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Volumn 21, Issue 2, 2013, Pages 100-109

Mycobacterium tuberculosis-secreted phosphatases: From pathogenesis to targets for TB drug development

Author keywords

Mycobacteria; Phosphatase; PtpA; PtpB; SapM; Tuberculosis

Indexed keywords

2 OXO 1,2 DIHYDROBENZO[CD]INDOLE 6 SULFONAMIDE; BENZOFURAN SALICYLATE; BRUNSVICAMIDE DERIVATIVE; CHALCONE DERIVATIVE; DIFLUOROMETHYLPHOSPHONIC ACID; HYDROXYPYRROLE BENZOIC ACID DERIVATIVE; INDOLIN 2 ON 3 SPIROTHIAZOLIDINONE; INDOLIZINE DERIVATIVE; INDOLOQUINOLIZIDINE DERIVATIVE; ISOTHIAZOLIDINONE; ISOXAZOLE AZIDE DERIVATIVE; ISOXAZOLE CARBOXYLATE; ISOXAZOLE SALICYLATE; MACROLINE DERIVATIVE; OXALYLAMINO METHYLENE THIOPHENE SULFONAMIDE; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR; PIPERAZINYL THIOPHENYL ETHYL OXALAMIDE; PRODIGIOSIN DERIVATIVE; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE A; PROTEIN TYROSINE PHOSPHATASE B; ROSEOPHILIN DERIVATIVE; SECRETED ACID PHOSPHATASE M; STEVASTELIN DERIVATIVE; TUBERCULOSTATIC AGENT; UNCLASSIFIED DRUG;

EID: 84873180453     PISSN: 0966842X     EISSN: 18784380     Source Type: Journal    
DOI: 10.1016/j.tim.2012.09.002     Document Type: Review
Times cited : (74)

References (85)
  • 1
    • 0030913232 scopus 로고    scopus 로고
    • Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions
    • Black D.S., Bliska J.B. Identification of p130Cas as a substrate of Yersinia YopH (Yop51), a bacterial protein tyrosine phosphatase that translocates into mammalian cells and targets focal adhesions. EMBO J. 1997, 16:2730-2744.
    • (1997) EMBO J. , vol.16 , pp. 2730-2744
    • Black, D.S.1    Bliska, J.B.2
  • 2
    • 0030978909 scopus 로고    scopus 로고
    • The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions
    • Persson C., et al. The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions. EMBO J. 1997, 16:2307-2318.
    • (1997) EMBO J. , vol.16 , pp. 2307-2318
    • Persson, C.1
  • 3
    • 84858766192 scopus 로고    scopus 로고
    • Finding the smoking gun: protein tyrosine phosphatases as tools and targets of unicellular microorganisms and viruses
    • Heneberg P. Finding the smoking gun: protein tyrosine phosphatases as tools and targets of unicellular microorganisms and viruses. Curr. Med. Chem. 2012, 19:1530-1566.
    • (2012) Curr. Med. Chem. , vol.19 , pp. 1530-1566
    • Heneberg, P.1
  • 4
    • 43049181499 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis virulence is mediated by PtpA dephosphorylation of human vacuolar protein sorting 33B
    • Bach H., et al. Mycobacterium tuberculosis virulence is mediated by PtpA dephosphorylation of human vacuolar protein sorting 33B. Cell Host Microbe 2008, 3:316-322.
    • (2008) Cell Host Microbe , vol.3 , pp. 316-322
    • Bach, H.1
  • 5
    • 82755181483 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis protein tyrosine phosphatase (PtpA) excludes host vacuolar-H+-ATPase to inhibit phagosome acidification
    • Wong D., et al. Mycobacterium tuberculosis protein tyrosine phosphatase (PtpA) excludes host vacuolar-H+-ATPase to inhibit phagosome acidification. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:19371-19376.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 19371-19376
    • Wong, D.1
  • 6
    • 0034460958 scopus 로고    scopus 로고
    • Secretion of an acid phosphatase (SapM) by Mycobacterium tuberculosis that is similar to eukaryotic acid phosphatases
    • Saleh M.T., Belisle J.T. Secretion of an acid phosphatase (SapM) by Mycobacterium tuberculosis that is similar to eukaryotic acid phosphatases. J. Bacteriol. 2000, 182:6850-6853.
    • (2000) J. Bacteriol. , vol.182 , pp. 6850-6853
    • Saleh, M.T.1    Belisle, J.T.2
  • 7
    • 15244340430 scopus 로고    scopus 로고
    • Mechanism of phagolysosome biogenesis block by viable Mycobacterium tuberculosis
    • Vergne I., et al. Mechanism of phagolysosome biogenesis block by viable Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:4033-4038.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 4033-4038
    • Vergne, I.1
  • 8
    • 64649095990 scopus 로고    scopus 로고
    • Inhibition of MptpB phosphatase from Mycobacterium tuberculosis impairs mycobacterial survival in macrophages
    • Beresford N.J., et al. Inhibition of MptpB phosphatase from Mycobacterium tuberculosis impairs mycobacterial survival in macrophages. J. Antimicrob. Chemother. 2009, 63:928-936.
    • (2009) J. Antimicrob. Chemother. , vol.63 , pp. 928-936
    • Beresford, N.J.1
  • 9
    • 77949536564 scopus 로고    scopus 로고
    • Targeting Mycobacterium protein tyrosine phosphatase B for antituberculosis agents
    • Zhou B., et al. Targeting Mycobacterium protein tyrosine phosphatase B for antituberculosis agents. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:4573-4578.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 4573-4578
    • Zhou, B.1
  • 10
    • 13944258097 scopus 로고    scopus 로고
    • Endocytic delivery to lysosomes mediated by concurrent fusion and kissing events in living cells
    • Bright N.A., et al. Endocytic delivery to lysosomes mediated by concurrent fusion and kissing events in living cells. Curr. Biol. 2005, 15:360-365.
    • (2005) Curr. Biol. , vol.15 , pp. 360-365
    • Bright, N.A.1
  • 11
    • 0028220231 scopus 로고
    • Lack of acidification in Mycobacterium phagosomes produced by exclusion of the vesicular proton-ATPase
    • Sturgill-Koszycki S., et al. Lack of acidification in Mycobacterium phagosomes produced by exclusion of the vesicular proton-ATPase. Science 1994, 263:678-681.
    • (1994) Science , vol.263 , pp. 678-681
    • Sturgill-Koszycki, S.1
  • 12
    • 0034013295 scopus 로고    scopus 로고
    • Phagosome dynamics and function
    • Tjelle T.E., et al. Phagosome dynamics and function. Bioessays 2000, 22:255-263.
    • (2000) Bioessays , vol.22 , pp. 255-263
    • Tjelle, T.E.1
  • 13
    • 0742288047 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis phagosome maturation arrest: mycobacterial phosphatidylinositol analog phosphatidylinositol mannoside stimulates early endosomal fusion
    • Vergne I., et al. Mycobacterium tuberculosis phagosome maturation arrest: mycobacterial phosphatidylinositol analog phosphatidylinositol mannoside stimulates early endosomal fusion. Mol. Biol. Cell 2004, 15:751-760.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 751-760
    • Vergne, I.1
  • 14
    • 26244436989 scopus 로고    scopus 로고
    • Mycobacterial manipulation of the host cell
    • Hestvik A.L., et al. Mycobacterial manipulation of the host cell. FEMS Microbiol. Rev. 2005, 29:1041-1050.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 1041-1050
    • Hestvik, A.L.1
  • 15
    • 0034194181 scopus 로고    scopus 로고
    • The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis
    • Av-Gay Y., Everett M. The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis. Trends Microbiol. 2000, 8:238-244.
    • (2000) Trends Microbiol. , vol.8 , pp. 238-244
    • Av-Gay, Y.1    Everett, M.2
  • 16
    • 66549090908 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis PtkA is a novel protein tyrosine kinase whose substrate is PtpA
    • Bach H., et al. Mycobacterium tuberculosis PtkA is a novel protein tyrosine kinase whose substrate is PtpA. Biochem. J. 2009, 420:155-160.
    • (2009) Biochem. J. , vol.420 , pp. 155-160
    • Bach, H.1
  • 17
    • 0033806882 scopus 로고    scopus 로고
    • Cloning and characterization of secretory tyrosine phosphatases of Mycobacterium tuberculosis
    • Koul A., et al. Cloning and characterization of secretory tyrosine phosphatases of Mycobacterium tuberculosis. J. Bacteriol. 2000, 182:5425-5432.
    • (2000) J. Bacteriol. , vol.182 , pp. 5425-5432
    • Koul, A.1
  • 18
    • 0036218194 scopus 로고    scopus 로고
    • Expression and localization of the Mycobacterium tuberculosis protein tyrosine phosphatase PtpA
    • Cowley S.C., et al. Expression and localization of the Mycobacterium tuberculosis protein tyrosine phosphatase PtpA. Res. Microbiol. 2002, 153:233-241.
    • (2002) Res. Microbiol. , vol.153 , pp. 233-241
    • Cowley, S.C.1
  • 19
    • 75349083412 scopus 로고    scopus 로고
    • Protein kinase and phosphatase signaling in Mycobacterium tuberculosis physiology and pathogenesis
    • Chao J.D., et al. Protein kinase and phosphatase signaling in Mycobacterium tuberculosis physiology and pathogenesis. Biochim. Biophys. Acta 2010, 1804:620-627.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 620-627
    • Chao, J.D.1
  • 20
    • 77956519362 scopus 로고    scopus 로고
    • Convergence of Ser/Thr and two-component signaling to coordinate expression of the dormancy regulon in Mycobacterium tuberculosis
    • Chao J.D., et al. Convergence of Ser/Thr and two-component signaling to coordinate expression of the dormancy regulon in Mycobacterium tuberculosis. J. Biol. Chem. 2010, 285:29239-29246.
    • (2010) J. Biol. Chem. , vol.285 , pp. 29239-29246
    • Chao, J.D.1
  • 21
    • 10744227858 scopus 로고    scopus 로고
    • Disruption of mptpB impairs the ability of Mycobacterium tuberculosis to survive in guinea pigs
    • Singh R., et al. Disruption of mptpB impairs the ability of Mycobacterium tuberculosis to survive in guinea pigs. Mol. Microbiol. 2003, 50:751-762.
    • (2003) Mol. Microbiol. , vol.50 , pp. 751-762
    • Singh, R.1
  • 22
    • 77958056047 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases as drug targets: strategies and challenges of inhibitor development
    • Barr A.J. Protein tyrosine phosphatases as drug targets: strategies and challenges of inhibitor development. Future Med. Chem. 2010, 2:1563-1576.
    • (2010) Future Med. Chem. , vol.2 , pp. 1563-1576
    • Barr, A.J.1
  • 23
    • 84867280562 scopus 로고    scopus 로고
    • The apo-structure of the low-molecular-weight protein tyrosine phosphatase A (MptpA) from Mycobacterium tuberculosis allows for better target-specific drug development
    • Stehle T., et al. The apo-structure of the low-molecular-weight protein tyrosine phosphatase A (MptpA) from Mycobacterium tuberculosis allows for better target-specific drug development. J. Biol. Chem. 2012, 287:34569-34582.
    • (2012) J. Biol. Chem. , vol.287 , pp. 34569-34582
    • Stehle, T.1
  • 24
    • 34047255891 scopus 로고    scopus 로고
    • Structural basis for selective inhibition of Mycobacterium tuberculosis protein tyrosine phosphatase PtpB
    • Grundner C., et al. Structural basis for selective inhibition of Mycobacterium tuberculosis protein tyrosine phosphatase PtpB. Structure 2007, 15:499-509.
    • (2007) Structure , vol.15 , pp. 499-509
    • Grundner, C.1
  • 25
    • 27644474405 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis protein tyrosine phosphatase PtpB structure reveals a diverged fold and a buried active site
    • Grundner C., et al. Mycobacterium tuberculosis protein tyrosine phosphatase PtpB structure reveals a diverged fold and a buried active site. Structure 2005, 13:1625-1634.
    • (2005) Structure , vol.13 , pp. 1625-1634
    • Grundner, C.1
  • 26
    • 77953138509 scopus 로고    scopus 로고
    • Inhibition of Mycobacterium tuberculosis tyrosine phosphatase PtpA by synthetic chalcones: kinetics, molecular modeling, toxicity and effect on growth
    • Mascarello A., et al. Inhibition of Mycobacterium tuberculosis tyrosine phosphatase PtpA by synthetic chalcones: kinetics, molecular modeling, toxicity and effect on growth. Bioorg. Med. Chem. 2010, 18:3783-3789.
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 3783-3789
    • Mascarello, A.1
  • 27
    • 0034460958 scopus 로고    scopus 로고
    • Secretion of an acid phosphatase (SapM) by Mycobacterium tuberculosis that is similar to eukaryotic acid phosphatases
    • Saleh M.T., Belisle J.T. Secretion of an acid phosphatase (SapM) by Mycobacterium tuberculosis that is similar to eukaryotic acid phosphatases. J. Bacteriol. 2000, 182:6850-6853.
    • (2000) J. Bacteriol. , vol.182 , pp. 6850-6853
    • Saleh, M.T.1    Belisle, J.T.2
  • 28
    • 79953276682 scopus 로고    scopus 로고
    • Disruption of the SapM locus in Mycobacterium bovis BCG improves its protective efficacy as a vaccine against M. tuberculosis
    • Festjens N., et al. Disruption of the SapM locus in Mycobacterium bovis BCG improves its protective efficacy as a vaccine against M. tuberculosis. EMBO Mol. Med. 2011, 3:222-234.
    • (2011) EMBO Mol. Med. , vol.3 , pp. 222-234
    • Festjens, N.1
  • 29
    • 84860502287 scopus 로고    scopus 로고
    • The fbpA/sapM double knock out strain of Mycobacterium tuberculosis is highly attenuated and immunogenic in macrophages
    • Saikolappan S., et al. The fbpA/sapM double knock out strain of Mycobacterium tuberculosis is highly attenuated and immunogenic in macrophages. PLoS ONE 2012, 7:e36198.
    • (2012) PLoS ONE , vol.7
    • Saikolappan, S.1
  • 30
    • 14644438366 scopus 로고    scopus 로고
    • Crystal structure of low-molecular-weight protein tyrosine phosphatase from Mycobacterium tuberculosis at 1.9-A resolution
    • Madhurantakam C., et al. Crystal structure of low-molecular-weight protein tyrosine phosphatase from Mycobacterium tuberculosis at 1.9-A resolution. J. Bacteriol. 2005, 187:2175-2181.
    • (2005) J. Bacteriol. , vol.187 , pp. 2175-2181
    • Madhurantakam, C.1
  • 31
    • 0036305442 scopus 로고    scopus 로고
    • Low molecular weight protein tyrosine phosphatases: small, but smart
    • Raugei G., et al. Low molecular weight protein tyrosine phosphatases: small, but smart. Cell. Mol. Life Sci. 2002, 59:941-949.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 941-949
    • Raugei, G.1
  • 32
    • 77957664606 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis tyrosine phosphatase A (PtpA) activity is modulated by S-nitrosylation
    • Ecco G., et al. Mycobacterium tuberculosis tyrosine phosphatase A (PtpA) activity is modulated by S-nitrosylation. Chem. Commun. (Camb.) 2010, 46:7501-7503.
    • (2010) Chem. Commun. (Camb.) , vol.46 , pp. 7501-7503
    • Ecco, G.1
  • 33
    • 0034943323 scopus 로고    scopus 로고
    • The class C Vps complex functions at multiple stages of the vacuolar transport pathway
    • Peterson M.R., Emr S.D. The class C Vps complex functions at multiple stages of the vacuolar transport pathway. Traffic 2001, 2:476-486.
    • (2001) Traffic , vol.2 , pp. 476-486
    • Peterson, M.R.1    Emr, S.D.2
  • 34
    • 0030830765 scopus 로고    scopus 로고
    • A novel RING finger protein complex essential for a late step in protein transport to the yeast vacuole
    • Rieder S.E., Emr S.D. A novel RING finger protein complex essential for a late step in protein transport to the yeast vacuole. Mol. Biol. Cell 1997, 8:2307-2327.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2307-2327
    • Rieder, S.E.1    Emr, S.D.2
  • 35
    • 77649102858 scopus 로고    scopus 로고
    • Retrieval of the vacuolar H-ATPase from phagosomes revealed by live cell imaging
    • Clarke M., et al. Retrieval of the vacuolar H-ATPase from phagosomes revealed by live cell imaging. PLoS ONE 2010, 5:e8585.
    • (2010) PLoS ONE , vol.5
    • Clarke, M.1
  • 36
    • 69649106201 scopus 로고    scopus 로고
    • Direct recruitment of H+-ATPase from lysosomes for phagosomal acidification
    • Sun-Wada G., et al. Direct recruitment of H+-ATPase from lysosomes for phagosomal acidification. J. Cell Sci. 2009, 122:2504-2513.
    • (2009) J. Cell Sci. , vol.122 , pp. 2504-2513
    • Sun-Wada, G.1
  • 37
    • 34247568898 scopus 로고    scopus 로고
    • The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis
    • Peplowska K., et al. The CORVET tethering complex interacts with the yeast Rab5 homolog Vps21 and is involved in endo-lysosomal biogenesis. Dev. Cell 2007, 12:739-750.
    • (2007) Dev. Cell , vol.12 , pp. 739-750
    • Peplowska, K.1
  • 38
    • 0034735539 scopus 로고    scopus 로고
    • New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion
    • Wurmser A.E., et al. New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion. J. Cell Biol. 2000, 151:551-562.
    • (2000) J. Cell Biol. , vol.151 , pp. 551-562
    • Wurmser, A.E.1
  • 39
    • 67949091245 scopus 로고    scopus 로고
    • Vps-C complexes: gatekeepers of endolysosomal traffic
    • Nickerson D.P., et al. Vps-C complexes: gatekeepers of endolysosomal traffic. Curr. Opin. Cell Biol. 2009, 21:543-551.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 543-551
    • Nickerson, D.P.1
  • 40
    • 43049147117 scopus 로고    scopus 로고
    • A pathway for phagosome maturation during engulfment of apoptotic cells
    • Kinchen J.M., et al. A pathway for phagosome maturation during engulfment of apoptotic cells. Nat. Cell Biol. 2008, 10:556-566.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 556-566
    • Kinchen, J.M.1
  • 41
    • 42149136830 scopus 로고    scopus 로고
    • The vacuolar V1/V0-ATPase is involved in the release of the HOPS subunit Vps41 from vacuoles, vacuole fragmentation and fusion
    • Takeda K., et al. The vacuolar V1/V0-ATPase is involved in the release of the HOPS subunit Vps41 from vacuoles, vacuole fragmentation and fusion. FEBS Lett. 2008, 582:1558-1563.
    • (2008) FEBS Lett. , vol.582 , pp. 1558-1563
    • Takeda, K.1
  • 42
    • 0035252348 scopus 로고    scopus 로고
    • Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion
    • Peters C., et al. Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion. Nature 2001, 409:581-588.
    • (2001) Nature , vol.409 , pp. 581-588
    • Peters, C.1
  • 43
    • 34547842536 scopus 로고    scopus 로고
    • MptpB, a virulence factor from Mycobacterium tuberculosis, exhibits triple-specificity phosphatase activity
    • Beresford N., et al. MptpB, a virulence factor from Mycobacterium tuberculosis, exhibits triple-specificity phosphatase activity. Biochem. J. 2007, 406:13-18.
    • (2007) Biochem. J. , vol.406 , pp. 13-18
    • Beresford, N.1
  • 44
    • 0034035311 scopus 로고    scopus 로고
    • Interleukin-6 induces early gamma interferon production in the infected lung but is not required for generation of specific immunity to Mycobacterium tuberculosis infection
    • Saunders B.M., et al. Interleukin-6 induces early gamma interferon production in the infected lung but is not required for generation of specific immunity to Mycobacterium tuberculosis infection. Infect. Immun. 2000, 68:3322-3326.
    • (2000) Infect. Immun. , vol.68 , pp. 3322-3326
    • Saunders, B.M.1
  • 45
    • 0036263080 scopus 로고    scopus 로고
    • Differential regulation of the mitogen-activated protein kinases by pathogenic and nonpathogenic mycobacteria
    • Roach S.K., Schorey J.S. Differential regulation of the mitogen-activated protein kinases by pathogenic and nonpathogenic mycobacteria. Infect. Immun. 2002, 70:3040-3052.
    • (2002) Infect. Immun. , vol.70 , pp. 3040-3052
    • Roach, S.K.1    Schorey, J.S.2
  • 46
    • 36448953072 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis 6-kDa early secreted antigenic target (ESAT-6) protein downregulates lipopolysaccharide induced c-myc expression by modulating the extracellular signal regulated kinases 1/2
    • Ganguly N., et al. Mycobacterium tuberculosis 6-kDa early secreted antigenic target (ESAT-6) protein downregulates lipopolysaccharide induced c-myc expression by modulating the extracellular signal regulated kinases 1/2. BMC Immunol. 2007, 8:24.
    • (2007) BMC Immunol. , vol.8 , pp. 24
    • Ganguly, N.1
  • 47
    • 33646357881 scopus 로고    scopus 로고
    • The mycobacterial 38-kilodalton glycolipoprotein antigen activates the mitogen-activated protein kinase pathway and release of proinflammatory cytokines through Toll-like receptors 2 and 4 in human monocytes
    • Jung S.B., et al. The mycobacterial 38-kilodalton glycolipoprotein antigen activates the mitogen-activated protein kinase pathway and release of proinflammatory cytokines through Toll-like receptors 2 and 4 in human monocytes. Infect. Immun. 2006, 74:2686-2696.
    • (2006) Infect. Immun. , vol.74 , pp. 2686-2696
    • Jung, S.B.1
  • 48
    • 51349145277 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase PtpA is not required for Mycobacterium tuberculosis growth in mice
    • Grundner C., et al. Protein tyrosine phosphatase PtpA is not required for Mycobacterium tuberculosis growth in mice. FEMS Microbiol. Lett. 2008, 287:181-184.
    • (2008) FEMS Microbiol. Lett. , vol.287 , pp. 181-184
    • Grundner, C.1
  • 50
    • 77956299896 scopus 로고    scopus 로고
    • Granuloma encapsulation is a key factor for containing tuberculosis infection in minipigs
    • Gil O., et al. Granuloma encapsulation is a key factor for containing tuberculosis infection in minipigs. PLoS ONE 2010, 5:e10030.
    • (2010) PLoS ONE , vol.5
    • Gil, O.1
  • 51
    • 70349756864 scopus 로고    scopus 로고
    • Productive steps toward an antimicrobial targeting virulence
    • Barczak A.K., Hung D.T. Productive steps toward an antimicrobial targeting virulence. Curr. Opin. Microbiol. 2009, 12:490-496.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 490-496
    • Barczak, A.K.1    Hung, D.T.2
  • 52
    • 70749146770 scopus 로고    scopus 로고
    • High-throughput discovery of Mycobacterium tuberculosis protein tyrosine phosphatase B (MptpB) inhibitors using click chemistry
    • Tan L.P., et al. High-throughput discovery of Mycobacterium tuberculosis protein tyrosine phosphatase B (MptpB) inhibitors using click chemistry. Org. Lett. 2009, 11:5102-5105.
    • (2009) Org. Lett. , vol.11 , pp. 5102-5105
    • Tan, L.P.1
  • 53
    • 27144444772 scopus 로고    scopus 로고
    • Structure-based design and discovery of protein tyrosine phosphatase inhibitors incorporating novel isothiazolidinone heterocyclic phosphotyrosine mimetics
    • Combs A.P., et al. Structure-based design and discovery of protein tyrosine phosphatase inhibitors incorporating novel isothiazolidinone heterocyclic phosphotyrosine mimetics. J. Med. Chem. 2005, 48:6544-6548.
    • (2005) J. Med. Chem. , vol.48 , pp. 6544-6548
    • Combs, A.P.1
  • 54
    • 55549140118 scopus 로고    scopus 로고
    • Synthetic chalcones as efficient inhibitors of Mycobacterium tuberculosis protein tyrosine phosphatase PtpA
    • Chiaradia L.D., et al. Synthetic chalcones as efficient inhibitors of Mycobacterium tuberculosis protein tyrosine phosphatase PtpA. Bioorg. Med. Chem. Lett. 2008, 18:6227-6230.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 6227-6230
    • Chiaradia, L.D.1
  • 55
    • 26944488334 scopus 로고    scopus 로고
    • Discovery of Mycobacterium tuberculosis protein tyrosine phosphatase A (MptpA) inhibitors based on natural products and a fragment-based approach
    • Manger M., et al. Discovery of Mycobacterium tuberculosis protein tyrosine phosphatase A (MptpA) inhibitors based on natural products and a fragment-based approach. Chembiochem 2005, 6:1749-1753.
    • (2005) Chembiochem , vol.6 , pp. 1749-1753
    • Manger, M.1
  • 56
    • 51449088440 scopus 로고    scopus 로고
    • Discovery of a new class of inhibitors of Mycobacterium tuberculosis protein tyrosine phosphatase B by biology-oriented synthesis
    • Noren-Muller A., et al. Discovery of a new class of inhibitors of Mycobacterium tuberculosis protein tyrosine phosphatase B by biology-oriented synthesis. Angew. Chem. Int. Ed. Engl. 2008, 47:5973-5977.
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 5973-5977
    • Noren-Muller, A.1
  • 57
    • 34547758886 scopus 로고    scopus 로고
    • Fragment-based substrate activity screening method for the identification of potent inhibitors of the Mycobacterium tuberculosis phosphatase PtpB
    • Soellner M.B., et al. Fragment-based substrate activity screening method for the identification of potent inhibitors of the Mycobacterium tuberculosis phosphatase PtpB. J. Am. Chem. Soc. 2007, 129:9613-9615.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 9613-9615
    • Soellner, M.B.1
  • 58
    • 77955962258 scopus 로고    scopus 로고
    • Design and synthesis of nonpeptidic, small molecule inhibitors for the Mycobacterium tuberculosis protein tyrosine phosphatase PtpB
    • Rawls K.A., et al. Design and synthesis of nonpeptidic, small molecule inhibitors for the Mycobacterium tuberculosis protein tyrosine phosphatase PtpB. Org. Biomol. Chem. 2010, 8:4066-4070.
    • (2010) Org. Biomol. Chem. , vol.8 , pp. 4066-4070
    • Rawls, K.A.1
  • 59
    • 77958100393 scopus 로고    scopus 로고
    • Identification and characterization of novel inhibitors of mPTPB, an essential virulent phosphatase from Mycobacterium tuberculosis
    • Chen L., et al. Identification and characterization of novel inhibitors of mPTPB, an essential virulent phosphatase from Mycobacterium tuberculosis. ACS Med. Chem. Lett. 2010, 1:355-359.
    • (2010) ACS Med. Chem. Lett. , vol.1 , pp. 355-359
    • Chen, L.1
  • 60
    • 71849090071 scopus 로고    scopus 로고
    • Fragment-based discovery of selective inhibitors of the Mycobacterium tuberculosis protein tyrosine phosphatase PtpA
    • Rawls K.A., et al. Fragment-based discovery of selective inhibitors of the Mycobacterium tuberculosis protein tyrosine phosphatase PtpA. Bioorg. Med. Chem. Lett. 2009, 19:6851-6854.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 6851-6854
    • Rawls, K.A.1
  • 61
    • 84855857053 scopus 로고    scopus 로고
    • Synthesis, biological evaluation, and molecular modeling of chalcone derivatives as potent inhibitors of Mycobacterium tuberculosis protein tyrosine phosphatases (PtpA and PtpB)
    • Chiaradia L.D., et al. Synthesis, biological evaluation, and molecular modeling of chalcone derivatives as potent inhibitors of Mycobacterium tuberculosis protein tyrosine phosphatases (PtpA and PtpB). J. Med. Chem. 2012, 55:390-402.
    • (2012) J. Med. Chem. , vol.55 , pp. 390-402
    • Chiaradia, L.D.1
  • 62
    • 33746047675 scopus 로고    scopus 로고
    • Discovery of protein phosphatase inhibitor classes by biology-oriented synthesis
    • Noren-Muller A., et al. Discovery of protein phosphatase inhibitor classes by biology-oriented synthesis. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:10606-10611.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 10606-10611
    • Noren-Muller, A.1
  • 63
    • 77955574023 scopus 로고    scopus 로고
    • Identification of thiazolidinones spiro-fused to indolin-2-ones as potent and selective inhibitors of the Mycobacterium tuberculosis protein tyrosine phosphatase B
    • Vintonyak V.V., et al. Identification of thiazolidinones spiro-fused to indolin-2-ones as potent and selective inhibitors of the Mycobacterium tuberculosis protein tyrosine phosphatase B. Angew. Chem. Int. Ed. Engl. 2010, 49:5902-5905.
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 5902-5905
    • Vintonyak, V.V.1
  • 64
    • 0033575956 scopus 로고    scopus 로고
    • A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion
    • Fu Y., Galan J.E. A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature 1999, 401:293-297.
    • (1999) Nature , vol.401 , pp. 293-297
    • Fu, Y.1    Galan, J.E.2
  • 65
    • 61849166099 scopus 로고    scopus 로고
    • The Salmonella effector SptP dephosphorylates host AAA+ ATPase VCP to promote development of its intracellular replicative niche
    • Humphreys D., et al. The Salmonella effector SptP dephosphorylates host AAA+ ATPase VCP to promote development of its intracellular replicative niche. Cell Host Microbe 2009, 5:225-233.
    • (2009) Cell Host Microbe , vol.5 , pp. 225-233
    • Humphreys, D.1
  • 66
    • 33750600406 scopus 로고    scopus 로고
    • Salmonella enterica serovar Typhimurium effectors SopB, SopE, SopE2 and SipA disrupt tight junction structure and function
    • Boyle E.C., et al. Salmonella enterica serovar Typhimurium effectors SopB, SopE, SopE2 and SipA disrupt tight junction structure and function. Cell. Microbiol. 2006, 8:1946-1957.
    • (2006) Cell. Microbiol. , vol.8 , pp. 1946-1957
    • Boyle, E.C.1
  • 67
    • 0032564446 scopus 로고    scopus 로고
    • SopB, a protein required for virulence of Salmonella dublin, is an inositol phosphate phosphatase
    • Norris F.A., et al. SopB, a protein required for virulence of Salmonella dublin, is an inositol phosphate phosphatase. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:14057-14059.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 14057-14059
    • Norris, F.A.1
  • 68
    • 33750724697 scopus 로고    scopus 로고
    • Differential activation and function of Rho GTPases during Salmonella-host cell interactions
    • Patel J.C., Galan J.E. Differential activation and function of Rho GTPases during Salmonella-host cell interactions. J. Cell Biol. 2006, 175:453-463.
    • (2006) J. Cell Biol. , vol.175 , pp. 453-463
    • Patel, J.C.1    Galan, J.E.2
  • 69
    • 0035147455 scopus 로고    scopus 로고
    • A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization
    • Zhou D., et al. A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization. Mol. Microbiol. 2001, 39:248-259.
    • (2001) Mol. Microbiol. , vol.39 , pp. 248-259
    • Zhou, D.1
  • 70
    • 79959475597 scopus 로고    scopus 로고
    • LipA, a tyrosine and lipid phosphatase involved in the virulence of Listeria monocytogenes
    • Kastner R., et al. LipA, a tyrosine and lipid phosphatase involved in the virulence of Listeria monocytogenes. Infect. Immun. 2011, 79:2489-2498.
    • (2011) Infect. Immun. , vol.79 , pp. 2489-2498
    • Kastner, R.1
  • 71
    • 18644379244 scopus 로고    scopus 로고
    • Conversion of PtdIns(4,5)P(2) into PtdIns(5)P by the S. flexneri effector IpgD reorganizes host cell morphology
    • Niebuhr K., et al. Conversion of PtdIns(4,5)P(2) into PtdIns(5)P by the S. flexneri effector IpgD reorganizes host cell morphology. EMBO J. 2002, 21:5069-5078.
    • (2002) EMBO J. , vol.21 , pp. 5069-5078
    • Niebuhr, K.1
  • 72
    • 33644850315 scopus 로고    scopus 로고
    • PtdIns5P activates the host cell PI3-kinase/Akt pathway during Shigella flexneri infection
    • Pendaries C., et al. PtdIns5P activates the host cell PI3-kinase/Akt pathway during Shigella flexneri infection. EMBO J. 2006, 25:1024-1034.
    • (2006) EMBO J. , vol.25 , pp. 1024-1034
    • Pendaries, C.1
  • 73
    • 77954479994 scopus 로고    scopus 로고
    • Francisella acid phosphatases inactivate the NADPH oxidase in human phagocytes
    • Mohapatra N.P., et al. Francisella acid phosphatases inactivate the NADPH oxidase in human phagocytes. J. Immunol. 2010, 184:5141-5150.
    • (2010) J. Immunol. , vol.184 , pp. 5141-5150
    • Mohapatra, N.P.1
  • 74
    • 0035167098 scopus 로고    scopus 로고
    • Legionella pneumophila major acid phosphatase and its role in intracellular infection
    • Aragon V., et al. Legionella pneumophila major acid phosphatase and its role in intracellular infection. Infect. Immun. 2001, 69:177-185.
    • (2001) Infect. Immun. , vol.69 , pp. 177-185
    • Aragon, V.1
  • 75
    • 0022398312 scopus 로고
    • Properties of an acid phosphatase from Legionella micdadei which blocks superoxide anion production by human neutrophils
    • Saha A.K., et al. Properties of an acid phosphatase from Legionella micdadei which blocks superoxide anion production by human neutrophils. Arch. Biochem. Biophys. 1985, 243:150-160.
    • (1985) Arch. Biochem. Biophys. , vol.243 , pp. 150-160
    • Saha, A.K.1
  • 76
    • 78650907944 scopus 로고    scopus 로고
    • Coxiella burnetii acid phosphatase inhibits the release of reactive oxygen intermediates in polymorphonuclear leukocytes
    • Hill J., Samuel J.E. Coxiella burnetii acid phosphatase inhibits the release of reactive oxygen intermediates in polymorphonuclear leukocytes. Infect. Immun. 2011, 79:414-420.
    • (2011) Infect. Immun. , vol.79 , pp. 414-420
    • Hill, J.1    Samuel, J.E.2
  • 77
    • 0038501083 scopus 로고    scopus 로고
    • The Pseudomonas syringae type III-secreted protein HopPtoD2 possesses protein tyrosine phosphatase activity and suppresses programmed cell death in plants
    • Espinosa A., et al. The Pseudomonas syringae type III-secreted protein HopPtoD2 possesses protein tyrosine phosphatase activity and suppresses programmed cell death in plants. Mol. Microbiol. 2003, 49:377-387.
    • (2003) Mol. Microbiol. , vol.49 , pp. 377-387
    • Espinosa, A.1
  • 79
    • 84857667691 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis SecA2 system subverts phagosome maturation to promote growth in macrophages
    • Sullivan J.T., et al. The Mycobacterium tuberculosis SecA2 system subverts phagosome maturation to promote growth in macrophages. Infect. Immun. 2012, 80:996-1006.
    • (2012) Infect. Immun. , vol.80 , pp. 996-1006
    • Sullivan, J.T.1
  • 80
    • 0033592871 scopus 로고    scopus 로고
    • Mycobacterial infection of macrophages results in membrane-permeable phagosomes
    • Teitelbaum R., et al. Mycobacterial infection of macrophages results in membrane-permeable phagosomes. Proc. Natl. Acad. Sci. U.S.A. 1999, 96:15190-15195.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 15190-15195
    • Teitelbaum, R.1
  • 81
    • 0036785655 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis phagosome in human macrophages is isolated from the host cell cytoplasm
    • Clemens D.L., et al. The Mycobacterium tuberculosis phagosome in human macrophages is isolated from the host cell cytoplasm. Infect. Immun. 2002, 70:5800-5807.
    • (2002) Infect. Immun. , vol.70 , pp. 5800-5807
    • Clemens, D.L.1
  • 82
    • 34547766513 scopus 로고    scopus 로고
    • ESAT-6 from Mycobacterium tuberculosis dissociates from its putative chaperone CFP-10 under acidic conditions and exhibits membrane-lysing activity
    • de Jonge M.I., et al. ESAT-6 from Mycobacterium tuberculosis dissociates from its putative chaperone CFP-10 under acidic conditions and exhibits membrane-lysing activity. J. Bacteriol. 2007, 189:6028-6034.
    • (2007) J. Bacteriol. , vol.189 , pp. 6028-6034
    • de Jonge, M.I.1
  • 83
    • 33746918717 scopus 로고    scopus 로고
    • Brunsvicamides A-C: sponge-related cyanobacterial peptides with Mycobacterium tuberculosis protein tyrosine phosphatase inhibitory activity
    • Muller D., et al. Brunsvicamides A-C: sponge-related cyanobacterial peptides with Mycobacterium tuberculosis protein tyrosine phosphatase inhibitory activity. J. Med. Chem. 2006, 49:4871-4878.
    • (2006) J. Med. Chem. , vol.49 , pp. 4871-4878
    • Muller, D.1
  • 84
    • 27744514053 scopus 로고    scopus 로고
    • 3-Substituted indolizine-1-carbonitrile derivatives as phosphatase inhibitors
    • Weide T., et al. 3-Substituted indolizine-1-carbonitrile derivatives as phosphatase inhibitors. Bioorg. Med. Chem. Lett. 2006, 16:59-63.
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 59-63
    • Weide, T.1
  • 85
    • 67349260111 scopus 로고    scopus 로고
    • A dynamic reinfection hypothesis of latent tuberculosis infection
    • Cardona P.J. A dynamic reinfection hypothesis of latent tuberculosis infection. Infection 2009, 37:80-86.
    • (2009) Infection , vol.37 , pp. 80-86
    • Cardona, P.J.1


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