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Volumn 45, Issue 6, 2006, Pages 1537-1546

Activity screening of carrier domains within nonribosomal peptide synthetases using complex substrate mixtures and large molecule mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

ASSAYS; FOURIER TRANSFORM INFRARED SPECTROSCOPY; MASS SPECTROMETRY; MOLECULAR DYNAMICS; SCREENING;

EID: 32344442373     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052333k     Document Type: Article
Times cited : (54)

References (49)
  • 2
    • 27544477567 scopus 로고    scopus 로고
    • Discovery of a new peptide natural product by Streptomyces coelicolor genome mining
    • Lautru, S., Deeth, R. J., Bailey, L. M., and Challis, G. L. (2005) Discovery of a new peptide natural product by Streptomyces coelicolor genome mining, Nat. Chem. Biol. 1 (5), 265-269.
    • (2005) Nat. Chem. Biol. , vol.1 , Issue.5 , pp. 265-269
    • Lautru, S.1    Deeth, R.J.2    Bailey, L.M.3    Challis, G.L.4
  • 3
    • 20144363202 scopus 로고    scopus 로고
    • The neocarzinostatin biosynthetic gene cluster from Streptomyces carzinostaticus ATCC 15944 involving two iterative type I polyketide syntheses
    • Liu, W., Nonaka, K., Nie, L., Zhang, J., Christenson, S. D., Bae, J., Van Lanen, S. G., Zazopoulos, E., Farnet, C. M., Yang, C. F., and Shen, B. (2005) The neocarzinostatin biosynthetic gene cluster from Streptomyces carzinostaticus ATCC 15944 involving two iterative type I polyketide syntheses, Chem. Biol. 12 (3), 293-302.
    • (2005) Chem. Biol. , vol.12 , Issue.3 , pp. 293-302
    • Liu, W.1    Nonaka, K.2    Nie, L.3    Zhang, J.4    Christenson, S.D.5    Bae, J.6    Van Lanen, S.G.7    Zazopoulos, E.8    Farnet, C.M.9    Yang, C.F.10    Shen, B.11
  • 4
    • 9144265841 scopus 로고    scopus 로고
    • Identification and analysis of a siderophore biosynthetic gene cluster from Agrobacterium tumefaciens C58
    • Rondon, M. R., Ballering, K. S., and Thomas, M. G. (2004) Identification and analysis of a siderophore biosynthetic gene cluster from Agrobacterium tumefaciens C58, Microbiology 150 (11), 3857-3866.
    • (2004) Microbiology , vol.150 , Issue.11 , pp. 3857-3866
    • Rondon, M.R.1    Ballering, K.S.2    Thomas, M.G.3
  • 5
    • 14344261742 scopus 로고    scopus 로고
    • Characterization of the formation of the pyrrole moiety during clorobiocin and coumermycin A1 biosynthesis
    • Garneau, S., Dorrestein, P. C., Kelleher, N. L., and Walsh, C. T. (2005) Characterization of the formation of the pyrrole moiety during clorobiocin and coumermycin A1 biosynthesis, Biochemistry 44 (8), 2770-2780.
    • (2005) Biochemistry , vol.44 , Issue.8 , pp. 2770-2780
    • Garneau, S.1    Dorrestein, P.C.2    Kelleher, N.L.3    Walsh, C.T.4
  • 6
    • 0036008124 scopus 로고    scopus 로고
    • Formation of β-hydroxy histidine in the biosynthesis of nikkomycin antibiotics
    • Chen, H., Hubbard, B. K., O'Connor, S. E., and Walsh, C. T. (2002) Formation of β-hydroxy histidine in the biosynthesis of nikkomycin antibiotics, Chem. Biol. 9 (1), 103-112.
    • (2002) Chem. Biol. , vol.9 , Issue.1 , pp. 103-112
    • Chen, H.1    Hubbard, B.K.2    O'Connor, S.E.3    Walsh, C.T.4
  • 7
    • 1642304143 scopus 로고    scopus 로고
    • Polyketide and nonribosomal peptide antibiotics: Modularity and versatility
    • Walsh, C. T. (2004) Polyketide and nonribosomal peptide antibiotics: Modularity and versatility, Science 303 (5665), 1805-1810.
    • (2004) Science , vol.303 , Issue.5665 , pp. 1805-1810
    • Walsh, C.T.1
  • 8
    • 9244234513 scopus 로고    scopus 로고
    • Biosynthesis of nonribosomal peptides
    • Finking, R., and Marahiel, M. A. (2004) Biosynthesis of nonribosomal peptides, Annu. Rev. Microbiol. 58, 453-488.
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 453-488
    • Finking, R.1    Marahiel, M.A.2
  • 9
    • 14644394879 scopus 로고    scopus 로고
    • Evidence for diversifying selection at the pyoverdine locus of Pseudomonas aeruginosa
    • Smith, E. E., Sims, E. H., Spencer, D. H., Kaul, R., and Olson, M. V. (2005) Evidence for diversifying selection at the pyoverdine locus of Pseudomonas aeruginosa, J. Bacteriol. 187 (6), 2138-2147.
    • (2005) J. Bacteriol. , vol.187 , Issue.6 , pp. 2138-2147
    • Smith, E.E.1    Sims, E.H.2    Spencer, D.H.3    Kaul, R.4    Olson, M.V.5
  • 10
    • 0038112130 scopus 로고    scopus 로고
    • The npgA/cfwA gene encodes a putative 4′-phosphopantetheinyl transferase which is essential for penicillin biosynthesis in Aspergillus nidulans
    • Keszenman-Pereyra, D., Lawrence, S., Twfieg, M.-E., Price, J., and Turner, G. (2003) The npgA/cfwA gene encodes a putative 4′- phosphopantetheinyl transferase which is essential for penicillin biosynthesis in Aspergillus nidulans, Curr. Genet. 43 (3), 186-190.
    • (2003) Curr. Genet. , vol.43 , Issue.3 , pp. 186-190
    • Keszenman-Pereyra, D.1    Lawrence, S.2    Twfieg, M.-E.3    Price, J.4    Turner, G.5
  • 11
    • 10944269741 scopus 로고    scopus 로고
    • An oxidative phenol coupling reaction catalyzed by OxyB, a cytochrome P450 from the vancomycin-producing microorganism
    • Zerbe, K., Woithe, K., Li, D. B., Vitali, F., Bigler, L., and Robinson, J. A. (2004) An oxidative phenol coupling reaction catalyzed by OxyB, a cytochrome P450 from the vancomycin-producing microorganism, Angew. Chem., Int. Ed. 43 (48), 6709-6713.
    • (2004) Angew. Chem., Int. Ed. , vol.43 , Issue.48 , pp. 6709-6713
    • Zerbe, K.1    Woithe, K.2    Li, D.B.3    Vitali, F.4    Bigler, L.5    Robinson, J.A.6
  • 12
    • 26844445505 scopus 로고    scopus 로고
    • Structure, function, and biosynthesis of gramicidin S synthetase
    • Vater, J., and Stein, T. H. (1999) Structure, function, and biosynthesis of gramicidin S synthetase, Compr. Nat. Prod. Chem. 4, 319-352.
    • (1999) Compr. Nat. Prod. Chem. , vol.4 , pp. 319-352
    • Vater, J.1    Stein, T.H.2
  • 14
    • 32344443996 scopus 로고    scopus 로고
    • Natural insights for chemical biologists
    • Walsh, C. T. (2005) Natural insights for chemical biologists, Nat. Chem. Biol. 1 (3), 122-124.
    • (2005) Nat. Chem. Biol. , vol.1 , Issue.3 , pp. 122-124
    • Walsh, C.T.1
  • 15
    • 20444443559 scopus 로고    scopus 로고
    • Utilizing the power of microbial genetics to bridge the gap between the promise and the application of marine natural products
    • Fortman, J. L., and Sherman, D. H. (2005) Utilizing the power of microbial genetics to bridge the gap between the promise and the application of marine natural products, ChemBioChem 6 (6), 960-978.
    • (2005) ChemBioChem , vol.6 , Issue.6 , pp. 960-978
    • Fortman, J.L.1    Sherman, D.H.2
  • 16
    • 0033179468 scopus 로고    scopus 로고
    • The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases
    • Stachelhaus, T., Mootz, H. D., and Marahiel, M. A. (1999) The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases, Chem. Biol. 6 (8), 493-505.
    • (1999) Chem. Biol. , vol.6 , Issue.8 , pp. 493-505
    • Stachelhaus, T.1    Mootz, H.D.2    Marahiel, M.A.3
  • 17
    • 0034013269 scopus 로고    scopus 로고
    • Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains
    • Challis, G. L., Ravel, J., and Townsend, C. A. (2000) Predictive, structure-based model of amino acid recognition by nonribosomal peptide synthetase adenylation domains, Chem. Biol. 7(3), 211-224.
    • (2000) Chem. Biol. , vol.7 , Issue.3 , pp. 211-224
    • Challis, G.L.1    Ravel, J.2    Townsend, C.A.3
  • 18
    • 14044264103 scopus 로고    scopus 로고
    • In silico analysis of the adenylation domains of the freestanding enzymes belonging to the eucaryotic nonribosomal peptide synthetase-like family
    • Di Vincenzo, L., Grgurina, I., and Pascarella, S. (2005) In silico analysis of the adenylation domains of the freestanding enzymes belonging to the eucaryotic nonribosomal peptide synthetase-like family, FEBS J. 272 (4), 929-941.
    • (2005) FEBS J. , vol.272 , Issue.4 , pp. 929-941
    • Di Vincenzo, L.1    Grgurina, I.2    Pascarella, S.3
  • 19
    • 23944436899 scopus 로고    scopus 로고
    • Biosynthesis of the β-amino acid moiety of the enediyne antitumor antibiotic C-1027 featuring β-amino acyl-S-carrier protein intermediates
    • Van Lanen, S. G., Dorrestein, P. C., Christenson, S. D., Liu, W., Ju, J., Kelleher, N. L., and Shen, B. (2005) Biosynthesis of the β-amino acid moiety of the enediyne antitumor antibiotic C-1027 featuring β-amino acyl-S-carrier protein intermediates, J. Am. Chem. Soc. 127 (33), 11594-11595.
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.33 , pp. 11594-11595
    • Van Lanen, S.G.1    Dorrestein, P.C.2    Christenson, S.D.3    Liu, W.4    Ju, J.5    Kelleher, N.L.6    Shen, B.7
  • 20
    • 4344645019 scopus 로고    scopus 로고
    • Biosynthetic pathway and gene cluster analysis of Curacin A, an antitubulin natural product from the tropical marine cyanobacterium Lyngbya majuscula
    • Chang, Z., Sitachitta, N., Rossi, J. V., Roberts, M. A., Flatt, P. M., Jia, J., Sherman, D. H., and Gerwick, W. H. (2004) Biosynthetic pathway and gene cluster analysis of Curacin A, an antitubulin natural product from the tropical marine cyanobacterium Lyngbya majuscula, J. Nat. Prod. 67 (8), 1356-1367.
    • (2004) J. Nat. Prod. , vol.67 , Issue.8 , pp. 1356-1367
    • Chang, Z.1    Sitachitta, N.2    Rossi, J.V.3    Roberts, M.A.4    Flatt, P.M.5    Jia, J.6    Sherman, D.H.7    Gerwick, W.H.8
  • 21
    • 0037043734 scopus 로고    scopus 로고
    • Biomimetic synthesis and optimization of cyclic peptide antibiotics
    • Kohli, R. M., Walsh, C. T., and Burkart, M. D. (2002) Biomimetic synthesis and optimization of cyclic peptide antibiotics, Nature 478 (6898), 658-661.
    • (2002) Nature , vol.478 , Issue.6898 , pp. 658-661
    • Kohli, R.M.1    Walsh, C.T.2    Burkart, M.D.3
  • 22
    • 0034648798 scopus 로고    scopus 로고
    • Peptide cyclization catalysed by the thioesterase domain of tyrocidine synthetase
    • Trauger, J. W., Kohli, R. M., Mootz, H. D., Marahiel, M. A., and Walsh, C. T. (2000) Peptide cyclization catalysed by the thioesterase domain of tyrocidine synthetase, Nature 407 (6801), 215-218.
    • (2000) Nature , vol.407 , Issue.6801 , pp. 215-218
    • Trauger, J.W.1    Kohli, R.M.2    Mootz, H.D.3    Marahiel, M.A.4    Walsh, C.T.5
  • 23
    • 1542350250 scopus 로고    scopus 로고
    • In vitro and in vivo production of new aminocoumarins by a combined biochemical, genetic, and synthetic approach
    • Galm, U., Dessoy, M. A., Schmidt, J., Wessjohann, L. A., and Heide, L. (2004) In vitro and in vivo production of new aminocoumarins by a combined biochemical, genetic, and synthetic approach, Chem. Biol. 11 (2), 173-183.
    • (2004) Chem. Biol. , vol.11 , Issue.2 , pp. 173-183
    • Galm, U.1    Dessoy, M.A.2    Schmidt, J.3    Wessjohann, L.A.4    Heide, L.5
  • 24
    • 18444376480 scopus 로고    scopus 로고
    • Heterologous expression of novobiocin and clorobiocin biosynthetic gene clusters
    • Eustaquio, A. S., Gust, B., Galm, U., Li, S.-M., Chater, K. F., and Heide, L. (2005) Heterologous expression of novobiocin and clorobiocin biosynthetic gene clusters, Appl. Environ. Microbiol. 71 (5), 2452-2459.
    • (2005) Appl. Environ. Microbiol. , vol.71 , Issue.5 , pp. 2452-2459
    • Eustaquio, A.S.1    Gust, B.2    Galm, U.3    Li, S.-M.4    Chater, K.F.5    Heide, L.6
  • 25
    • 1842865010 scopus 로고    scopus 로고
    • New aminocoumarin antibiotics from a cloQ-defective mutant of the clorobiocin producer Streptomyces roseochromogenes DS 12.976
    • Freitag, A., Galm, U., Li, S.-M., and Heide, L. (2004) New aminocoumarin antibiotics from a cloQ-defective mutant of the clorobiocin producer Streptomyces roseochromogenes DS 12.976, J. Antibiot. 57 (3), 205-209.
    • (2004) J. Antibiot. , vol.57 , Issue.3 , pp. 205-209
    • Freitag, A.1    Galm, U.2    Li, S.-M.3    Heide, L.4
  • 26
    • 0033150199 scopus 로고    scopus 로고
    • Assembly line enzymology by multimodular nonribosomal peptide synthetases: The thioesterase domain of E. coli EntF catalyzes both elongation and cyclolactonization
    • Shaw-Reid, C. A., Kelleher, N. L., Losey, H. C., Gehring, A. M., Berg, C., and Walsh, C. T. (1999) Assembly line enzymology by multimodular nonribosomal peptide synthetases: The thioesterase domain of E. coli EntF catalyzes both elongation and cyclolactonization, Chem. Biol. 6 (6), 385-400.
    • (1999) Chem. Biol. , vol.6 , Issue.6 , pp. 385-400
    • Shaw-Reid, C.A.1    Kelleher, N.L.2    Losey, H.C.3    Gehring, A.M.4    Berg, C.5    Walsh, C.T.6
  • 27
    • 0344823693 scopus 로고    scopus 로고
    • Site-specific observation of acyl intermediate processing in thiotemplate biosynthesis by Fourier transform mass spectrometry: The polyketide module of yersiniabactin synthetase
    • Mazur, M. T., Walsh, C. T., and Kelleher, N. L. (2003) Site-specific observation of acyl intermediate processing in thiotemplate biosynthesis by Fourier transform mass spectrometry: The polyketide module of yersiniabactin synthetase, Biochemistry 42 (46), 13393-13400.
    • (2003) Biochemistry , vol.42 , Issue.46 , pp. 13393-13400
    • Mazur, M.T.1    Walsh, C.T.2    Kelleher, N.L.3
  • 28
    • 0242266935 scopus 로고    scopus 로고
    • Fourier-transform mass spectrometry for detection of thioester-bound intermediates in unfractionated proteolytic mixtures of 80 and 191 kDa portions of Bacitracin a synthetase
    • Hicks, L., Weinreb, P., Konz, D., Marahiel, M. A., Walsh, C. T., and Kelleher, N. L. (2003) Fourier-transform mass spectrometry for detection of thioester-bound intermediates in unfractionated proteolytic mixtures of 80 and 191 kDa portions of Bacitracin A synthetase, Anal. Chim. Acta 496 (1-2), 217-224.
    • (2003) Anal. Chim. Acta , vol.496 , Issue.1-2 , pp. 217-224
    • Hicks, L.1    Weinreb, P.2    Konz, D.3    Marahiel, M.A.4    Walsh, C.T.5    Kelleher, N.L.6
  • 29
    • 6044236054 scopus 로고    scopus 로고
    • Mass spectrometric interrogation of thioester-bound intermediates in the initial stages of epothilone biosynthesis
    • Hicks, L. M., O'Connor, S. E., Mazur, M. T., Walsh, C. T., and Kelleher, N. L. (2004) Mass spectrometric interrogation of thioester-bound intermediates in the initial stages of epothilone biosynthesis, Chem. Biol. 11 (3), 327-335.
    • (2004) Chem. Biol. , vol.11 , Issue.3 , pp. 327-335
    • Hicks, L.M.1    O'Connor, S.E.2    Mazur, M.T.3    Walsh, C.T.4    Kelleher, N.L.5
  • 30
    • 6044254962 scopus 로고    scopus 로고
    • Kinetic and regiospecific interrogation of covalent intermediates in the non-ribosomal peptide synthesis of yersiniabactin
    • McLoughlin, S. M., and Kelleher, N. L. (2004) Kinetic and regiospecific interrogation of covalent intermediates in the non-ribosomal peptide synthesis of yersiniabactin, J. Am. Chem. Soc. 126 (41), 13265-13275.
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.41 , pp. 13265-13275
    • McLoughlin, S.M.1    Kelleher, N.L.2
  • 31
    • 17644367150 scopus 로고    scopus 로고
    • Elucidating the substrate specificity and condensation domain activity of FkbP, the FK520 pipecolate-incorporating enzyme
    • Gatto, G. J., Jr., McLoughlin, S. M., Kelleher, N. L., and Walsh, C. T. (2005) Elucidating the substrate specificity and condensation domain activity of FkbP, the FK520 pipecolate-incorporating enzyme, Biochemistry 44 (16), 5993-6002.
    • (2005) Biochemistry , vol.44 , Issue.16 , pp. 5993-6002
    • Gatto Jr., G.J.1    McLoughlin, S.M.2    Kelleher, N.L.3    Walsh, C.T.4
  • 33
    • 27544500799 scopus 로고    scopus 로고
    • Characterization of a new tailoring domain in polyketide biogenesis: The amine transferase domain of MycA in the mycosubtilin gene cluster
    • Aron, Z. D., Dorrestein, P. C., Blackball, J. R., Kelleher, N. L., and Walsh, C. T. (2005) Characterization of a new tailoring domain in polyketide biogenesis: The amine transferase domain of MycA in the mycosubtilin gene cluster, J. Am. Chem. Soc. 127 (43), 14986-14987.
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.43 , pp. 14986-14987
    • Aron, Z.D.1    Dorrestein, P.C.2    Blackball, J.R.3    Kelleher, N.L.4    Walsh, C.T.5
  • 34
    • 18944399910 scopus 로고    scopus 로고
    • Chain initiation on type I modular polyketide synthases revealed by limited proteolysis and ion-trap mass spectrometry
    • Hong, H., Appleyard, A. N., Siskos, A. P., Garcia-Bernardo, J., Staunton, J., and Leadlay, P. F. (2005) Chain initiation on type I modular polyketide synthases revealed by limited proteolysis and ion-trap mass spectrometry, FEBS J. 272 (10), 2373-2387.
    • (2005) FEBS J. , vol.272 , Issue.10 , pp. 2373-2387
    • Hong, H.1    Appleyard, A.N.2    Siskos, A.P.3    Garcia-Bernardo, J.4    Staunton, J.5    Leadlay, P.F.6
  • 35
    • 24344469124 scopus 로고    scopus 로고
    • Analysis of covalently bound polyketide intermediates on 6-deoxyerythronolide B synthase by tandem proteolysis-mass spectrometry
    • Schnarr, N. A., Chen, A. Y., Cane, D. E., and Khosla, C. (2005) Analysis of covalently bound polyketide intermediates on 6-deoxyerythronolide B synthase by tandem proteolysis-mass spectrometry, Biochemistry 44 (35), 11836-11842.
    • (2005) Biochemistry , vol.44 , Issue.35 , pp. 11836-11842
    • Schnarr, N.A.1    Chen, A.Y.2    Cane, D.E.3    Khosla, C.4
  • 37
    • 0033485259 scopus 로고    scopus 로고
    • Crystal structure of the surfactin synthetase-activating enzyme Sfp: A prototype of the 4′-phosphopantetheinyl transferase superfamily
    • Reuter, K., Mofid, M. R., Marahiel, M. A., and Ficner, R. (1999) Crystal structure of the surfactin synthetase-activating enzyme Sfp: A prototype of the 4′-phosphopantetheinyl transferase superfamily, EMBO J. 18 (23), 6823-6831.
    • (1999) EMBO J. , vol.18 , Issue.23 , pp. 6823-6831
    • Reuter, K.1    Mofid, M.R.2    Marahiel, M.A.3    Ficner, R.4
  • 38
    • 0033539471 scopus 로고    scopus 로고
    • Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore pyochelin: In vitro reconstitution of aryl-4,2-bisthiazoline synthetase activity from PchD, PchE, and PchF
    • Quadri, L. E. N., Keating, T. A., Patel, H. M., and Walsh, C. T. (1999) Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore pyochelin: In vitro reconstitution of aryl-4,2-bisthiazoline synthetase activity from PchD, PchE, and PchF, Biochemistry 38 (45), 14941-14954.
    • (1999) Biochemistry , vol.38 , Issue.45 , pp. 14941-14954
    • Quadri, L.E.N.1    Keating, T.A.2    Patel, H.M.3    Walsh, C.T.4
  • 39
    • 3042551455 scopus 로고    scopus 로고
    • Structure and biosynthesis of the Jamaicamides, new mixed polyketide-peptide neurotoxins from the marine cyanobacterium Lyngbya majuscula
    • Edwards, D. J., Marquez, B. L., Nogle, L. M., McPhail, K., Goeger, D. E., Roberts, M. A., and Gerwick, W. H. (2004) Structure and biosynthesis of the Jamaicamides, new mixed polyketide-peptide neurotoxins from the marine cyanobacterium Lyngbya majuscula, Chem. Biol. 11 (6), 817-833.
    • (2004) Chem. Biol. , vol.11 , Issue.6 , pp. 817-833
    • Edwards, D.J.1    Marquez, B.L.2    Nogle, L.M.3    McPhail, K.4    Goeger, D.E.5    Roberts, M.A.6    Gerwick, W.H.7
  • 40
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the Gram-positive bacterium Bacillus subtilis
    • Kunst, F., Ogasawara, N., Moszer, I., et al. (1997) The complete genome sequence of the Gram-positive bacterium Bacillus subtilis, Nature 390, 249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3
  • 42
    • 18444415756 scopus 로고    scopus 로고
    • Bacillus subtilis antibiotics: Structures, syntheses and specific functions
    • Stein, T. (2005) Bacillus subtilis antibiotics: Structures, syntheses and specific functions, Mol. Microbiol. 56 (4), 845-857.
    • (2005) Mol. Microbiol. , vol.56 , Issue.4 , pp. 845-857
    • Stein, T.1
  • 43
    • 0031623267 scopus 로고    scopus 로고
    • Fourier transform ion cyclotron resonance mass spectrometry: A primer
    • Marshall, A. G., Hendrickson, C. L., and Jackson, G. S. (1998) Fourier transform ion cyclotron resonance mass spectrometry: A primer, Mass Spectrom. Rev. 17 (1), 1-35.
    • (1998) Mass Spectrom. Rev. , vol.17 , Issue.1 , pp. 1-35
    • Marshall, A.G.1    Hendrickson, C.L.2    Jackson, G.S.3
  • 45
    • 0037595678 scopus 로고    scopus 로고
    • Total synthesis of (-)-Minquartynoic Acid: An anti-cancer, anti-HIV natural product
    • Gung, B. W., and Dickson, H. (2002) Total synthesis of (-)-Minquartynoic Acid: An anti-cancer, anti-HIV natural product, Org. Lett. 4 (15), 2517-2519.
    • (2002) Org. Lett. , vol.4 , Issue.15 , pp. 2517-2519
    • Gung, B.W.1    Dickson, H.2
  • 48
    • 0030481735 scopus 로고    scopus 로고
    • A high-performance modular data system for Fourier transform ion cyclotron resonance mass spectrometry
    • Senko, M. W., Canterbury, J. D., Guan, S., and Marshall, A. G. (1996) A high-performance modular data system for Fourier transform ion cyclotron resonance mass spectrometry, Rapid Commun. Mass Spectrom. 10, 1839-1844.
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 1839-1844
    • Senko, M.W.1    Canterbury, J.D.2    Guan, S.3    Marshall, A.G.4


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