scopus 로고
    • Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes
    • Layer, G., Moser, J., Heinz, D. W., Jahn, D., and Schubert, W. D. (2003) Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of radical SAM enzymes EMBO J. 22, 6214-6224
    • (2003) EMBO J. , vol.22 , pp. 6214-6224
    • Layer, G.1    Moser, J.2    Heinz, D.W.3    Jahn, D.4    Schubert, W.D.5
  • 110
    • 70350729448 scopus 로고    scopus 로고
    • Prenyl transfer to aromatic substrates in the biosynthesis of aminocoumarins, meroterpenoids and phenazines: The ABBA prenyltransferase family
    • Saleh, O., Haagen, Y., Seeger, K., and Heide, L. (2009) Prenyl transfer to aromatic substrates in the biosynthesis of aminocoumarins, meroterpenoids and phenazines: the ABBA prenyltransferase family Phytochemistry 70, 1728-1738
    • (2009) Phytochemistry , vol.70 , pp. 1728-1738
    • Saleh, O.1    Haagen, Y.2    Seeger, K.3    Heide, L.4
  • 111
    • 0034003923 scopus 로고    scopus 로고
    • Efficient synthesis of octandrenolone and related dipyranoacetophenones
    • Pernin, R., Muyard, F., Bevalot, F., Tillequin, F., and Vaquette, J. (2000) Efficient synthesis of octandrenolone and related dipyranoacetophenones J. Nat. Prod. 63, 245-247
    • (2000) J. Nat. Prod. , vol.63 , pp. 245-247
    • Pernin, R.1    Muyard, F.2    Bevalot, F.3    Tillequin, F.4    Vaquette, J.5
  • 112
    • 0034608905 scopus 로고    scopus 로고
    • A fully synthetic route to the neurotrophic illicinones: Synthesis of tricycloillicinone and bicycloillicinone aldehyde
    • Pettus, T. R. R., Inoue, M., Chen, X., and Danishefsky, S. J. (2000) A fully synthetic route to the neurotrophic illicinones: synthesis of tricycloillicinone and bicycloillicinone aldehyde J. Am. Chem. Soc. 122, 6160-6168
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 6160-6168
    • Pettus, T.R.R.1    Inoue, M.2    Chen, X.3    Danishefsky, S.J.4
  • 113
    • 2142769749 scopus 로고
    • Application of the Claisen rearrangement
    • Quillinan, A. J. and Scheinmann, F. (1971) Application of the Claisen rearrangement J. Chem. Soc. D 966-967
    • (1971) J. Chem. Soc. D , pp. 966-967
    • Quillinan, A.J.1    Scheinmann, F.2
  • 114
    • 0019169721 scopus 로고
    • Prophage-mediated production of a bacteriocinlike substance by SP beta lysogens of Bacillus subtilis
    • Hemphill, H. E., Gage, I., Zahler, S. A., and Korman, R. Z. (1980) Prophage-mediated production of a bacteriocinlike substance by SP beta lysogens of Bacillus subtilis Can. J. Microbiol. 26, 1328-1333
    • (1980) Can. J. Microbiol. , vol.26 , pp. 1328-1333
    • Hemphill, H.E.1    Gage, I.2    Zahler, S.A.3    Korman, R.Z.4
  • 115
    • 0032483367 scopus 로고    scopus 로고
    • Identification and characterization of the structural and transporter genes for, and the chemical and biological properties of, sublancin 168, a novel lantibiotic produced by Bacillus subtilis 168
    • Paik, S. H., Chakicherla, A., and Hansen, J. N. (1998) Identification and characterization of the structural and transporter genes for, and the chemical and biological properties of, sublancin 168, a novel lantibiotic produced by Bacillus subtilis 168 J. Biol. Chem. 273, 23134-23142
    • (1998) J. Biol. Chem. , vol.273 , pp. 23134-23142
    • Paik, S.H.1    Chakicherla, A.2    Hansen, J.N.3
  • 117
    • 80054734191 scopus 로고    scopus 로고
    • Substrate selectivity of the sublancin S-glycosyltransferase
    • Wang, H. and van der Donk, W. A. (2011) Substrate selectivity of the sublancin S-glycosyltransferase J. Am. Chem. Soc. 133, 16394-16397
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 16394-16397
    • Wang, H.1    Van Der Donk, W.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.