Proteomic and Morphologic Evidence for Taurine-5-Bromosalicylaldehyde Schiff Base as an Efficient Anti-Mycobacterial Drug

키워드

참고문헌 (32)

1. "GLOBAL TUBERCULOSIS REPORT 2018" (2018)[URL]
2. Rîmbu C, "Antibacterial activity of Pd(II) complexes with salicylaldehyde-amino acids Schiff bases ligands", Chem. Pharm. Bull. (Tokyo), 62, pp.12~15 (2014)
3. Chaudhary NK, "Metal complexes of a novel schiff base based on penicillin: characterization, molecular modeling, and antibacterial activity study", Bioinorg. Chem. Appl, 2017, pp.6927675~ (2017)
4. Siddappa K, "Synthesis, spectroscopic characterization, and biological evaluation studies of 5bromo-3-(((hydroxy-2-methylquinolin-7-yl)methylene)hydrazono) indolin-2-one and its metal (II) complexes", Bioinorg. Chem. Appl, 2014, pp.483282~ (2014)
5. Andiappan K, "In vitro cytotoxicity activity of novel Schiff base ligand-lanthanide complexes", Sci. Rep, 8(1), pp.3054~ (2018)
6. Zhang X, "Induction of tumor cell apoptosis by taurine Schiff base copper complex is associated with the inhibition of proteasomal activity", Int. J. Mol. Med, 22, pp.677~682 (2008)
7. Li L, "DNA binding, DNA cleavage and BSA interaction of a mixed-ligand copper(II)complex with taurine Schiff base and 1, 10-phenanthroline", J. Photochem. Photobiol. B, 125, pp.56~62 (2013)
8. Ruqiang Yuan, "In Vitro Activity of Taurine-5-Bromosalicylaldehyde Schiff Base Against Planktonic and Biofilm Cultures of Methicillin-Resistant Staphylococcus aureus", Journal of Microbiology and Biotechnology, 24(8), pp.1059~1064 (2014), 한국미생물·생명공학회[DOI]
9. Zhang W, "Expression, essentiality, and a microtiter plate assay for mycobacterial GlmU, the bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase", Int. J. Biochem. Cell Biol, 40, pp.2560~2571 (2008)
10. Chen Y, "Deficiency of D-alanyl-D-alanine ligase A attenuated cell division and greatly altered the proteome of Mycobacterium smegmatis", MicrobiologyOpen, 3, pp.e819~ (2019)
11. Yang S, "The biological properties and potential interacting proteins of DalanylD-alanine ligase A from Mycobacterium tuberculosis", Molecules, 23, pp.E324~ (2018)
12. Marland Z, "Expression, purification, crystallization and preliminary X-ray diffraction analysis of an essential lipoprotein implicated in cell-wall biosynthesis in Mycobacteria", Acta crystallogr. Sec. F, Struct. Biol. Cryst. Commun, 61, pp.1081~1083 (2005)
13. Pan F, "Cell wall core galactofuran synthesis is essential for growth of mycobacteria", J. Bacteriol, 183, pp.3991~3998 (2001)
14. Kieser KJ, "Peptidoglycan synthesis in Mycobacterium tuberculosis is organized into networks with varying drug susceptibility", Proc. Nat. Acad. Sci. USA, 112, pp.13087~13092 (2015)
15. Rombouts Y, "Exposure of mycobacteria to cell wallinhibitory drugs decreases production of arabinoglycerolipid related to Mycolyl-arabinogalactan-peptidoglycan metabolism", J. Biol. Chem, 287, pp.11060~11069 (2012)
16. Alderwick LJ, "The mycobacterial cell wall--peptidoglycan and arabinogalactan", Cold Spring Harb. Perspect. Med, 5, pp.a021113~ (2015)
17. Jankute M, "Assembly of the mycobacterial cell wall", Ann. Rev. Microbiol, 69, pp.405~423 (2015)
18. Lewis K, "Programmed death in bacteria", Microbiol. Mol. Biol. Rev, 64, pp.503~514 (2000)
19. Tanouchi Y, "Programmed cell death in bacteria and implications for antibiotic therapy", Trends Microbiol, 21, pp.265~270 (2013)
20. Peters NT, "A fail-safe mechanism in the septal ring assembly pathway generated by the sequential recruitment of cell separation amidases and their activators", J. Bacteriol, 193, pp.4973~4983 (2011)
21. Yang DC, "A conformational switch controls cell wall-remodelling enzymes required for bacterial cell division", Mol. Microbiol, 85, pp.768~781 (2012)
22. Chauviac F-X, "Crystal structure of reduced MsAcg, a putative nitroreductase from mycobacterium smegmatisand a close homologue of mycobacterium tuberculosis Acg", J. Biol. Chem, 287, pp.44372~44383 (2012)
23. Pitsawong W, "Mechanism-informed refinement reveals altered substrate-binding mode for catalytically competent nitroreductase", Structure, 25, pp.978~987 (2017)
24. Cortial S, "NADH oxidase activity of Bacillus subtilis nitroreductase NfrA1 : insight into its biological role", FEBS Lett, 584, pp.3916~3922 (2010)
25. Hektor HJ, "Identification of a magnesium-dependent NAD(P)(H)-binding domain in the nicotinoprotein methanol dehydrogenase from Bacillus methanolicus", J. Biol. Chem, 277, pp.46966~46973 (2002)
26. Liu H, "Novel TetR family transcriptional factor regulates expression of multiple transport-related genes and affects rifampicin resistance in Mycobacterium smegmatis", Sci. Rep, 6, pp.27489~ (2016)
27. Titgemeyer F, "A genomic view of sugar transport in Mycobacterium smegmatis and Mycobacterium tuberculosis", J. Bacteriol, 189, pp.5903~5915 (2007)
28. Valente W, "A Kinetic Study of In vitro lysis of mycobacterium smegmatis", Chem. Eng. Sci, 64, pp.1944~1952 (2009)
29. Agrawal P, "Use of Mycobacterium smegmatis deficient in ADP-ribosyltransferase as surrogate for Mycobacterium tuberculosis in drug testing and mutation analysis", PLoS One, 10, pp.e0122076~ (2015)
30. Namouchi A, "Phenotypic and genomic comparison of Mycobacterium aurum and surrogate model species to Mycobacterium tuberculosis : implications for drug discovery", BMC Genomics, 18(1), pp.530~ (2017)
31. Verma A, "Mycobacterium tuberculosis rrn promoters : differential usage and growth rate-dependent control", J. Bacteriol, 181, pp.4326~4333 (1999)
32. Manca C, "Mycobacterium tuberculosis catalase and peroxidase activities and resistance to oxidative killing in human monocytes in vitro", Infect. Immun, 67, pp.74~79 (1999)

관련 논문AI추천