메뉴 건너뛰기




Volumn 29, Issue 6, 2004, Pages 282-285

Stop the killer: How to inhibit the anthrax lethal factor metalloprotease

Author keywords

[No Author keywords available]

Indexed keywords

ANTHRAX TOXIN; ANTIBIOTIC AGENT; CATECHIN; EPIGALLOCATECHIN; EPIGALLOCATECHIN GALLATE; HYDROXAMIC ACID DERIVATIVE; ILOMASTAT; METALLOPROTEINASE; METALLOPROTEINASE INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE; NSC 12155; NSC 357756; NSC 369721; QUINOLINE DERIVATIVE; UNCLASSIFIED DRUG; UREA DERIVATIVE;

EID: 3242804491     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2004.04.011     Document Type: Short Survey
Times cited : (31)

References (24)
  • 3
    • 0036053928 scopus 로고    scopus 로고
    • Bioterriorism: From threat to reality
    • Atlas R.M. Bioterriorism: from threat to reality. Annu. Rev. Microbiol. 56:2002;167-185
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 167-185
    • Atlas, R.M.1
  • 5
    • 0026775916 scopus 로고
    • Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen
    • Molloy S.S., et al. Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. J. Biol. Chem. 267:1992;16396-16402
    • (1992) J. Biol. Chem. , vol.267 , pp. 16396-16402
    • Molloy, S.S.1
  • 7
    • 0037415611 scopus 로고    scopus 로고
    • Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process
    • Abrami L., et al. Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. J. Cell Biol. 160:2003;321-328
    • (2003) J. Cell Biol. , vol.160 , pp. 321-328
    • Abrami, L.1
  • 8
    • 2542509040 scopus 로고    scopus 로고
    • The vacuolar ATPase proton pump is required for the cytotoxicity of Bacillus anthracis lethal toxin
    • Menard A., et al. The vacuolar ATPase proton pump is required for the cytotoxicity of Bacillus anthracis lethal toxin. FEBS Lett. 386:1996;161-164
    • (1996) FEBS Lett. , vol.386 , pp. 161-164
    • Menard, A.1
  • 9
    • 0000947082 scopus 로고
    • Anthrax toxin edema factor: A bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells
    • Leppla S.H. Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells. Proc. Natl. Acad. Sci. U. S. A. 79:1982;3162-3166
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 3162-3166
    • Leppla, S.H.1
  • 10
    • 18244414803 scopus 로고    scopus 로고
    • Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor
    • Duesbery N.S., et al. Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor. Science. 280:1998;734-737
    • (1998) Science , vol.280 , pp. 734-737
    • Duesbery, N.S.1
  • 11
    • 0032581369 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages
    • Vitale G., et al. Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages. Biochem. Biophys. Res. Commun. 248:1998;706-711
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 706-711
    • Vitale, G.1
  • 12
    • 0034672216 scopus 로고    scopus 로고
    • Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor
    • Vitale G., et al. Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor. Biochem. J. 352:2000;739-745
    • (2000) Biochem. J. , vol.352 , pp. 739-745
    • Vitale, G.1
  • 13
    • 0035829518 scopus 로고    scopus 로고
    • Crystal structure of the anthrax lethal factor
    • Pannifer A.D., et al. Crystal structure of the anthrax lethal factor. Nature. 414:2001;229-233
    • (2001) Nature , vol.414 , pp. 229-233
    • Pannifer, A.D.1
  • 14
    • 0034997845 scopus 로고    scopus 로고
    • Mitogen-activated protein (MAP) kinase pathways: Regulation and physiological functions
    • Pearson G., et al. Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions. Endocr. Rev. 22:2001;153-183
    • (2001) Endocr. Rev. , vol.22 , pp. 153-183
    • Pearson, G.1
  • 15
    • 0037400611 scopus 로고    scopus 로고
    • Molecular recognitions in the MAP kinase cascades
    • Tanoue T., Nishida E. Molecular recognitions in the MAP kinase cascades. Cell Signal. 15:2003;455-462
    • (2003) Cell Signal. , vol.15 , pp. 455-462
    • Tanoue, T.1    Nishida, E.2
  • 16
    • 0037954572 scopus 로고    scopus 로고
    • Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions
    • Biondi R.M., Nebreda A.R. Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions. Biochem. J. 372:2003;1-13
    • (2003) Biochem. J. , vol.372 , pp. 1-13
    • Biondi, R.M.1    Nebreda, A.R.2
  • 17
    • 0036468526 scopus 로고    scopus 로고
    • Quickening the pace of anthrax research: Three advances point towards possible therapies
    • Chaudry G.J., et al. Quickening the pace of anthrax research: three advances point towards possible therapies. Trends Microbiol. 10:2002;58-62
    • (2002) Trends Microbiol. , vol.10 , pp. 58-62
    • Chaudry, G.J.1
  • 18
    • 0037173617 scopus 로고    scopus 로고
    • Screening inhibitors of anthrax lethal factor
    • Tonello F., et al. Screening inhibitors of anthrax lethal factor. Nature. 418:2002;386
    • (2002) Nature , vol.418 , pp. 386
    • Tonello, F.1
  • 19
    • 0037076271 scopus 로고    scopus 로고
    • A peptide-based fluorescence resonance energy transfer assay for Bacillus anthracis lethal factor protease
    • Cummings R.T., et al. A peptide-based fluorescence resonance energy transfer assay for Bacillus anthracis lethal factor protease. Proc. Natl. Acad. Sci. U. S. A. 99:2002;6603-6606
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 6603-6606
    • Cummings, R.T.1
  • 20
    • 0037493019 scopus 로고    scopus 로고
    • Structure-based inhibitor discovery against adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough
    • Soelaiman S., et al. Structure-based inhibitor discovery against adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough. J. Biol. Chem. 278:2003;25990-25997
    • (2003) J. Biol. Chem. , vol.278 , pp. 25990-25997
    • Soelaiman, S.1
  • 21
    • 0347192782 scopus 로고    scopus 로고
    • The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor
    • Turk B.E., et al. The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor. Nat. Struct. Mol. Biol. 11:2004;60-66
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 60-66
    • Turk, B.E.1
  • 22
    • 10744223044 scopus 로고    scopus 로고
    • Identification of small molecule inhibitors of anthrax lethal factor
    • Panchal R.G., et al. Identification of small molecule inhibitors of anthrax lethal factor. Nat. Struct. Mol. Biol. 11:2004;67-72
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 67-72
    • Panchal, R.G.1
  • 23
    • 0034387741 scopus 로고    scopus 로고
    • Novel approaches to targeting neuropeptide systems
    • Roques B.P. Novel approaches to targeting neuropeptide systems. Trends Pharmacol. Sci. 21:2000;475-483
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 475-483
    • Roques, B.P.1
  • 24
    • 2442478677 scopus 로고    scopus 로고
    • Potent inhibitors of anthrax lethal factor from green tea
    • Dell'Aica I., et al. Potent inhibitors of anthrax lethal factor from green tea. EMBO Rep. 5:2004;418-422
    • (2004) EMBO Rep. , vol.5 , pp. 418-422
    • Dell'Aica, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.