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Volumn 58, Issue 13, 2015, Pages 5208-5217

Fragment-Based Exploration of Binding Site Flexibility in Mycobacterium tuberculosis BioA

Author keywords

[No Author keywords available]

Indexed keywords

AMINOTRANSFERASE; BIOA PROTEIN; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN; BIOA PROTEIN, BACTERIA; MOLECULAR LIBRARY;

EID: 84937510652     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/acs.jmedchem.5b00092     Document Type: Article
Times cited : (30)

References (41)
  • 1
    • 77952326903 scopus 로고    scopus 로고
    • The population dynamics and control of tuberculosis
    • Dye, C.; Williams, B. G. The population dynamics and control of tuberculosis Science 2010, 328, 856-861
    • (2010) Science , vol.328 , pp. 856-861
    • Dye, C.1    Williams, B.G.2
  • 2
    • 84894198937 scopus 로고    scopus 로고
    • World Health Organization: Geneva
    • Global Tuberculosis Report 2014; World Health Organization: Geneva, 2014.
    • (2014) Global Tuberculosis Report 2014
  • 3
    • 0033812380 scopus 로고    scopus 로고
    • Role of individual drugs in the chemotherapy of tuberculosis
    • Mitchison, D. A. Role of individual drugs in the chemotherapy of tuberculosis Int. J. Tubercosis Lung Dis. 2000, 4, 796-806
    • (2000) Int. J. Tubercosis Lung Dis. , vol.4 , pp. 796-806
    • Mitchison, D.A.1
  • 4
    • 0022335191 scopus 로고
    • The action of antituberculosis drugs in short-course chemotherapy
    • Mitchison, D. A. The action of antituberculosis drugs in short-course chemotherapy Tubercle 1985, 66, 219-225
    • (1985) Tubercle , vol.66 , pp. 219-225
    • Mitchison, D.A.1
  • 6
    • 84902208513 scopus 로고    scopus 로고
    • Multidrug-resistant and extensively drug-resistant tuberculosis: A review of current concepts and future challenges
    • Günther, G. Multidrug-resistant and extensively drug-resistant tuberculosis: a review of current concepts and future challenges Clin. Med. 2014, 14, 279-285
    • (2014) Clin. Med. , vol.14 , pp. 279-285
    • Günther, G.1
  • 7
    • 84881367368 scopus 로고    scopus 로고
    • A medicinal chemists' guide to the unique difficulties of lead optimization for tuberculosis
    • Dartois, V.; Barry, C. E., III. A medicinal chemists' guide to the unique difficulties of lead optimization for tuberculosis Bioorg. Med. Chem. Lett. 2013, 23, 4741-4750
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 4741-4750
    • Dartois, V.1    Barry, C.E.2
  • 8
    • 0024315260 scopus 로고
    • The mechanism of biotin-dependent enzymes
    • Knowles, J. R. The mechanism of biotin-dependent enzymes Annu. Rev. Biochem. 1989, 58, 195-221
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 195-221
    • Knowles, J.R.1
  • 9
    • 0023662690 scopus 로고
    • Determination of free biotin in plasma by liquid chromatography with fluorimetric detection
    • Hayakawa, K.; Oizumi, J. Determination of free biotin in plasma by liquid chromatography with fluorimetric detection J. Chromatogr. 1987, 413, 247-250
    • (1987) J. Chromatogr. , vol.413 , pp. 247-250
    • Hayakawa, K.1    Oizumi, J.2
  • 10
    • 0242268400 scopus 로고    scopus 로고
    • Genetic requirements for mycobacterial survival during infection
    • Sassetti, C. M.; Rubin, E. J. Genetic requirements for mycobacterial survival during infection Proc. Natl. Acad. Sci. U. S. A. 2003, 100, 12989-12994
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 12989-12994
    • Sassetti, C.M.1    Rubin, E.J.2
  • 11
    • 80955133079 scopus 로고    scopus 로고
    • Biotin biosynthesis in Mycobacterium tuberculosis: Physiology, biochemistry and molecular intervention
    • Salaemae, W.; Azhar, A.; Booker, G. W.; Polyak, S. W. Biotin biosynthesis in Mycobacterium tuberculosis: physiology, biochemistry and molecular intervention Protein Cell 2011, 2, 691-695
    • (2011) Protein Cell , vol.2 , pp. 691-695
    • Salaemae, W.1    Azhar, A.2    Booker, G.W.3    Polyak, S.W.4
  • 12
    • 33749421509 scopus 로고    scopus 로고
    • 7,8-Diaminoperlargonic acid aminotransferase from Mycobacterium tuberculosis, a potential therapeutic target. Characterization and inhibition studies
    • Mann, S.; Ploux, O. 7,8-Diaminoperlargonic acid aminotransferase from Mycobacterium tuberculosis, a potential therapeutic target. Characterization and inhibition studies FEBS J. 2006, 273, 4778-4789
    • (2006) FEBS J. , vol.273 , pp. 4778-4789
    • Mann, S.1    Ploux, O.2
  • 15
    • 0016789486 scopus 로고
    • Studies of the mode of action of amiclenomycin
    • Hotta, K.; Kitahara, T.; Okami, Y. Studies of the mode of action of amiclenomycin J. Antibiot. 1975, 28, 222-228
    • (1975) J. Antibiot. , vol.28 , pp. 222-228
    • Hotta, K.1    Kitahara, T.2    Okami, Y.3
  • 16
    • 0037044734 scopus 로고    scopus 로고
    • Structural basis for the inhibition of the biosynthesis of biotin by the antibiotic amiclenomycin
    • Sandmark, J.; Mann, S.; Marquet, A.; Schneider, G. Structural basis for the inhibition of the biosynthesis of biotin by the antibiotic amiclenomycin J. Biol. Chem. 2002, 277, 43352-43358
    • (2002) J. Biol. Chem. , vol.277 , pp. 43352-43358
    • Sandmark, J.1    Mann, S.2    Marquet, A.3    Schneider, G.4
  • 18
    • 77955234669 scopus 로고    scopus 로고
    • Structural characterization of the Mycobacterium tuberculosis biotin biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin synthetase
    • Dey, S.; Lane, J. M.; Lee, R. E.; Rubin, E. J.; Sacchettini, J. C. Structural characterization of the Mycobacterium tuberculosis biotin biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin synthetase Biochemistry 2010, 49, 6746-6760
    • (2010) Biochemistry , vol.49 , pp. 6746-6760
    • Dey, S.1    Lane, J.M.2    Lee, R.E.3    Rubin, E.J.4    Sacchettini, J.C.5
  • 21
    • 84888004411 scopus 로고    scopus 로고
    • Metabolic suppression identifies new antibacterial inhibitors under nutrient limitation
    • Zlitni, S.; Ferruccio, L. F.; Brown, E. D. Metabolic suppression identifies new antibacterial inhibitors under nutrient limitation Nature Chem. Biol. 2013, 9, 796-804
    • (2013) Nature Chem. Biol. , vol.9 , pp. 796-804
    • Zlitni, S.1    Ferruccio, L.F.2    Brown, E.D.3
  • 22
    • 84896701988 scopus 로고    scopus 로고
    • Inhibition of Mycobacterium tuberculosis transaminase BioA by aryl hydrazines and hydrazides
    • Dai, R.; Wilson, D. J.; Geders, T. W.; Aldrich, C. C.; Finzel, B. C. Inhibition of Mycobacterium tuberculosis transaminase BioA by aryl hydrazines and hydrazides ChemBioChem 2014, 15, 575-586
    • (2014) ChemBioChem , vol.15 , pp. 575-586
    • Dai, R.1    Wilson, D.J.2    Geders, T.W.3    Aldrich, C.C.4    Finzel, B.C.5
  • 24
    • 84856935181 scopus 로고    scopus 로고
    • Introduction to fragment-based drug discovery
    • Erlanson, D. A. Introduction to fragment-based drug discovery Top Curr. Chem. 2012, 317, 1-32
    • (2012) Top Curr. Chem. , vol.317 , pp. 1-32
    • Erlanson, D.A.1
  • 25
  • 26
    • 33947464286 scopus 로고
    • Pyridoxal Catalysis of Non-enzymatic Transamination in Ethanol Solution1
    • Matsuo, Y. Pyridoxal Catalysis of Non-enzymatic Transamination in Ethanol Solution1 J. Am. Chem. Soc. 1957, 79, 2016-2019
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 2016-2019
    • Matsuo, Y.1
  • 27
    • 0023918315 scopus 로고
    • Schiff bases of pyridoxal 5′-phosphate with Tris and glycine
    • Mitra, J.; Metzler, D. Schiff bases of pyridoxal 5′-phosphate with Tris and glycine Biochim. Biophys. Acta, Gen. Subj. 1988, 965, 93-96
    • (1988) Biochim. Biophys. Acta, Gen. Subj. , vol.965 , pp. 93-96
    • Mitra, J.1    Metzler, D.2
  • 28
    • 84862516771 scopus 로고    scopus 로고
    • Use of differential scanning fluorimetry to optimize the purification and crystallization of PLP-dependent enzymes
    • Geders, T. W.; Gustafson, K.; Finzel, B. C. Use of differential scanning fluorimetry to optimize the purification and crystallization of PLP-dependent enzymes Acta Crystallographr., Sect. F: Struct. Biol. Cryst. Commun. 2012, 68, 596-600
    • (2012) Acta Crystallographr., Sect. F: Struct. Biol. Cryst. Commun. , vol.68 , pp. 596-600
    • Geders, T.W.1    Gustafson, K.2    Finzel, B.C.3
  • 31
    • 80054911951 scopus 로고    scopus 로고
    • LigPlot+: Multiple ligand-protein interaction diagrams for drug discovery
    • Laskowski, R. A.; Swindells, M. B. LigPlot+: multiple ligand-protein interaction diagrams for drug discovery J. Chem. Inf. Model. 2011, 51, 2778-2786
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 2778-2786
    • Laskowski, R.A.1    Swindells, M.B.2
  • 32
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • Niesen, F. H.; Berglund, H.; Vedadi, M. The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability Nature Protoc. 2007, 2, 2212-2221
    • (2007) Nature Protoc. , vol.2 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3


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