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Volumn 52, Issue 35, 2013, Pages 5985-5996

Applications of small molecule probes in dissecting mechanisms of bacterial virulence and host responses

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVITY-BASED PROBE; BACTERIAL INFECTIONS; BACTERIAL PATHOGENESIS; CATALYTIC MECHANISMS; DEVELOPMENT AND APPLICATIONS; ENZYME ACTIVATION; ENZYME FUNCTIONS; GENETIC TECHNIQUES;

EID: 84883479874     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400854d     Document Type: Article
Times cited : (18)

References (84)
  • 1
    • 50649112213 scopus 로고    scopus 로고
    • Activity-based protein profiling: From enzyme chemistry to proteomic chemistry
    • Cravatt, B. F., Wright, A. T., and Kozarich, J. W. (2008) Activity-based protein profiling: From enzyme chemistry to proteomic chemistry Annu. Rev. Biochem. 77, 383-414
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 383-414
    • Cravatt, B.F.1    Wright, A.T.2    Kozarich, J.W.3
  • 2
    • 83055180536 scopus 로고    scopus 로고
    • Functional imaging of proteases: Recent advances in the design and application of substrate-based and activity-based probes
    • Edgington, L. E., Verdoes, M., and Bogyo, M. (2012) Functional imaging of proteases: Recent advances in the design and application of substrate-based and activity-based probes Curr. Opin. Chem. Biol. 15, 798-805
    • (2012) Curr. Opin. Chem. Biol. , vol.15 , pp. 798-805
    • Edgington, L.E.1    Verdoes, M.2    Bogyo, M.3
  • 3
    • 33846807650 scopus 로고    scopus 로고
    • Tagging and detection strategies for activity-based proteomics
    • Sadaghiani, A. M., Verhelst, S. H., and Bogyo, M. (2007) Tagging and detection strategies for activity-based proteomics Curr. Opin. Chem. Biol. 11, 20-28
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 20-28
    • Sadaghiani, A.M.1    Verhelst, S.H.2    Bogyo, M.3
  • 4
    • 80052137604 scopus 로고    scopus 로고
    • Molecular mechanisms of inflammasome activation during microbial infections
    • Broz, P. and Monack, D. M. (2011) Molecular mechanisms of inflammasome activation during microbial infections Immunol. Rev. 243, 174-190
    • (2011) Immunol. Rev. , vol.243 , pp. 174-190
    • Broz, P.1    Monack, D.M.2
  • 5
    • 33645805882 scopus 로고    scopus 로고
    • Self-compartmentalized bacterial proteases and pathogenesis
    • Butler, S. M., Festa, R. A., Pearce, M. J., and Darwin, K. H. (2006) Self-compartmentalized bacterial proteases and pathogenesis Mol. Microbiol. 60, 553-562
    • (2006) Mol. Microbiol. , vol.60 , pp. 553-562
    • Butler, S.M.1    Festa, R.A.2    Pearce, M.J.3    Darwin, K.H.4
  • 6
    • 81255127216 scopus 로고    scopus 로고
    • Regulated proteolysis in Gram-negative bacteria: How and when?
    • Gur, E., Biran, D., and Ron, E. Z. (2011) Regulated proteolysis in Gram-negative bacteria: How and when? Nat. Rev. Microbiol. 9, 839-848
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 839-848
    • Gur, E.1    Biran, D.2    Ron, E.Z.3
  • 7
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • Schroder, K. and Tschopp, J. (2010) The inflammasomes Cell 140, 821-832
    • (2010) Cell , vol.140 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 8
    • 79952064512 scopus 로고    scopus 로고
    • Autoproteolytic activation of bacterial toxins
    • Shen, A. (2010) Autoproteolytic activation of bacterial toxins Toxins (Basel) 2, 963-977
    • (2010) Toxins (Basel) , vol.2 , pp. 963-977
    • Shen, A.1
  • 10
    • 84865339202 scopus 로고    scopus 로고
    • Caspase-1 activity is required to bypass macrophage apoptosis upon Salmonella infection
    • Puri, A. W., Broz, P., Shen, A., Monack, D. M., and Bogyo, M. (2012) Caspase-1 activity is required to bypass macrophage apoptosis upon Salmonella infection Nat. Chem. Biol. 8, 745-747
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 745-747
    • Puri, A.W.1    Broz, P.2    Shen, A.3    Monack, D.M.4    Bogyo, M.5
  • 13
    • 35848965006 scopus 로고    scopus 로고
    • Activity-based protein profiling for the functional annotation of enzymes
    • Barglow, K. T. and Cravatt, B. F. (2007) Activity-based protein profiling for the functional annotation of enzymes Nat. Methods 4, 822-827
    • (2007) Nat. Methods , vol.4 , pp. 822-827
    • Barglow, K.T.1    Cravatt, B.F.2
  • 15
    • 0033835372 scopus 로고    scopus 로고
    • Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools
    • Greenbaum, D., Medzihradszky, K. F., Burlingame, A., and Bogyo, M. (2000) Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools Chem. Biol. 7, 569-581
    • (2000) Chem. Biol. , vol.7 , pp. 569-581
    • Greenbaum, D.1    Medzihradszky, K.F.2    Burlingame, A.3    Bogyo, M.4
  • 17
    • 33745188914 scopus 로고    scopus 로고
    • Metalloprotease inhibitors GM6001 and TAPI-0 inhibit the obligate intracellular human pathogen Chlamydia trachomatis by targeting peptide deformylase of the bacterium
    • Balakrishnan, A., Patel, B., Sieber, S. A., Chen, D., Pachikara, N., Zhong, G., Cravatt, B. F., and Fan, H. (2006) Metalloprotease inhibitors GM6001 and TAPI-0 inhibit the obligate intracellular human pathogen Chlamydia trachomatis by targeting peptide deformylase of the bacterium J. Biol. Chem. 281, 16691-16699
    • (2006) J. Biol. Chem. , vol.281 , pp. 16691-16699
    • Balakrishnan, A.1    Patel, B.2    Sieber, S.A.3    Chen, D.4    Pachikara, N.5    Zhong, G.6    Cravatt, B.F.7    Fan, H.8
  • 21
    • 71749087319 scopus 로고    scopus 로고
    • Cwp84, a surface-associated cysteine protease, plays a role in the maturation of the surface layer of Clostridium difficile
    • Kirby, J. M., Ahern, H., Roberts, A. K., Kumar, V., Freeman, Z., Acharya, K. R., and Shone, C. C. (2009) Cwp84, a surface-associated cysteine protease, plays a role in the maturation of the surface layer of Clostridium difficile J. Biol. Chem. 284, 34666-34673
    • (2009) J. Biol. Chem. , vol.284 , pp. 34666-34673
    • Kirby, J.M.1    Ahern, H.2    Roberts, A.K.3    Kumar, V.4    Freeman, Z.5    Acharya, K.R.6    Shone, C.C.7
  • 22
    • 84855821826 scopus 로고    scopus 로고
    • Novel inhibitors of surface layer processing in Clostridium difficile
    • Tam Dang, T. H., Fagan, R. P., Fairweather, N. F., and Tate, E. W. (2012) Novel inhibitors of surface layer processing in Clostridium difficile Bioorg. Med. Chem. 20, 614-621
    • (2012) Bioorg. Med. Chem. , vol.20 , pp. 614-621
    • Tam Dang, T.H.1    Fagan, R.P.2    Fairweather, N.F.3    Tate, E.W.4
  • 23
    • 0015501703 scopus 로고
    • Multiple penicillin-binding components in Bacillus subtilis, Bacillus cereus, Staphylococcus aureus, and Escherichia coli
    • Suginaka, H., Blumberg, P. M., and Strominger, J. L. (1972) Multiple penicillin-binding components in Bacillus subtilis, Bacillus cereus, Staphylococcus aureus, and Escherichia coli J. Biol. Chem. 247, 5279-5288
    • (1972) J. Biol. Chem. , vol.247 , pp. 5279-5288
    • Suginaka, H.1    Blumberg, P.M.2    Strominger, J.L.3
  • 24
    • 0016144019 scopus 로고
    • Covalent affinity chromatography of penicillin-binding components from bacterial membranes
    • Blumberg, P. M. and Strominger, J. L. (1974) Covalent affinity chromatography of penicillin-binding components from bacterial membranes Methods Enzymol. 34, 401-405
    • (1974) Methods Enzymol. , vol.34 , pp. 401-405
    • Blumberg, P.M.1    Strominger, J.L.2
  • 27
    • 55549091103 scopus 로고    scopus 로고
    • β-Lactones as specific inhibitors of ClpP attenuate the production of extracellular virulence factors of Staphylococcus aureus
    • Bottcher, T. and Sieber, S. A. (2008) β-Lactones as specific inhibitors of ClpP attenuate the production of extracellular virulence factors of Staphylococcus aureus J. Am. Chem. Soc. 130, 14400-14401
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 14400-14401
    • Bottcher, T.1    Sieber, S.A.2
  • 28
    • 47149092981 scopus 로고    scopus 로고
    • β-Lactones as privileged structures for the active-site labeling of versatile bacterial enzyme classes
    • Bottcher, T. and Sieber, S. A. (2008) β-Lactones as privileged structures for the active-site labeling of versatile bacterial enzyme classes Angew. Chem., Int. Ed. 47, 4600-4603
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 4600-4603
    • Bottcher, T.1    Sieber, S.A.2
  • 29
    • 65549130471 scopus 로고    scopus 로고
    • Structurally refined β-lactones as potent inhibitors of devastating bacterial virulence factors
    • Bottcher, T. and Sieber, S. A. (2009) Structurally refined β-lactones as potent inhibitors of devastating bacterial virulence factors ChemBioChem 10, 663-666
    • (2009) ChemBioChem , vol.10 , pp. 663-666
    • Bottcher, T.1    Sieber, S.A.2
  • 30
    • 68149125606 scopus 로고    scopus 로고
    • β-Lactones decrease the intracellular virulence of Listeria monocytogenes in macrophages
    • Bottcher, T. and Sieber, S. A. (2009) β-Lactones decrease the intracellular virulence of Listeria monocytogenes in macrophages ChemMedChem 4, 1260-1263
    • (2009) ChemMedChem , vol.4 , pp. 1260-1263
    • Bottcher, T.1    Sieber, S.A.2
  • 32
    • 53549118638 scopus 로고    scopus 로고
    • β-Lactams as selective chemical probes for the in vivo labeling of bacterial enzymes involved in cell wall biosynthesis, antibiotic resistance, and virulence
    • Staub, I. and Sieber, S. A. (2008) β-Lactams as selective chemical probes for the in vivo labeling of bacterial enzymes involved in cell wall biosynthesis, antibiotic resistance, and virulence J. Am. Chem. Soc. 130, 13400-13409
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 13400-13409
    • Staub, I.1    Sieber, S.A.2
  • 33
    • 70149092317 scopus 로고    scopus 로고
    • β-Lactam probes as selective chemical-proteomic tools for the identification and functional characterization of resistance associated enzymes in MRSA
    • Staub, I. and Sieber, S. A. (2009) β-Lactam probes as selective chemical-proteomic tools for the identification and functional characterization of resistance associated enzymes in MRSA J. Am. Chem. Soc. 131, 6271-6276
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 6271-6276
    • Staub, I.1    Sieber, S.A.2
  • 34
    • 80855133541 scopus 로고    scopus 로고
    • Vibralactone as a tool to study the activity and structure of the ClpP1P2 complex from Listeria monocytogenes
    • Zeiler, E., Braun, N., Bottcher, T., Kastenmuller, A., Weinkauf, S., and Sieber, S. A. (2011) Vibralactone as a tool to study the activity and structure of the ClpP1P2 complex from Listeria monocytogenes Angew. Chem., Int. Ed. 50, 11001-11004
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 11001-11004
    • Zeiler, E.1    Braun, N.2    Bottcher, T.3    Kastenmuller, A.4    Weinkauf, S.5    Sieber, S.A.6
  • 36
    • 84867364326 scopus 로고    scopus 로고
    • Target analysis of α-alkylidene-γ-butyrolactones in uropathogenic E. Coli
    • Kunzmann, M. H. and Sieber, S. A. (2012) Target analysis of α-alkylidene-γ-butyrolactones in uropathogenic E. coli Mol. BioSyst. 8, 3061-3067
    • (2012) Mol. BioSyst. , vol.8 , pp. 3061-3067
    • Kunzmann, M.H.1    Sieber, S.A.2
  • 37
    • 77952571663 scopus 로고    scopus 로고
    • Showdomycin as a versatile chemical tool for the detection of pathogenesis-associated enzymes in bacteria
    • Bottcher, T. and Sieber, S. A. (2010) Showdomycin as a versatile chemical tool for the detection of pathogenesis-associated enzymes in bacteria J. Am. Chem. Soc. 132, 6964-6972
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6964-6972
    • Bottcher, T.1    Sieber, S.A.2
  • 38
    • 67649863774 scopus 로고    scopus 로고
    • Cinnamic aldehyde derived probes for the active site labelling of pathogenesis associated enzymes
    • Pitscheider, M. and Sieber, S. A. (2009) Cinnamic aldehyde derived probes for the active site labelling of pathogenesis associated enzymes Chem. Commun. 3741-3743
    • (2009) Chem. Commun. , pp. 3741-3743
    • Pitscheider, M.1    Sieber, S.A.2
  • 39
    • 0033897724 scopus 로고    scopus 로고
    • Molecular characterization of the β-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling
    • Cheng, Q., Li, H., Merdek, K., and Park, J. T. (2000) Molecular characterization of the β-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling J. Bacteriol. 182, 4836-4840
    • (2000) J. Bacteriol. , vol.182 , pp. 4836-4840
    • Cheng, Q.1    Li, H.2    Merdek, K.3    Park, J.T.4
  • 40
    • 0034671524 scopus 로고    scopus 로고
    • Characterization of a β-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and β-lactamase induction
    • Votsch, W. and Templin, M. F. (2000) Characterization of a β-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and β-lactamase induction J. Biol. Chem. 275, 39032-39038
    • (2000) J. Biol. Chem. , vol.275 , pp. 39032-39038
    • Votsch, W.1    Templin, M.F.2
  • 41
    • 38349018251 scopus 로고    scopus 로고
    • Synthesis and use of mechanism-based protein-profiling probes for retaining β- D -glucosaminidases facilitate identification of Pseudomonas aeruginosa NagZ
    • Stubbs, K. A., Scaffidi, A., Debowski, A. W., Mark, B. L., Stick, R. V., and Vocadlo, D. J. (2008) Synthesis and use of mechanism-based protein-profiling probes for retaining β- d -glucosaminidases facilitate identification of Pseudomonas aeruginosa NagZ J. Am. Chem. Soc. 130, 327-335
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 327-335
    • Stubbs, K.A.1    Scaffidi, A.2    Debowski, A.W.3    Mark, B.L.4    Stick, R.V.5    Vocadlo, D.J.6
  • 42
    • 67049107914 scopus 로고    scopus 로고
    • Inactivation of the glycoside hydrolase NagZ attenuates antipseudomonal β-lactam resistance in Pseudomonas aeruginosa
    • Asgarali, A., Stubbs, K. A., Oliver, A., Vocadlo, D. J., and Mark, B. L. (2009) Inactivation of the glycoside hydrolase NagZ attenuates antipseudomonal β-lactam resistance in Pseudomonas aeruginosa Antimicrob. Agents Chemother. 53, 2274-2282
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 2274-2282
    • Asgarali, A.1    Stubbs, K.A.2    Oliver, A.3    Vocadlo, D.J.4    Mark, B.L.5
  • 43
    • 77955760680 scopus 로고    scopus 로고
    • Dichotomy of gingipains action as virulence factors: From cleaving substrates with the precision of a surgeon's knife to a meat chopper-like brutal degradation of proteins
    • Guo, Y., Nguyen, K. A., and Potempa, J. (2010) Dichotomy of gingipains action as virulence factors: From cleaving substrates with the precision of a surgeon's knife to a meat chopper-like brutal degradation of proteins Periodontol 2000 54, 15-44
    • (2010) Periodontol 2000 , vol.54 , pp. 15-44
    • Guo, Y.1    Nguyen, K.A.2    Potempa, J.3
  • 46
    • 84857790535 scopus 로고    scopus 로고
    • Clostridium difficile toxins: Mediators of inflammation
    • Shen, A. (2012) Clostridium difficile toxins: Mediators of inflammation J. Innate Immun. 4, 149-158
    • (2012) J. Innate Immun. , vol.4 , pp. 149-158
    • Shen, A.1
  • 47
    • 78649357145 scopus 로고    scopus 로고
    • Rational design of inhibitors and activity-based probes targeting Clostridium difficile virulence factor TcdB
    • Puri, A. W., Lupardus, P. J., Deu, E., Albrow, V. E., Garcia, K. C., Bogyo, M., and Shen, A. (2010) Rational design of inhibitors and activity-based probes targeting Clostridium difficile virulence factor TcdB Chem. Biol. 17, 1201-1211
    • (2010) Chem. Biol. , vol.17 , pp. 1201-1211
    • Puri, A.W.1    Lupardus, P.J.2    Deu, E.3    Albrow, V.E.4    Garcia, K.C.5    Bogyo, M.6    Shen, A.7
  • 49
    • 84858866411 scopus 로고    scopus 로고
    • TcdB from hypervirulent Clostridium difficile exhibits increased efficiency of autoprocessing
    • Lanis, J. M., Hightower, L. D., Shen, A., and Ballard, J. D. (2012) TcdB from hypervirulent Clostridium difficile exhibits increased efficiency of autoprocessing Mol. Microbiol. 84, 66-76
    • (2012) Mol. Microbiol. , vol.84 , pp. 66-76
    • Lanis, J.M.1    Hightower, L.D.2    Shen, A.3    Ballard, J.D.4
  • 50
    • 77958132074 scopus 로고    scopus 로고
    • Variations in TcdB activity and the hypervirulence of emerging strains of Clostridium difficile
    • Lanis, J. M., Barua, S., and Ballard, J. D. (2010) Variations in TcdB activity and the hypervirulence of emerging strains of Clostridium difficile PLoS Pathog. 6, e1001061
    • (2010) PLoS Pathog. , vol.6 , pp. 1001061
    • Lanis, J.M.1    Barua, S.2    Ballard, J.D.3
  • 51
    • 79952159132 scopus 로고    scopus 로고
    • Emerging inflammasome effector mechanisms
    • Lamkanfi, M. (2011) Emerging inflammasome effector mechanisms Nat. Rev. Immunol. 11, 213-220
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 213-220
    • Lamkanfi, M.1
  • 52
    • 69249140641 scopus 로고    scopus 로고
    • Lysosomes as "suicide bags" in cell death: Myth or reality?
    • Turk, B. and Turk, V. (2009) Lysosomes as "suicide bags" in cell death: Myth or reality? J. Biol. Chem. 284, 21783-21787
    • (2009) J. Biol. Chem. , vol.284 , pp. 21783-21787
    • Turk, B.1    Turk, V.2
  • 56
    • 79959572202 scopus 로고    scopus 로고
    • Chlamydia pneumoniae inhibits activated human T lymphocyte proliferation by the induction of apoptotic and pyroptotic pathways
    • Olivares-Zavaleta, N., Carmody, A., Messer, R., Whitmire, W. M., and Caldwell, H. D. (2011) Chlamydia pneumoniae inhibits activated human T lymphocyte proliferation by the induction of apoptotic and pyroptotic pathways J. Immunol. 186, 7120-7126
    • (2011) J. Immunol. , vol.186 , pp. 7120-7126
    • Olivares-Zavaleta, N.1    Carmody, A.2    Messer, R.3    Whitmire, W.M.4    Caldwell, H.D.5
  • 57
    • 84875778389 scopus 로고    scopus 로고
    • Inhibition of the Plasma-Membrane-Associated Serine Protease Cathepsin G by Mycobacterium tuberculosis Rv3364c Suppresses Caspase-1 and Pyroptosis in Macrophages
    • Danelishvili, L., Everman, J. L., McNamara, M. J., and Bermudez, L. E. (2012) Inhibition of the Plasma-Membrane-Associated Serine Protease Cathepsin G by Mycobacterium tuberculosis Rv3364c Suppresses Caspase-1 and Pyroptosis in Macrophages Front. Microbiol. 2, 281
    • (2012) Front. Microbiol. , vol.2 , pp. 281
    • Danelishvili, L.1    Everman, J.L.2    McNamara, M.J.3    Bermudez, L.E.4
  • 58
    • 84860342710 scopus 로고    scopus 로고
    • Caspase-1 has both proinflammatory and regulatory properties in Helicobacter infections, which are differentially mediated by its substrates IL-1β and IL-18
    • Hitzler, I., Sayi, A., Kohler, E., Engler, D. B., Koch, K. N., Hardt, W. D., and Muller, A. (2012) Caspase-1 has both proinflammatory and regulatory properties in Helicobacter infections, which are differentially mediated by its substrates IL-1β and IL-18 J. Immunol. 188, 3594-3602
    • (2012) J. Immunol. , vol.188 , pp. 3594-3602
    • Hitzler, I.1    Sayi, A.2    Kohler, E.3    Engler, D.B.4    Koch, K.N.5    Hardt, W.D.6    Muller, A.7
  • 59
    • 77955390094 scopus 로고    scopus 로고
    • Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella
    • Broz, P., Newton, K., Lamkanfi, M., Mariathasan, S., Dixit, V. M., and Monack, D. M. (2010) Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella J. Exp. Med. 207, 1745-1755
    • (2010) J. Exp. Med. , vol.207 , pp. 1745-1755
    • Broz, P.1    Newton, K.2    Lamkanfi, M.3    Mariathasan, S.4    Dixit, V.M.5    Monack, D.M.6
  • 60
    • 78650210802 scopus 로고    scopus 로고
    • Differential requirement for caspase-1 autoproteolysis in pathogen-induced cell death and cytokine processing
    • Broz, P., von Moltke, J., Jones, J. W., Vance, R. E., and Monack, D. M. (2010) Differential requirement for caspase-1 autoproteolysis in pathogen-induced cell death and cytokine processing Cell Host Microbe 8, 471-483
    • (2010) Cell Host Microbe , vol.8 , pp. 471-483
    • Broz, P.1    Von Moltke, J.2    Jones, J.W.3    Vance, R.E.4    Monack, D.M.5
  • 61
    • 0037372795 scopus 로고    scopus 로고
    • Role of Toll-like receptor signaling in the apoptotic response of macrophages to Yersinia infection
    • Zhang, Y. and Bliska, J. B. (2003) Role of Toll-like receptor signaling in the apoptotic response of macrophages to Yersinia infection Infect. Immun. 71, 1513-1519
    • (2003) Infect. Immun. , vol.71 , pp. 1513-1519
    • Zhang, Y.1    Bliska, J.B.2
  • 63
    • 2942537824 scopus 로고    scopus 로고
    • Targeting Rac1 by the Yersinia effector protein YopE inhibits caspase-1-mediated maturation and release of interleukin-1β
    • Schotte, P., Denecker, G., Van Den Broeke, A., Vandenabeele, P., Cornelis, G. R., and Beyaert, R. (2004) Targeting Rac1 by the Yersinia effector protein YopE inhibits caspase-1-mediated maturation and release of interleukin-1β J. Biol. Chem. 279, 25134-25142
    • (2004) J. Biol. Chem. , vol.279 , pp. 25134-25142
    • Schotte, P.1    Denecker, G.2    Van Den Broeke, A.3    Vandenabeele, P.4    Cornelis, G.R.5    Beyaert, R.6
  • 64
    • 37349046671 scopus 로고    scopus 로고
    • Macrophage activation redirects Yersinia -infected host cell death from apoptosis to caspase-1-dependent pyroptosis
    • Bergsbaken, T. and Cookson, B. T. (2007) Macrophage activation redirects Yersinia -infected host cell death from apoptosis to caspase-1-dependent pyroptosis PLoS Pathog. 3, e161
    • (2007) PLoS Pathog. , vol.3 , pp. 161
    • Bergsbaken, T.1    Cookson, B.T.2
  • 65
    • 51949097139 scopus 로고    scopus 로고
    • Caspase-1 activation in macrophages infected with Yersinia pestis KIM requires the type III secretion system effector YopJ
    • Lilo, S., Zheng, Y., and Bliska, J. B. (2008) Caspase-1 activation in macrophages infected with Yersinia pestis KIM requires the type III secretion system effector YopJ Infect. Immun. 76, 3911-3923
    • (2008) Infect. Immun. , vol.76 , pp. 3911-3923
    • Lilo, S.1    Zheng, Y.2    Bliska, J.B.3
  • 66
    • 79955776183 scopus 로고    scopus 로고
    • A Yersinia effector with enhanced inhibitory activity on the NF-κB pathway activates the NLRP3/ASC/caspase-1 inflammasome in macrophages
    • Zheng, Y., Lilo, S., Brodsky, I. E., Zhang, Y., Medzhitov, R., Marcu, K. B., and Bliska, J. B. (2011) A Yersinia effector with enhanced inhibitory activity on the NF-κB pathway activates the NLRP3/ASC/caspase-1 inflammasome in macrophages PLoS Pathog. 7, e1002026
    • (2011) PLoS Pathog. , vol.7 , pp. 1002026
    • Zheng, Y.1    Lilo, S.2    Brodsky, I.E.3    Zhang, Y.4    Medzhitov, R.5    Marcu, K.B.6    Bliska, J.B.7
  • 67
    • 33748598700 scopus 로고    scopus 로고
    • Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
    • Gurcel, L., Abrami, L., Girardin, S., Tschopp, J., and van der Goot, F. G. (2006) Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival Cell 126, 1135-1145
    • (2006) Cell , vol.126 , pp. 1135-1145
    • Gurcel, L.1    Abrami, L.2    Girardin, S.3    Tschopp, J.4    Van Der Goot, F.G.5
  • 68
    • 33845766627 scopus 로고    scopus 로고
    • Commonly used caspase inhibitors designed based on substrate specificity profiles lack selectivity
    • Berger, A. B., Sexton, K. B., and Bogyo, M. (2006) Commonly used caspase inhibitors designed based on substrate specificity profiles lack selectivity Cell Res. 16, 961-963
    • (2006) Cell Res. , vol.16 , pp. 961-963
    • Berger, A.B.1    Sexton, K.B.2    Bogyo, M.3
  • 69
    • 34547650722 scopus 로고    scopus 로고
    • All that glitters is not gold: All that FLICA binds is not caspase. A caution in data interpretation - And new opportunities
    • Darzynkiewicz, Z. and Pozarowski, P. (2007) All that glitters is not gold: All that FLICA binds is not caspase. A caution in data interpretation-and new opportunities Cytometry, Part A 71, 536-537
    • (2007) Cytometry, Part A , vol.71 , pp. 536-537
    • Darzynkiewicz, Z.1    Pozarowski, P.2
  • 72
    • 34250195275 scopus 로고    scopus 로고
    • The Nod-like receptor family member Naip5/Birc1e restricts Legionella pneumophila growth independently of caspase-1 activation
    • Lamkanfi, M., Amer, A., Kanneganti, T. D., Munoz-Planillo, R., Chen, G., Vandenabeele, P., Fortier, A., Gros, P., and Nunez, G. (2007) The Nod-like receptor family member Naip5/Birc1e restricts Legionella pneumophila growth independently of caspase-1 activation J. Immunol. 178, 8022-8027
    • (2007) J. Immunol. , vol.178 , pp. 8022-8027
    • Lamkanfi, M.1    Amer, A.2    Kanneganti, T.D.3    Munoz-Planillo, R.4    Chen, G.5    Vandenabeele, P.6    Fortier, A.7    Gros, P.8    Nunez, G.9
  • 74
    • 80053379974 scopus 로고    scopus 로고
    • Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity
    • Kofoed, E. M. and Vance, R. E. (2011) Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity Nature 477, 592-595
    • (2011) Nature , vol.477 , pp. 592-595
    • Kofoed, E.M.1    Vance, R.E.2
  • 76
    • 84856729230 scopus 로고    scopus 로고
    • Broad-specificity efflux pumps and their role in multidrug resistance of Gram-negative bacteria
    • Nikaido, H. and Pages, J. M. (2012) Broad-specificity efflux pumps and their role in multidrug resistance of Gram-negative bacteria FEMS Microbiol. Rev. 36, 340-363
    • (2012) FEMS Microbiol. Rev. , vol.36 , pp. 340-363
    • Nikaido, H.1    Pages, J.M.2
  • 77
    • 65249146929 scopus 로고    scopus 로고
    • Multidrug resistance in bacteria
    • Nikaido, H. (2009) Multidrug resistance in bacteria Annu. Rev. Biochem. 78, 119-146
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 119-146
    • Nikaido, H.1
  • 78
    • 84861864686 scopus 로고    scopus 로고
    • Activity-based probe for histidine kinase signaling
    • Wilke, K. E., Francis, S., and Carlson, E. E. (2012) Activity-based probe for histidine kinase signaling J. Am. Chem. Soc. 134, 9150-9153
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 9150-9153
    • Wilke, K.E.1    Francis, S.2    Carlson, E.E.3
  • 79
    • 40849126450 scopus 로고    scopus 로고
    • Discovery of virulence factors of pathogenic bacteria
    • Wu, H. J., Wang, A. H., and Jennings, M. P. (2008) Discovery of virulence factors of pathogenic bacteria Curr. Opin. Chem. Biol. 12, 93-101
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 93-101
    • Wu, H.J.1    Wang, A.H.2    Jennings, M.P.3
  • 81
    • 69249093873 scopus 로고    scopus 로고
    • Using small molecules to dissect mechanisms of microbial pathogenesis
    • Puri, A. W. and Bogyo, M. (2009) Using small molecules to dissect mechanisms of microbial pathogenesis ACS Chem. Biol. 4, 603-616
    • (2009) ACS Chem. Biol. , vol.4 , pp. 603-616
    • Puri, A.W.1    Bogyo, M.2
  • 84
    • 84879350060 scopus 로고    scopus 로고
    • A coupled protein and probe engineering approach for selective inhibition and activity-based probe labeling of the caspases
    • Xiao, J., Broz, P., Puri, A. W., Deu, E., Morell, M., Monack, D. M., and Bogyo, M. (2013) A coupled protein and probe engineering approach for selective inhibition and activity-based probe labeling of the caspases J. Am. Chem. Soc. 135, 9130-9138
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 9130
    • Xiao, J.1    Broz, P.2    Puri, A.W.3    Deu, E.4    Morell, M.5    Monack, D.M.6    Bogyo, M.7


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