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Volumn 11, Issue 11, 2016, Pages 3035-3042

Inhibition of the flavin-dependent monooxygenase siderophore A (SidA) blocks siderophore biosynthesis and aspergillus fumigatus growth

Author keywords

[No Author keywords available]

Indexed keywords

AGAR; CELASTROL; SIDEROPHORE; SIDEROPHORE A; UNCLASSIFIED DRUG; MIXED FUNCTION OXIDASE;

EID: 84996866505     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.6b00666     Document Type: Article
Times cited : (24)

References (57)
  • 1
    • 84881021238 scopus 로고    scopus 로고
    • Allergic bronchopulmonary aspergillosis: Review of literature and proposal of new diagnostic and classification criteria
    • Agarwal, R., Chakrabarti, A., Shah, A., Gupta, D., Meis, J. F., Guleria, R., Moss, R., and Denning, D. W. (2013) Allergic bronchopulmonary aspergillosis: review of literature and proposal of new diagnostic and classification criteria Clin. Exp. Allergy 43, 850-873 10.1111/cea.12141
    • (2013) Clin. Exp. Allergy , vol.43 , pp. 850-873
    • Agarwal, R.1    Chakrabarti, A.2    Shah, A.3    Gupta, D.4    Meis, J.F.5    Guleria, R.6    Moss, R.7    Denning, D.W.8
  • 4
    • 84943360476 scopus 로고    scopus 로고
    • Combination Therapy for Invasive Aspergillosis: Controversies and Conclusions
    • Schlamm, H. T. and Marr, K. A. (2015) Combination Therapy for Invasive Aspergillosis: Controversies and Conclusions Curr. Fungal Infect. Rep. 9, 130-134 10.1007/s12281-015-0220-7
    • (2015) Curr. Fungal Infect. Rep. , vol.9 , pp. 130-134
    • Schlamm, H.T.1    Marr, K.A.2
  • 5
    • 84892836801 scopus 로고    scopus 로고
    • Aspergillus fumigatus What Makes the Species a Ubiquitous Human Fungal Pathogen?
    • Kwon-Chung, K. J. and Sugui, J. A. (2013) Aspergillus fumigatus What Makes the Species a Ubiquitous Human Fungal Pathogen? PLoS Pathog. 9, e1003743 10.1371/journal.ppat.1003743
    • (2013) PLoS Pathog. , vol.9 , pp. e1003743
    • Kwon-Chung, K.J.1    Sugui, J.A.2
  • 6
    • 80051799474 scopus 로고    scopus 로고
    • Iron homeostasis, Achilles' heel of Aspergillus fumigatus?
    • Schrettl, M. and Haas, H. (2011) Iron homeostasis, Achilles' heel of Aspergillus fumigatus? Curr. Opin. Microbiol. 14, 400-405 10.1016/j.mib.2011.06.002
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 400-405
    • Schrettl, M.1    Haas, H.2
  • 7
    • 84897457176 scopus 로고    scopus 로고
    • Onflicting Interests in the Pathogen-Host Tug of War: Fungal Micronutrient Scavenging Versus Mammalian Nutritional Immunity
    • Potrykus, J., Ballou, E. R., Childers, D. S., and Brown, A. J. P. (2014) onflicting Interests in the Pathogen-Host Tug of War: Fungal Micronutrient Scavenging Versus Mammalian Nutritional Immunity PLoS Pathog. 10, e1003910 10.1371/journal.ppat.1003910
    • (2014) PLoS Pathog. , vol.10 , pp. e1003910
    • Potrykus, J.1    Ballou, E.R.2    Childers, D.S.3    Brown, A.J.P.4
  • 8
    • 1342344975 scopus 로고    scopus 로고
    • Survival of Aspergillus fumigatus in Serum Involves Removal of Iron from Transferrin: The Role of Siderophores
    • Hissen, A. H. T., Chow, J. M. T., Pinto, L. J., and Moore, M. M. (2004) Survival of Aspergillus fumigatus in Serum Involves Removal of Iron from Transferrin: the Role of Siderophores Infect. Immun. 72, 1402-1408 10.1128/IAI.72.3.1402-1408.2004
    • (2004) Infect. Immun. , vol.72 , pp. 1402-1408
    • Hissen, A.H.T.1    Chow, J.M.T.2    Pinto, L.J.3    Moore, M.M.4
  • 9
    • 8644220677 scopus 로고    scopus 로고
    • Siderophore biosynthesis but not Reductive Iron Assimilation is essential for Aspergillus fumigatus virulence
    • Schrettl, M., Bignell, E., Kragl, C., Joechl, C., Rogers, T., Arst, H. N., Haynes, K., and Haas, H. (2004) Siderophore biosynthesis but not Reductive Iron Assimilation is essential for Aspergillus fumigatus virulence J. Exp. Med. 200, 1213-1219 10.1084/jem.20041242
    • (2004) J. Exp. Med. , vol.200 , pp. 1213-1219
    • Schrettl, M.1    Bignell, E.2    Kragl, C.3    Joechl, C.4    Rogers, T.5    Arst, H.N.6    Haynes, K.7    Haas, H.8
  • 10
    • 84907143758 scopus 로고    scopus 로고
    • Fungal siderophore metabolism with a focus on Aspergillus fumigatus
    • Haas, H. (2014) Fungal siderophore metabolism with a focus on Aspergillus fumigatus Nat. Prod. Rep. 31, 1266-1276 10.1039/C4NP00071D
    • (2014) Nat. Prod. Rep. , vol.31 , pp. 1266-1276
    • Haas, H.1
  • 12
    • 79961062166 scopus 로고    scopus 로고
    • SidL, an Aspergillus fumigatus Transacetylase Involved in Biosynthesis of the Siderophores Ferricrocin and Hydroxyferricrocin
    • Blatzer, M., Schrettl, M., Sarg, B., Lindner, H. H., Pfaller, K., and Haas, H. (2011) SidL, an Aspergillus fumigatus Transacetylase Involved in Biosynthesis of the Siderophores Ferricrocin and Hydroxyferricrocin Appl. Environ. Microbiol. 77, 4959-4966 10.1128/AEM.00182-11
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 4959-4966
    • Blatzer, M.1    Schrettl, M.2    Sarg, B.3    Lindner, H.H.4    Pfaller, K.5    Haas, H.6
  • 13
    • 84864066994 scopus 로고    scopus 로고
    • Iron - A key nexus in the virulence of Aspergillus fumigatus
    • Haas, H. (2012) Iron-a key nexus in the virulence of Aspergillus fumigatus Front. Microbiol. 3, 28 10.3389/fmicb.2012.00028
    • (2012) Front. Microbiol. , vol.3 , pp. 28
    • Haas, H.1
  • 14
    • 23944524422 scopus 로고    scopus 로고
    • The Aspergillus fumigatus Siderophore Biosynthetic Gene sidA, Encoding L-Ornithine N5-Oxygenase, Is Required for Virulence
    • Hissen, A. H. T., Wan, A. N. C., Warwas, M. L., Pinto, L. J., and Moore, M. M. (2005) The Aspergillus fumigatus Siderophore Biosynthetic Gene sidA, Encoding L-Ornithine N5-Oxygenase, Is Required for Virulence Infect. Immun. 73, 5493-5503 10.1128/IAI.73.9.5493-5503.2005
    • (2005) Infect. Immun. , vol.73 , pp. 5493-5503
    • Hissen, A.H.T.1    Wan, A.N.C.2    Warwas, M.L.3    Pinto, L.J.4    Moore, M.M.5
  • 15
    • 84866061118 scopus 로고    scopus 로고
    • Structural Insight into the Mechanism of Oxygen Activation and Substrate Selectivity of Flavin-Dependent N-Hydroxylating Monooxygenases
    • Franceschini, S., Fedkenheuer, M., Vogelaar, N. J., Robinson, H. H., Sobrado, P., and Mattevi, A. (2012) Structural Insight into the Mechanism of Oxygen Activation and Substrate Selectivity of Flavin-Dependent N-Hydroxylating Monooxygenases Biochemistry 51, 7043-7045 10.1021/bi301072w
    • (2012) Biochemistry , vol.51 , pp. 7043-7045
    • Franceschini, S.1    Fedkenheuer, M.2    Vogelaar, N.J.3    Robinson, H.H.4    Sobrado, P.5    Mattevi, A.6
  • 16
    • 84895777610 scopus 로고    scopus 로고
    • C4a-Hydroperoxyflavin Formation in N-Hydroxylating Flavin Monooxygenases Is Mediated by the 2′-OH of the Nicotinamide Ribose of NADP+
    • Robinson, R., Badieyan, S., and Sobrado, P. (2013) C4a-Hydroperoxyflavin Formation in N-Hydroxylating Flavin Monooxygenases Is Mediated by the 2′-OH of the Nicotinamide Ribose of NADP+ Biochemistry 52, 9089-9091 10.1021/bi4014903
    • (2013) Biochemistry , vol.52 , pp. 9089-9091
    • Robinson, R.1    Badieyan, S.2    Sobrado, P.3
  • 17
    • 77955251194 scopus 로고    scopus 로고
    • Aspergillus fumigatus SidA Is a Highly Specific Ornithine Hydroxylase with Bound Flavin Cofactor
    • Chocklett, S. W. and Sobrado, P. (2010) Aspergillus fumigatus SidA Is a Highly Specific Ornithine Hydroxylase with Bound Flavin Cofactor Biochemistry 49, 6777-6783 10.1021/bi100291n
    • (2010) Biochemistry , vol.49 , pp. 6777-6783
    • Chocklett, S.W.1    Sobrado, P.2
  • 18
    • 84887486191 scopus 로고    scopus 로고
    • Role of Ser-257 in the Sliding Mechanism of NADP(H) in the Reaction Catalyzed by the Aspergillus fumigatus Flavin-dependent Ornithine N5-Monooxygenase SidA
    • Shirey, C., Badieyan, S., and Sobrado, P. (2013) Role of Ser-257 in the Sliding Mechanism of NADP(H) in the Reaction Catalyzed by the Aspergillus fumigatus Flavin-dependent Ornithine N5-Monooxygenase SidA J. Biol. Chem. 288, 32440-32448 10.1074/jbc.M113.487181
    • (2013) J. Biol. Chem. , vol.288 , pp. 32440-32448
    • Shirey, C.1    Badieyan, S.2    Sobrado, P.3
  • 20
    • 84859647304 scopus 로고    scopus 로고
    • A fluorescence polarization binding assay to identify inhibitors of flavin-dependent monooxygenases
    • Qi, J., Kizjakina, K., Robinson, R., Tolani, K., and Sobrado, P. (2012) A fluorescence polarization binding assay to identify inhibitors of flavin-dependent monooxygenases Anal. Biochem. 425, 80-87 10.1016/j.ab.2012.03.002
    • (2012) Anal. Biochem. , vol.425 , pp. 80-87
    • Qi, J.1    Kizjakina, K.2    Robinson, R.3    Tolani, K.4    Sobrado, P.5
  • 21
    • 0027294886 scopus 로고
    • Kinetics of residual chloride transport in human red blood cells after maximum covalent 4,4′-diisothiocyanostilbene-2,2′-disulfonic acid binding
    • Gasbjerg, P., Funder, J., and Brahm, J. (1993) Kinetics of residual chloride transport in human red blood cells after maximum covalent 4,4′-diisothiocyanostilbene-2,2′-disulfonic acid binding J. Gen. Physiol. 101, 715-732 10.1085/jgp.101.5.715
    • (1993) J. Gen. Physiol. , vol.101 , pp. 715-732
    • Gasbjerg, P.1    Funder, J.2    Brahm, J.3
  • 22
    • 0027179989 scopus 로고
    • DIDS (4,4′-diisothiocyanatostilbene-2,2′-disulfonic acid) inhibits an early step of protein translocation across the mammalian ER membrane
    • Jungnickel, B. and Rapoport, T. A. (1993) DIDS (4,4′-diisothiocyanatostilbene-2,2′-disulfonic acid) inhibits an early step of protein translocation across the mammalian ER membrane FEBS Lett. 329, 268-272 10.1016/0014-5793(93)80235-M
    • (1993) FEBS Lett. , vol.329 , pp. 268-272
    • Jungnickel, B.1    Rapoport, T.A.2
  • 23
    • 33751321865 scopus 로고    scopus 로고
    • A detergent-based assay for the detection of promiscuous inhibitors
    • Feng, B. Y. and Shoichet, B. K. (2006) A detergent-based assay for the detection of promiscuous inhibitors Nat. Protoc. 1, 550-553 10.1038/nprot.2006.77
    • (2006) Nat. Protoc. , vol.1 , pp. 550-553
    • Feng, B.Y.1    Shoichet, B.K.2
  • 24
    • 65349155431 scopus 로고    scopus 로고
    • ThermoFAD, a Thermofluor®-adapted flavin ad hoc detection system for protein folding and ligand binding
    • Forneris, F., Orru, R., Bonivento, D., Chiarelli, L. R., and Mattevi, A. (2009) ThermoFAD, a Thermofluor®-adapted flavin ad hoc detection system for protein folding and ligand binding FEBS J. 276, 2833-2840 10.1111/j.1742-4658.2009.07006.x
    • (2009) FEBS J. , vol.276 , pp. 2833-2840
    • Forneris, F.1    Orru, R.2    Bonivento, D.3    Chiarelli, L.R.4    Mattevi, A.5
  • 26
    • 70349921403 scopus 로고    scopus 로고
    • Molecular Mechanism of Inhibition of the Human Protein Complex Hsp90-Cdc37, a Kinome Chaperone-Cochaperone, by Triterpene Celastrol
    • Sreeramulu, S., Gande, S. L., Göbel, M., and Schwalbe, H. (2009) Molecular Mechanism of Inhibition of the Human Protein Complex Hsp90-Cdc37, a Kinome Chaperone-Cochaperone, by Triterpene Celastrol Angew. Chem., Int. Ed. 48, 5853-5855 10.1002/anie.200900929
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 5853-5855
    • Sreeramulu, S.1    Gande, S.L.2    Göbel, M.3    Schwalbe, H.4
  • 27
    • 83055161400 scopus 로고    scopus 로고
    • Remarkable stereospecific conjugate additions to the Hsp90 inhibitor celastrol
    • Klaic, L., Trippier, P. C., Mishra, R. K., Morimoto, R. I., and Silverman, R. B. (2011) Remarkable stereospecific conjugate additions to the Hsp90 inhibitor celastrol J. Am. Chem. Soc. 133, 19634-19637 10.1021/ja208359a
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 19634-19637
    • Klaic, L.1    Trippier, P.C.2    Mishra, R.K.3    Morimoto, R.I.4    Silverman, R.B.5
  • 28
    • 0023127806 scopus 로고
    • Universal chemical assay for the detection and determination of siderophores
    • Schwyn, B. and Neilands, J. B. (1987) Universal chemical assay for the detection and determination of siderophores Anal. Biochem. 160, 47-56 10.1016/0003-2697(87)90612-9
    • (1987) Anal. Biochem. , vol.160 , pp. 47-56
    • Schwyn, B.1    Neilands, J.B.2
  • 29
    • 0034537481 scopus 로고    scopus 로고
    • Siderophore Production and Iron Reduction by Pseudomonas mendocina in Response to Iron Deprivation
    • Hersman, L., Huang, A., Maurice, P., and Forsythe, J. (2000) Siderophore Production and Iron Reduction by Pseudomonas mendocina in Response to Iron Deprivation Geomicrobiol. J. 17, 261-273 10.1080/01490450050192965
    • (2000) Geomicrobiol. J. , vol.17 , pp. 261-273
    • Hersman, L.1    Huang, A.2    Maurice, P.3    Forsythe, J.4
  • 31
    • 0030033830 scopus 로고    scopus 로고
    • Pyoverdin is essential for virulence of Pseudomonas aeruginosa
    • Meyer, J. M., Neely, A., Stintzi, A., Georges, C., and Holder, I. A. (1996) Pyoverdin is essential for virulence of Pseudomonas aeruginosa Infect. Immun. 64, 518-523
    • (1996) Infect. Immun. , vol.64 , pp. 518-523
    • Meyer, J.M.1    Neely, A.2    Stintzi, A.3    Georges, C.4    Holder, I.A.5
  • 32
    • 84930225222 scopus 로고    scopus 로고
    • Breaking a pathogen's iron will: Inhibiting siderophore production as an antimicrobial strategy
    • Lamb, A. L. (2015) Breaking a pathogen's iron will: Inhibiting siderophore production as an antimicrobial strategy Biochim. Biophys. Acta, Proteins Proteomics 1854, 1054-1070 10.1016/j.bbapap.2015.05.001
    • (2015) Biochim. Biophys. Acta, Proteins Proteomics , vol.1854 , pp. 1054-1070
    • Lamb, A.L.1
  • 34
    • 84908428878 scopus 로고    scopus 로고
    • Expanding the results of a high throughput screen against an isochorismate-pyruvate lyase to enzymes of a similar scaffold or mechanism
    • Meneely, K. M., Luo, Q., Riley, A. P., Taylor, B., Roy, A., Stein, R. L., Prisinzano, T. E., and Lamb, A. L. (2014) Expanding the results of a high throughput screen against an isochorismate-pyruvate lyase to enzymes of a similar scaffold or mechanism Bioorg. Med. Chem. 22, 5961-5969 10.1016/j.bmc.2014.09.010
    • (2014) Bioorg. Med. Chem. , vol.22 , pp. 5961-5969
    • Meneely, K.M.1    Luo, Q.2    Riley, A.P.3    Taylor, B.4    Roy, A.5    Stein, R.L.6    Prisinzano, T.E.7    Lamb, A.L.8
  • 35
    • 33344469904 scopus 로고    scopus 로고
    • Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis
    • Ferreras, J. A., Ryu, J.-S., Di Lello, F., Tan, D. S., and Quadri, L. E. N. (2005) Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis Nat. Chem. Biol. 1, 29-32 10.1038/nchembio706
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 29-32
    • Ferreras, J.A.1    Ryu, J.-S.2    Di Lello, F.3    Tan, D.S.4    Quadri, L.E.N.5
  • 36
    • 67249090804 scopus 로고    scopus 로고
    • Screening method to identify inhibitors of siderophore biosynthesis in the opportunistic fungal pathogen, Aspergillus fumigatus
    • Pinto, L. J. and Moore, M. M. (2009) Screening method to identify inhibitors of siderophore biosynthesis in the opportunistic fungal pathogen, Aspergillus fumigatus Lett. Appl. Microbiol. 49, 8-13 10.1111/j.1472-765X.2009.02582.x
    • (2009) Lett. Appl. Microbiol. , vol.49 , pp. 8-13
    • Pinto, L.J.1    Moore, M.M.2
  • 37
    • 84873586450 scopus 로고    scopus 로고
    • Effects of celastrol on human cervical cancer cells as revealed by ion-trap gas chromatography-mass spectrometry based metabolic profiling
    • Hu, Y., Qi, Y., Liu, H., Fan, G., and Chai, Y. (2013) Effects of celastrol on human cervical cancer cells as revealed by ion-trap gas chromatography-mass spectrometry based metabolic profiling Biochim. Biophys. Acta, Gen. Subj. 1830, 2779-2789 10.1016/j.bbagen.2012.10.024
    • (2013) Biochim. Biophys. Acta, Gen. Subj. , vol.1830 , pp. 2779-2789
    • Hu, Y.1    Qi, Y.2    Liu, H.3    Fan, G.4    Chai, Y.5
  • 38
    • 0034752311 scopus 로고    scopus 로고
    • Celastrol, a potent antioxidant and anti-inflammatory drug, as a possible treatment for Alzheimer's disease
    • Allison, A. C., Cacabelos, R., Lombardi, V. R. M., álvarez, X. A., and Vigo, C. (2001) Celastrol, a potent antioxidant and anti-inflammatory drug, as a possible treatment for Alzheimer's disease Prog. Neuro-Psychopharmacol. Biol. Psychiatry 25, 1341-1357 10.1016/S0278-5846(01)00192-0
    • (2001) Prog. Neuro-Psychopharmacol. Biol. Psychiatry , vol.25 , pp. 1341-1357
    • Allison, A.C.1    Cacabelos, R.2    Lombardi, V.R.M.3    Álvarez, X.A.4    Vigo, C.5
  • 39
    • 68349129966 scopus 로고    scopus 로고
    • Suppression of inflammatory responses by celastrol, a quinone methide triterpenoid isolated from Celastrus regelii
    • Kim, D. H., Shin, E. K., Kim, Y. H., Lee, B. W., Jun, J. G., Park, J. H. Y., and Kim, J. K. (2009) Suppression of inflammatory responses by celastrol, a quinone methide triterpenoid isolated from Celastrus regelii Eur. J. Clin. Invest. 39, 819-827 10.1111/j.1365-2362.2009.02186.x
    • (2009) Eur. J. Clin. Invest. , vol.39 , pp. 819-827
    • Kim, D.H.1    Shin, E.K.2    Kim, Y.H.3    Lee, B.W.4    Jun, J.G.5    Park, J.H.Y.6    Kim, J.K.7
  • 40
    • 84862676391 scopus 로고    scopus 로고
    • Celastrus and Its Bioactive Celastrol Protect against Bone Damage in Autoimmune Arthritis by Modulating Osteoimmune Cross-talk
    • Nanjundaiah, S. M., Venkatesha, S. H., Yu, H., Tong, L., Stains, J. P., and Moudgil, K. D. (2012) Celastrus and Its Bioactive Celastrol Protect against Bone Damage in Autoimmune Arthritis by Modulating Osteoimmune Cross-talk J. Biol. Chem. 287, 22216-22226 10.1074/jbc.M112.356816
    • (2012) J. Biol. Chem. , vol.287 , pp. 22216-22226
    • Nanjundaiah, S.M.1    Venkatesha, S.H.2    Yu, H.3    Tong, L.4    Stains, J.P.5    Moudgil, K.D.6
  • 41
    • 33646406554 scopus 로고    scopus 로고
    • Celastrol, a Triterpene Extracted from the Chinese "thunder of God Vine" Is a Potent Proteasome Inhibitor and Suppresses Human Prostate Cancer Growth in Nude Mice
    • Yang, H., Chen, D., Cui, Q. C., Yuan, X., and Dou, Q. P. (2006) Celastrol, a Triterpene Extracted from the Chinese "Thunder of God Vine" Is a Potent Proteasome Inhibitor and Suppresses Human Prostate Cancer Growth in Nude Mice Cancer Res. 66, 4758-4765 10.1158/0008-5472.CAN-05-4529
    • (2006) Cancer Res. , vol.66 , pp. 4758-4765
    • Yang, H.1    Chen, D.2    Cui, Q.C.3    Yuan, X.4    Dou, Q.P.5
  • 43
    • 78649921943 scopus 로고    scopus 로고
    • Toxic effects of celastrol on embryonic development of zebrafish (Danio rerio)
    • Wang, S., Liu, K., Wang, X., He, Q., and Chen, X. (2011) Toxic effects of celastrol on embryonic development of zebrafish (Danio rerio) Drug Chem. Toxicol. 34, 61-65 10.3109/01480545.2010.494664
    • (2011) Drug Chem. Toxicol. , vol.34 , pp. 61-65
    • Wang, S.1    Liu, K.2    Wang, X.3    He, Q.4    Chen, X.5
  • 44
    • 33744486642 scopus 로고    scopus 로고
    • Celastrol Blocks Neuronal Cell Death and Extends Life in Transgenic Mouse Model of Amyotrophic Lateral Sclerosis
    • Kiaei, M., Kipiani, K., Petri, S., Chen, J., Calingasan, N. Y., and Beal, M. F. (2005) Celastrol Blocks Neuronal Cell Death and Extends Life in Transgenic Mouse Model of Amyotrophic Lateral Sclerosis Neurodegener. Dis. 2, 246-254 10.1159/000090364
    • (2005) Neurodegener. Dis. , vol.2 , pp. 246-254
    • Kiaei, M.1    Kipiani, K.2    Petri, S.3    Chen, J.4    Calingasan, N.Y.5    Beal, M.F.6
  • 46
    • 84908432141 scopus 로고    scopus 로고
    • Celastrol inhibits Plasmodium falciparum enoyl-acyl carrier protein reductase
    • Tallorin, L., Durrant, J. D., Nguyen, Q. G., McCammon, J. A., and Burkart, M. D. (2014) Celastrol inhibits Plasmodium falciparum enoyl-acyl carrier protein reductase Bioorg. Med. Chem. 22, 6053-6061 10.1016/j.bmc.2014.09.002
    • (2014) Bioorg. Med. Chem. , vol.22 , pp. 6053-6061
    • Tallorin, L.1    Durrant, J.D.2    Nguyen, Q.G.3    McCammon, J.A.4    Burkart, M.D.5
  • 47
    • 77951953170 scopus 로고    scopus 로고
    • Non-Competitive Inhibition by Active Site Binders
    • Blat, Y. (2010) Non-Competitive Inhibition by Active Site Binders Chem. Biol. Drug Des. 75, 535-540 10.1111/j.1747-0285.2010.00972.x
    • (2010) Chem. Biol. Drug Des. , vol.75 , pp. 535-540
    • Blat, Y.1
  • 48
    • 11244289498 scopus 로고    scopus 로고
    • Antifungal properties of pristimerin and celastrol isolated from Celastrus hypoleucus
    • Luo, D.-Q., Wang, H., Tian, X., Shao, H.-J., and Liu, J.-K. (2005) Antifungal properties of pristimerin and celastrol isolated from Celastrus hypoleucus Pest Manage. Sci. 61, 85-90 10.1002/ps.953
    • (2005) Pest Manage. Sci. , vol.61 , pp. 85-90
    • Luo, D.-Q.1    Wang, H.2    Tian, X.3    Shao, H.-J.4    Liu, J.-K.5
  • 49
    • 79960112620 scopus 로고    scopus 로고
    • Autoinduction of Protein Expression
    • In; John Wiley & Sons, Inc. New York
    • Fox, B. G. and Blommel, P. G. (2001) Autoinduction of Protein Expression, In Curr. Protoc. Protein Sci.; John Wiley & Sons, Inc., New York.
    • (2001) Curr. Protoc. Protein Sci.
    • Fox, B.G.1    Blommel, P.G.2
  • 50
  • 51
    • 80053401997 scopus 로고    scopus 로고
    • Substrate Binding Modulates the Activity of Mycobacterium smegmatis G, a Flavin-Dependent Monooxygenase Involved in the Biosynthesis of Hydroxamate-Containing Siderophores
    • Robinson, R. and Sobrado, P. (2011) Substrate Binding Modulates the Activity of Mycobacterium smegmatis G, a Flavin-Dependent Monooxygenase Involved in the Biosynthesis of Hydroxamate-Containing Siderophores Biochemistry 50, 8489-8496 10.1021/bi200933h
    • (2011) Biochemistry , vol.50 , pp. 8489-8496
    • Robinson, R.1    Sobrado, P.2
  • 52
    • 84860255172 scopus 로고    scopus 로고
    • Biosynthesis of Piperazic Acid via N5-Hydroxy-Ornithine in Kutzneria spp. 744
    • Neumann, C. S., Jiang, W., Heemstra, J. R., Gontang, E. A., Kolter, R., and Walsh, C. T. (2012) Biosynthesis of Piperazic Acid via N5-Hydroxy-Ornithine in Kutzneria spp. 744 ChemBioChem 13, 972-976 10.1002/cbic.201200054
    • (2012) ChemBioChem , vol.13 , pp. 972-976
    • Neumann, C.S.1    Jiang, W.2    Heemstra, J.R.3    Gontang, E.A.4    Kolter, R.5    Walsh, C.T.6
  • 53
    • 84929378443 scopus 로고    scopus 로고
    • An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation
    • Binda, C., Robinson, R. M., Martin del Campo, J. S., Keul, N. D., Rodriguez, P. J., Robinson, H. H., Mattevi, A., and Sobrado, P. (2015) An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation J. Biol. Chem. 290, 12676-12688 10.1074/jbc.M114.629485
    • (2015) J. Biol. Chem. , vol.290 , pp. 12676-12688
    • Binda, C.1    Robinson, R.M.2    Martin Del Campo, J.S.3    Keul, N.D.4    Rodriguez, P.J.5    Robinson, H.H.6    Mattevi, A.7    Sobrado, P.8
  • 54
    • 0025293777 scopus 로고
    • Hydrogen peroxide production during experimental protein glycation
    • Jiang, Z.-Y., Woollard, A. C. S., and Wolff, S. P. (1990) Hydrogen peroxide production during experimental protein glycation FEBS Lett. 268, 69-71 10.1016/0014-5793(90)80974-N
    • (1990) FEBS Lett. , vol.268 , pp. 69-71
    • Jiang, Z.-Y.1    Woollard, A.C.S.2    Wolff, S.P.3
  • 55
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading
    • Trott, O. and Olson, A. J. (2010) AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization and multithreading J. Comput. Chem. 31, 455-461 10.1002/jcc.21334
    • (2010) J. Comput. Chem. , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 57
    • 0024147191 scopus 로고
    • High-performance liquid chromatography of siderophores from fungi
    • Konetschny-Rapp, S., Huschka, H.-G., Winkelmanne, G. n., and Jung, G. n. (1988) High-performance liquid chromatography of siderophores from fungi Biol. Met. 1, 9-17 10.1007/BF01128012
    • (1988) Biol. Met. , vol.1 , pp. 9-17
    • Konetschny-Rapp, S.1    Huschka, H.-G.2    Winkelmanne, G.N.3    Jung, G.N.4


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