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Volumn 67, Issue 9, 2014, Pages 671-676

Identification of anti-tuberculosis agents that target the cell-division protein FtsZ

Author keywords

[No Author keywords available]

Indexed keywords

297F; ANTINEOPLASTIC AGENT; BACTERICIDE; FTSZ PROTEIN; GUANOSINE TRIPHOSPHATASE; HYDROLASE INHIBITOR; ISONIAZID; LEVOFLOXACIN; POLYMER; RIFAMPICIN; TUBERCULOSTATIC AGENT; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CYTOSKELETON PROTEIN; FTSZ PROTEIN, BACTERIA;

EID: 84921743804     PISSN: 00218820     EISSN: 18811469     Source Type: Journal    
DOI: 10.1038/ja.2014.89     Document Type: Article
Times cited : (28)

References (31)
  • 1
    • 84873103676 scopus 로고    scopus 로고
    • WHO and the future of disease control programmes
    • Dye, C. et al. WHO and the future of disease control programmes. Lancet 381, 413-418 (2013).
    • (2013) Lancet , vol.381 , pp. 413-418
    • Dye, C.1
  • 2
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • Lowe, J. & Amos, L. A. Crystal structure of the bacterial cell-division protein FtsZ. Nature 391, 203-206 (1998).
    • (1998) Nature , vol.391 , pp. 203-206
    • Lowe, J.1    Amos, L.A.2
  • 3
    • 0036268368 scopus 로고    scopus 로고
    • Immediate GTP hydrolysis upon FtsZ polymerization
    • Scheffers, D. J. & Driessen, A. J. Immediate GTP hydrolysis upon FtsZ polymerization. Mol. Microbiol. 43, 1517-1521 (2002).
    • (2002) Mol. Microbiol. , vol.43 , pp. 1517-1521
    • Scheffers, D.J.1    Driessen, A.J.2
  • 4
    • 0042357108 scopus 로고    scopus 로고
    • Assembly of archaeal cell division protein FtsZ and a GTPase-inactive mutant into double-stranded filaments
    • Oliva, M. A. et al. Assembly of archaeal cell division protein FtsZ and a GTPase-inactive mutant into double-stranded filaments. J. Biol. Chem. 278, 33562-33570 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 33562-33570
    • Oliva, M.A.1
  • 5
    • 0242693139 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial cell division protein FtsZ: Poised at the edge of stability
    • Romberg, L. & Levin, P. A. Assembly dynamics of the bacterial cell division protein FtsZ: poised at the edge of stability. Annu. Rev. Microbiol. 57, 125-154 (2003).
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 125-154
    • Romberg, L.1    Levin, P.A.2
  • 6
    • 0037783310 scopus 로고    scopus 로고
    • The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway
    • Bernhardt, T. G. & de Boer, P. A. The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway. Mol. Microbiol. 48, 1171-1182 (2003).
    • (2003) Mol. Microbiol. , vol.48 , pp. 1171-1182
    • Bernhardt, T.G.1    De Boer, P.A.2
  • 7
    • 70349762063 scopus 로고    scopus 로고
    • Novel compound with potential of an antibacterial drug targets FtsZ protein
    • Dasgupta, D. Novel compound with potential of an antibacterial drug targets FtsZ protein. Biochem. J. 423, e1-e3 (2009).
    • (2009) Biochem. J. , vol.423 , pp. e1-e3
    • Dasgupta, D.1
  • 8
    • 4444349738 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis FtsZ reveals unexpected, G protein-like conformational switches
    • Leung, A. K. et al. Structure of Mycobacterium tuberculosis FtsZ reveals unexpected, G protein-like conformational switches. J. Mol. Biol. 342, 953-970 (2004).
    • (2004) J. Mol. Biol. , vol.342 , pp. 953-970
    • Leung, A.K.1
  • 9
    • 70449640183 scopus 로고    scopus 로고
    • Differential assembly properties of Escherichia coli FtsZ and Mycobacterium tuberculosis FtsZ: An analysis using divalent calcium
    • Jaiswal, R. & Panda, D. Differential assembly properties of Escherichia coli FtsZ and Mycobacterium tuberculosis FtsZ: an analysis using divalent calcium. J. Biochem. 146, 733-742 (2009).
    • (2009) J. Biochem. , vol.146 , pp. 733-742
    • Jaiswal, R.1    Panda, D.2
  • 10
    • 33750376659 scopus 로고    scopus 로고
    • The prokaryotic cytoskeleton: A putative target for inhibitors and antibiotics?
    • Vollmer, W. The prokaryotic cytoskeleton: a putative target for inhibitors and antibiotics? Appl. Microbiol. Biotechnol. 73, 37-47 (2006).
    • (2006) Appl. Microbiol. Biotechnol. , vol.73 , pp. 37-47
    • Vollmer, W.1
  • 11
    • 39749130244 scopus 로고    scopus 로고
    • Curcumin inhibits FtsZ assembly: An attractive mechanism for its antibacterial activity
    • Rai, D., Singh, J. K., Roy, N. & Panda, D. Curcumin inhibits FtsZ assembly: an attractive mechanism for its antibacterial activity. Biochem. J. 410, 147-155 (2008).
    • (2008) Biochem. J. , vol.410 , pp. 147-155
    • Rai, D.1    Singh, J.K.2    Roy, N.3    Panda, D.4
  • 13
    • 34147136107 scopus 로고    scopus 로고
    • Totarol inhibits bacterial cytokinesis by perturbing the assembly dynamics of FtsZ
    • Jaiswal, R., Beuria, T. K., Mohan, R., Mahajan, S. K. & Panda, D. Totarol inhibits bacterial cytokinesis by perturbing the assembly dynamics of FtsZ. Biochemistry 46, 4211-4220 (2007).
    • (2007) Biochemistry , vol.46 , pp. 4211-4220
    • Jaiswal, R.1    Beuria, T.K.2    Mohan, R.3    Mahajan, S.K.4    Panda, D.5
  • 14
    • 80052708671 scopus 로고    scopus 로고
    • Limitations in the use of fluorescein diacetate/propidium iodide (FDA/PI) and cell permeable nucleic acid stains for viability measurements of isolated islets of langerhans
    • Boyd, V., Cholewa, O. M. & Papas, K. K. Limitations in the use of fluorescein diacetate/propidium iodide (FDA/PI) and cell permeable nucleic acid stains for viability measurements of isolated islets of langerhans. Curr. Trends Biotechnol. Pharm 2, 66-84 (2008).
    • (2008) Curr. Trends Biotechnol. Pharm , vol.2 , pp. 66-84
    • Boyd, V.1    Cholewa, O.M.2    Papas, K.K.3
  • 15
    • 0036791627 scopus 로고    scopus 로고
    • New (and not so new) antibacterial targets-from where and when will the novel drugs come?
    • Projan, S. J. New (and not so new) antibacterial targets-from where and when will the novel drugs come? Curr. Opin. Pharmacol. 2, 513-522 (2002).
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 513-522
    • Projan, S.J.1
  • 16
    • 0031924531 scopus 로고    scopus 로고
    • FtsZ dynamics during the division cycle of live Escherichia coli cells
    • Sun, Q. & Margolin, W. FtsZ dynamics during the division cycle of live Escherichia coli cells. J. Bacteriol. 180, 2050-2056 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 2050-2056
    • Sun, Q.1    Margolin, W.2
  • 17
    • 68549092791 scopus 로고    scopus 로고
    • Targeting FtsZ for antibacterial therapy: A promising avenue
    • Kapoor, S. & Panda, D. Targeting FtsZ for antibacterial therapy: a promising avenue. Expert. Opin. Ther. Targets 13, 1037-1051 (2009).
    • (2009) Expert. Opin. Ther. Targets , vol.13 , pp. 1037-1051
    • Kapoor, S.1    Panda, D.2
  • 18
    • 77956053743 scopus 로고    scopus 로고
    • Discovery of anti-TB agents that target the cell-division protein FtsZ
    • Kumar, K. et al. Discovery of anti-TB agents that target the cell-division protein FtsZ. Future Med. Chem. 2, 1305-1323 (2010).
    • (2010) Future Med. Chem. , vol.2 , pp. 1305-1323
    • Kumar, K.1
  • 19
    • 0242582382 scopus 로고    scopus 로고
    • Discovery of a small molecule that inhibits cell division by blocking FtsZ, a novel therapeutic target of antibiotics
    • Wang, J. et al. Discovery of a small molecule that inhibits cell division by blocking FtsZ, a novel therapeutic target of antibiotics. J. Biol. Chem. 278, 44424-44428 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 44424-44428
    • Wang, J.1
  • 20
    • 0034961176 scopus 로고    scopus 로고
    • (+)-Totarol from Chamaecyparis nootkatensis and activity against Mycobacterium tuberculosis
    • Constantine, G. H., Karchesy, J. J., Franzblau, S. G. & LaFleur, L. E. (+)-Totarol from Chamaecyparis nootkatensis and activity against Mycobacterium tuberculosis. Fitoterapia 72, 572-574 (2001).
    • (2001) Fitoterapia , vol.72 , pp. 572-574
    • Constantine, G.H.1    Karchesy, J.J.2    Franzblau, S.G.3    LaFleur, L.E.4
  • 21
    • 0038610624 scopus 로고    scopus 로고
    • Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ
    • Cordell, S. C, Robinson, E. J. & Lowe, J. Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ. Proc. Natl Acad. Sci. USA 100, 7889-7894 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 7889-7894
    • Cordell, S.C.1    Robinson, E.J.2    Lowe, J.3
  • 22
    • 0033917123 scopus 로고    scopus 로고
    • Slow polymerization of Mycobacterium tuberculosis FtsZ
    • White, E. L. et al. Slow polymerization of Mycobacterium tuberculosis FtsZ. J. Bacteriol. 182, 4028-4034 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 4028-4034
    • White, E.L.1
  • 23
    • 29444442409 scopus 로고    scopus 로고
    • Synthesis of antimicrobial natural products targeting FtsZ: (+/-) - Dichamanetin and (+/-)-2'-hydroxy-5'-benzylisouvarinol-B
    • Urgaonkar, S. et al. Synthesis of antimicrobial natural products targeting FtsZ: (+/-) - dichamanetin and (+/-)-2'-hydroxy-5'-benzylisouvarinol-B. Org. Lett. 7, 5609-5612 (2005).
    • (2005) Org. Lett. , vol.7 , pp. 5609-5612
    • Urgaonkar, S.1
  • 24
    • 4143110291 scopus 로고    scopus 로고
    • Targeting cell division: Small-molecule inhibitors of FtsZ GTPase perturb cytokinetic ring assembly and induce bacterial lethality
    • Margalit, D. N. et al. Targeting cell division: small-molecule inhibitors of FtsZ GTPase perturb cytokinetic ring assembly and induce bacterial lethality. Proc. Natl Acad. Sci. USA 101, 11821-11826 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 11821-11826
    • Margalit, D.N.1
  • 25
    • 0037386678 scopus 로고    scopus 로고
    • A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli
    • Geissler, B., Elraheb, D. & Margolin, W. A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli. Proc. Natl Acad. Sci. USA 100, 4197-4202 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 4197-4202
    • Geissler, B.1    Elraheb, D.2    Margolin, W.3
  • 26
    • 84861151969 scopus 로고    scopus 로고
    • FtsA forms actin-like protofilaments
    • Szwedziak, P., Wang, Q., Freund, S. M. & Lowe, J. FtsA forms actin-like protofilaments. EMBO J. 31, 2249-2260 (2012).
    • (2012) EMBO J. , vol.31 , pp. 2249-2260
    • Szwedziak, P.1    Wang, Q.2    Freund, S.M.3    Lowe, J.4
  • 27
    • 10044283085 scopus 로고    scopus 로고
    • Functional analysis of the cell division protein FtsW of Escherichia coli
    • Pastoret, S. et al. Functional analysis of the cell division protein FtsW of Escherichia coli. J. Bacteriol. 186, 8370-8379 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 8370-8379
    • Pastoret, S.1
  • 28
    • 0037022642 scopus 로고    scopus 로고
    • Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching
    • Stricker, J., Maddox, P., Salmon, E. D. & Erickson, H. P. Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. Proc. Natl Acad. Sci. USA 99, 3171-3175 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 3171-3175
    • Stricker, J.1    Maddox, P.2    Salmon, E.D.3    Erickson, H.P.4
  • 29
    • 29244432515 scopus 로고    scopus 로고
    • Sanguinarine blocks cytokinesis in bacteria by inhibiting FtsZ assembly and bundling
    • Beuria, T. K., Santra, M. K. & Panda, D. Sanguinarine blocks cytokinesis in bacteria by inhibiting FtsZ assembly and bundling. Biochemistry 44, 16584-16593 (2005).
    • (2005) Biochemistry , vol.44 , pp. 16584-16593
    • Beuria, T.K.1    Santra, M.K.2    Panda, D.3
  • 30
    • 77649191871 scopus 로고    scopus 로고
    • Microtubules and resistance to tubulin-binding agents
    • Kavallaris, M. Microtubules and resistance to tubulin-binding agents. Nat. Rev. Cancer 10, 194-204 (2010).
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 194-204
    • Kavallaris, M.1
  • 31
    • 79953200773 scopus 로고    scopus 로고
    • Association of seropositivity for influenza and coronaviruses with history of mood disorders and suicide attempts
    • Okusaga, O. et al. Association of seropositivity for influenza and coronaviruses with history of mood disorders and suicide attempts. J. Affect. Disord. 130, 220-225 (2011).
    • (2011) J. Affect. Disord. , vol.130 , pp. 220-225
    • Okusaga, O.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.