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Volumn 7, Issue 11, 2012, Pages

17-AAG Kills Intracellular Leishmania amazonensis while Reducing Inflammatory Responses in Infected Macrophages

Author keywords

[No Author keywords available]

Indexed keywords

INTERLEUKIN 1; INTERLEUKIN 6; MONOCYTE CHEMOTACTIC PROTEIN 1; MYELIN; NITRIC OXIDE; SUPEROXIDE; TANESPIMYCIN; TUMOR NECROSIS FACTOR ALPHA;

EID: 84869040743     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0049496     Document Type: Article
Times cited : (43)

References (60)
  • 1
    • 3042555141 scopus 로고    scopus 로고
    • Leishmaniasis: current situation and new perspectives
    • Desjeux P, (2004) Leishmaniasis: current situation and new perspectives. Comp Immunol Microbiol Infect Dis 27: 305-318.
    • (2004) Comp Immunol Microbiol Infect Dis , vol.27 , pp. 305-318
    • Desjeux, P.1
  • 2
    • 33846847777 scopus 로고    scopus 로고
    • Leishmania vaccines: progress and problems
    • Kedzierski L, Zhu Y, Handman E, (2006) Leishmania vaccines: progress and problems. Parasitology 133Suppl: S87-112.
    • (2006) Parasitology , vol.133
    • Kedzierski, L.1    Zhu, Y.2    Handman, E.3
  • 3
    • 0142258171 scopus 로고    scopus 로고
    • Leishmaniasis-current chemotherapy and recent advances in the search for novel drugs
    • Croft SL, Coombs GH, (2003) Leishmaniasis-current chemotherapy and recent advances in the search for novel drugs. Trends Parasitol 19: 502-508.
    • (2003) Trends Parasitol , vol.19 , pp. 502-508
    • Croft, S.L.1    Coombs, G.H.2
  • 6
    • 19444381776 scopus 로고    scopus 로고
    • Early-onset pentamidine-associated second-degree heart block and sinus bradycardia: case report and review of the literature
    • Antoniou T, Gough KA, (2005) Early-onset pentamidine-associated second-degree heart block and sinus bradycardia: case report and review of the literature. Pharmacotherapy 25: 899-903.
    • (2005) Pharmacotherapy , vol.25 , pp. 899-903
    • Antoniou, T.1    Gough, K.A.2
  • 7
    • 0028888323 scopus 로고
    • Pentamidine-induced derangements of glucose homeostasis. Determinant roles of renal failure and drug accumulation. A study of 128 patients
    • Assan R, Perronne C, Assan D, Chotard L, Mayaud C, et al. (1995) Pentamidine-induced derangements of glucose homeostasis. Determinant roles of renal failure and drug accumulation. A study of 128 patients. Diabetes Care 18: 47-55.
    • (1995) Diabetes Care , vol.18 , pp. 47-55
    • Assan, R.1    Perronne, C.2    Assan, D.3    Chotard, L.4    Mayaud, C.5
  • 8
    • 35548987998 scopus 로고    scopus 로고
    • Visceral leishmaniasis: what are the needs for diagnosis, treatment and control?
    • Chappuis F, Sundar S, Hailu A, Ghalib H, Rijal S, et al. (2007) Visceral leishmaniasis: what are the needs for diagnosis, treatment and control? Nat Rev Microbiol 5: 873-882.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 873-882
    • Chappuis, F.1    Sundar, S.2    Hailu, A.3    Ghalib, H.4    Rijal, S.5
  • 9
    • 80455174235 scopus 로고    scopus 로고
    • Structures, targets and recent approaches in anti-leishmanial drug discovery and development
    • Seifert K, (2011) Structures, targets and recent approaches in anti-leishmanial drug discovery and development. Open Med Chem J 5: 31-39.
    • (2011) Open Med Chem J , vol.5 , pp. 31-39
    • Seifert, K.1
  • 10
    • 0030863995 scopus 로고    scopus 로고
    • The amino-terminal domain of heat shock protein 90 (HSP90) that binds geldanamycin is an ATP/ADP switch domain that regulates Hsp90 conformation
    • Grenert JP, Sullivan WP, Fadden P, Haystead TA, Clark J, et al. (1997) The amino-terminal domain of heat shock protein 90 (HSP90) that binds geldanamycin is an ATP/ADP switch domain that regulates Hsp90 conformation. J Biol Chem 272: 23843-23850.
    • (1997) J Biol Chem , vol.272 , pp. 23843-23850
    • Grenert, J.P.1    Sullivan, W.P.2    Fadden, P.3    Haystead, T.A.4    Clark, J.5
  • 11
    • 0036219609 scopus 로고    scopus 로고
    • Hsp90 inhibitors as novel cancer chemotherapeutic agents
    • Neckers L, (2002) Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med 8: S55-61.
    • (2002) Trends Mol Med , vol.8
    • Neckers, L.1
  • 12
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, et al. (1997) Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90: 65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5
  • 14
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L, Lindquist SL, (2005) HSP90 and the chaperoning of cancer. Nat Rev Cancer 5: 761-772.
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 15
    • 34250351297 scopus 로고    scopus 로고
    • A postgenomic view of the heat shock proteins in kinetoplastids
    • Folgueira C, Requena JM, (2007) A postgenomic view of the heat shock proteins in kinetoplastids. FEMS Microbiol Rev 31: 359-377.
    • (2007) FEMS Microbiol Rev , vol.31 , pp. 359-377
    • Folgueira, C.1    Requena, J.M.2
  • 16
    • 0030667932 scopus 로고    scopus 로고
    • In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
    • Nathan DF, Vos MH, Lindquist S, (1997) In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc Natl Acad Sci U S A 94: 12949-12956.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12949-12956
    • Nathan, D.F.1    Vos, M.H.2    Lindquist, S.3
  • 17
    • 0031693703 scopus 로고    scopus 로고
    • The Hsp90 complex-a super-chaperone machine as a novel drug target
    • Scheibel T, Buchner J, (1998) The Hsp90 complex-a super-chaperone machine as a novel drug target. Biochem Pharmacol 56: 675-682.
    • (1998) Biochem Pharmacol , vol.56 , pp. 675-682
    • Scheibel, T.1    Buchner, J.2
  • 18
    • 0035203992 scopus 로고    scopus 로고
    • Heat shock protein 90 homeostasis controls stage differentiation in Leishmania donovani
    • Wiesgigl M, Clos J, (2001) Heat shock protein 90 homeostasis controls stage differentiation in Leishmania donovani. Mol Biol Cell 12: 3307-3316.
    • (2001) Mol Biol Cell , vol.12 , pp. 3307-3316
    • Wiesgigl, M.1    Clos, J.2
  • 19
    • 0038381514 scopus 로고    scopus 로고
    • Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes
    • Banumathy G, Singh V, Pavithra SR, Tatu U, (2003) Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes. J Biol Chem 278: 18336-18345.
    • (2003) J Biol Chem , vol.278 , pp. 18336-18345
    • Banumathy, G.1    Singh, V.2    Pavithra, S.R.3    Tatu, U.4
  • 20
    • 16244382411 scopus 로고    scopus 로고
    • Plasmodium falciparum calcineurin and its association with heat shock protein 90: mechanisms for the antimalarial activity of cyclosporin A and synergism with geldanamycin
    • Kumar R, Musiyenko A, Barik S, (2005) Plasmodium falciparum calcineurin and its association with heat shock protein 90: mechanisms for the antimalarial activity of cyclosporin A and synergism with geldanamycin. Mol Biochem Parasitol 141: 29-37.
    • (2005) Mol Biochem Parasitol , vol.141 , pp. 29-37
    • Kumar, R.1    Musiyenko, A.2    Barik, S.3
  • 21
    • 78649667345 scopus 로고    scopus 로고
    • Heat shock protein 90 as a drug target against protozoan infections: biochemical characterization of HSP90 from Plasmodium falciparum and Trypanosoma evansi and evaluation of its inhibitor as a candidate drug
    • Pallavi R, Roy N, Nageshan RK, Talukdar P, Pavithra SR, et al. (2010) Heat shock protein 90 as a drug target against protozoan infections: biochemical characterization of HSP90 from Plasmodium falciparum and Trypanosoma evansi and evaluation of its inhibitor as a candidate drug. J Biol Chem 285: 37964-37975.
    • (2010) J Biol Chem , vol.285 , pp. 37964-37975
    • Pallavi, R.1    Roy, N.2    Nageshan, R.K.3    Talukdar, P.4    Pavithra, S.R.5
  • 22
    • 0242661627 scopus 로고    scopus 로고
    • Molecular cloning of the 82-kDa heat shock protein (HSP90) of Toxoplasma gondii associated with the entry into and growth in host cells
    • Ahn HJ, Kim S, Nam HW, (2003) Molecular cloning of the 82-kDa heat shock protein (HSP90) of Toxoplasma gondii associated with the entry into and growth in host cells. Biochem Biophys Res Commun 311: 654-659.
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 654-659
    • Ahn, H.J.1    Kim, S.2    Nam, H.W.3
  • 23
    • 0029143254 scopus 로고
    • High constitutive levels of heat-shock proteins in human-pathogenic parasites of the genus Leishmania
    • Brandau S, Dresel A, Clos J, (1995) High constitutive levels of heat-shock proteins in human-pathogenic parasites of the genus Leishmania. Biochem J 310 (Pt 1): 225-232.
    • (1995) Biochem J , vol.310 , Issue.Pt 1 , pp. 225-232
    • Brandau, S.1    Dresel, A.2    Clos, J.3
  • 24
    • 70350231906 scopus 로고    scopus 로고
    • Apoptosis caused by Hsp90 inhibitor geldanamycin in Leishmania donovani during promastigote-to-amastigote transformation stage
    • Li Q, Zhou Y, Yao C, Ma X, Wang L, et al. (2009) Apoptosis caused by Hsp90 inhibitor geldanamycin in Leishmania donovani during promastigote-to-amastigote transformation stage. Parasitol Res 105: 1539-1548.
    • (2009) Parasitol Res , vol.105 , pp. 1539-1548
    • Li, Q.1    Zhou, Y.2    Yao, C.3    Ma, X.4    Wang, L.5
  • 25
    • 79952172924 scopus 로고    scopus 로고
    • Intracellular protozoan parasites of humans: the role of molecular chaperones in development and pathogenesis
    • Shonhai A, Maier AG, Przyborski JM, Blatch GL, (2011) Intracellular protozoan parasites of humans: the role of molecular chaperones in development and pathogenesis. Protein Pept Lett 18: 143-157.
    • (2011) Protein Pept Lett , vol.18 , pp. 143-157
    • Shonhai, A.1    Maier, A.G.2    Przyborski, J.M.3    Blatch, G.L.4
  • 26
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin
    • Schulte TW, Neckers LM, (1998) The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother Pharmacol 42: 273-279.
    • (1998) Cancer Chemother Pharmacol , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 27
    • 0043288724 scopus 로고    scopus 로고
    • Heat shock protein 90 as a molecular target for cancer therapeutics
    • Isaacs JS, Xu W, Neckers L, (2003) Heat shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell 3: 213-217.
    • (2003) Cancer Cell , vol.3 , pp. 213-217
    • Isaacs, J.S.1    Xu, W.2    Neckers, L.3
  • 28
    • 0037389770 scopus 로고    scopus 로고
    • Differential properties of CBA/J mononuclear phagocytes recovered from an inflammatory site and probed with two different species of Leishmania
    • Gomes IN, Calabrich AF, Tavares Rda S, Wietzerbin J, de Freitas LA, et al. (2003) Differential properties of CBA/J mononuclear phagocytes recovered from an inflammatory site and probed with two different species of Leishmania. Microbes Infect 5: 251-260.
    • (2003) Microbes Infect , vol.5 , pp. 251-260
    • Gomes, I.N.1    Calabrich, A.F.2    da Tavares, R.S.3    Wietzerbin, J.4    de Freitas, L.A.5
  • 29
    • 33744814650 scopus 로고    scopus 로고
    • Leishmania amazonensis: participation of regulatory T and B cells in the in vitro priming (PIV) of CBA/J spleen cells susceptible response
    • Veras PS, Welby-Borges M, de Santana CD, Nihei J, Cardillo F, et al. (2006) Leishmania amazonensis: participation of regulatory T and B cells in the in vitro priming (PIV) of CBA/J spleen cells susceptible response. Exp Parasitol 113: 201-205.
    • (2006) Exp Parasitol , vol.113 , pp. 201-205
    • Veras, P.S.1    Welby-Borges, M.2    de Santana, C.D.3    Nihei, J.4    Cardillo, F.5
  • 30
    • 0031668777 scopus 로고    scopus 로고
    • Inhibition of NADPH supply by 6-aminonicotinamide: effect on glutathione, nitric oxide and superoxide in J774 cells
    • Hothersall JS, Gordge M, Noronha-Dutra AA, (1998) Inhibition of NADPH supply by 6-aminonicotinamide: effect on glutathione, nitric oxide and superoxide in J774 cells. FEBS Lett 434: 97-100.
    • (1998) FEBS Lett , vol.434 , pp. 97-100
    • Hothersall, J.S.1    Gordge, M.2    Noronha-Dutra, A.A.3
  • 31
    • 0023706894 scopus 로고
    • Release of reactive nitrogen intermediates and reactive oxygen intermediates from mouse peritoneal macrophages. Comparison of activating cytokines and evidence for independent production
    • Ding AH, Nathan CF, Stuehr DJ, (1988) Release of reactive nitrogen intermediates and reactive oxygen intermediates from mouse peritoneal macrophages. Comparison of activating cytokines and evidence for independent production. J Immunol 141: 2407-2412.
    • (1988) J Immunol , vol.141 , pp. 2407-2412
    • Ding, A.H.1    Nathan, C.F.2    Stuehr, D.J.3
  • 32
    • 67649598078 scopus 로고    scopus 로고
    • Antimalarial activity of betulinic acid and derivatives in vitro against Plasmodium falciparum and in vivo in P. berghei-infected mice
    • de Sa MS, Costa JF, Krettli AU, Zalis MG, Maia GL, et al. (2009) Antimalarial activity of betulinic acid and derivatives in vitro against Plasmodium falciparum and in vivo in P. berghei-infected mice. Parasitol Res 105: 275-279.
    • (2009) Parasitol Res , vol.105 , pp. 275-279
    • de Sa, M.S.1    Costa, J.F.2    Krettli, A.U.3    Zalis, M.G.4    Maia, G.L.5
  • 33
    • 0035084863 scopus 로고    scopus 로고
    • Kinetics of the intracellular differentiation of Leishmania amazonensis and internalization of host MHC molecules by the intermediate parasite stages
    • Courret N, Frehel C, Prina E, Lang T, Antoine JC, (2001) Kinetics of the intracellular differentiation of Leishmania amazonensis and internalization of host MHC molecules by the intermediate parasite stages. Parasitology 122: 263-279.
    • (2001) Parasitology , vol.122 , pp. 263-279
    • Courret, N.1    Frehel, C.2    Prina, E.3    Lang, T.4    Antoine, J.C.5
  • 34
    • 84857058509 scopus 로고    scopus 로고
    • Heat shock protein 90 from neglected protozoan parasites
    • Roy N, Nageshan RK, Ranade S, Tatu U, (2012) Heat shock protein 90 from neglected protozoan parasites. Biochim Biophys Acta 1823: 707-711.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 707-711
    • Roy, N.1    Nageshan, R.K.2    Ranade, S.3    Tatu, U.4
  • 35
    • 3042541530 scopus 로고    scopus 로고
    • The heat shock protein 90 of Plasmodium falciparum and antimalarial activity of its inhibitor, geldanamycin
    • Kumar R, Musiyenko A, Barik S, (2003) The heat shock protein 90 of Plasmodium falciparum and antimalarial activity of its inhibitor, geldanamycin. Malar J 2: 30.
    • (2003) Malar J , vol.2 , pp. 30
    • Kumar, R.1    Musiyenko, A.2    Barik, S.3
  • 36
    • 57149123666 scopus 로고    scopus 로고
    • Molecular chaperones in pathogen virulence: emerging new targets for therapy
    • Neckers L, Tatu U, (2008) Molecular chaperones in pathogen virulence: emerging new targets for therapy. Cell Host Microbe 4: 519-527.
    • (2008) Cell Host Microbe , vol.4 , pp. 519-527
    • Neckers, L.1    Tatu, U.2
  • 37
    • 0042855994 scopus 로고    scopus 로고
    • 17AAG: low target binding affinity and potent cell activity-finding an explanation
    • Chiosis G, Huezo H, Rosen N, Mimnaugh E, Whitesell L, et al. (2003) 17AAG: low target binding affinity and potent cell activity-finding an explanation. Mol Cancer Ther 2: 123-129.
    • (2003) Mol Cancer Ther , vol.2 , pp. 123-129
    • Chiosis, G.1    Huezo, H.2    Rosen, N.3    Mimnaugh, E.4    Whitesell, L.5
  • 38
    • 0025098455 scopus 로고
    • Parasitophorous vacuoles of Leishmania amazonensis-infected macrophages maintain an acidic pH
    • Antoine JC, Prina E, Jouanne C, Bongrand P, (1990) Parasitophorous vacuoles of Leishmania amazonensis-infected macrophages maintain an acidic pH. Infect Immun 58: 779-787.
    • (1990) Infect Immun , vol.58 , pp. 779-787
    • Antoine, J.C.1    Prina, E.2    Jouanne, C.3    Bongrand, P.4
  • 39
    • 0025345363 scopus 로고
    • Localization and activity of various lysosomal proteases in Leishmania amazonensis-infected macrophages
    • Prina E, Antoine JC, Wiederanders B, Kirschke H, (1990) Localization and activity of various lysosomal proteases in Leishmania amazonensis-infected macrophages. Infect Immun 58: 1730-1737.
    • (1990) Infect Immun , vol.58 , pp. 1730-1737
    • Prina, E.1    Antoine, J.C.2    Wiederanders, B.3    Kirschke, H.4
  • 40
    • 41649111868 scopus 로고    scopus 로고
    • The innate immune response against Leishmania parasites
    • Liese J, Schleicher U, Bogdan C, (2008) The innate immune response against Leishmania parasites. Immunobiology 213: 377-387.
    • (2008) Immunobiology , vol.213 , pp. 377-387
    • Liese, J.1    Schleicher, U.2    Bogdan, C.3
  • 41
    • 0036831673 scopus 로고    scopus 로고
    • The immunology of susceptibility and resistance to Leishmania major in mice
    • Sacks D, Noben-Trauth N, (2002) The immunology of susceptibility and resistance to Leishmania major in mice. Nat Rev Immunol 2: 845-858.
    • (2002) Nat Rev Immunol , vol.2 , pp. 845-858
    • Sacks, D.1    Noben-Trauth, N.2
  • 42
    • 79956113905 scopus 로고    scopus 로고
    • Hsp90 regulates NADPH oxidase activity and is necessary for superoxide but not hydrogen peroxide production
    • Chen F, Pandey D, Chadli A, Catravas JD, Chen T, et al. (2011) Hsp90 regulates NADPH oxidase activity and is necessary for superoxide but not hydrogen peroxide production. Antioxid Redox Signal 14: 2107-2119.
    • (2011) Antioxid Redox Signal , vol.14 , pp. 2107-2119
    • Chen, F.1    Pandey, D.2    Chadli, A.3    Catravas, J.D.4    Chen, T.5
  • 43
    • 0038486928 scopus 로고    scopus 로고
    • Protein interactions with nitric oxide synthases: controlling the right time, the right place, and the right amount of nitric oxide
    • Kone BC, Kuncewicz T, Zhang W, Yu ZY, (2003) Protein interactions with nitric oxide synthases: controlling the right time, the right place, and the right amount of nitric oxide. Am J Physiol Renal Physiol 285: F178-190.
    • (2003) Am J Physiol Renal Physiol , vol.285
    • Kone, B.C.1    Kuncewicz, T.2    Zhang, W.3    Yu, Z.Y.4
  • 45
    • 0141480200 scopus 로고    scopus 로고
    • Heat shock protein 90 as an endogenous protein enhancer of inducible nitric-oxide synthase
    • Yoshida M, Xia Y, (2003) Heat shock protein 90 as an endogenous protein enhancer of inducible nitric-oxide synthase. J Biol Chem 278: 36953-36958.
    • (2003) J Biol Chem , vol.278 , pp. 36953-36958
    • Yoshida, M.1    Xia, Y.2
  • 46
    • 34848829167 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibitors prolong survival, attenuate inflammation, and reduce lung injury in murine sepsis
    • Chatterjee A, Dimitropoulou C, Drakopanayiotakis F, Antonova G, Snead C, et al. (2007) Heat shock protein 90 inhibitors prolong survival, attenuate inflammation, and reduce lung injury in murine sepsis. Am J Respir Crit Care Med 176: 667-675.
    • (2007) Am J Respir Crit Care Med , vol.176 , pp. 667-675
    • Chatterjee, A.1    Dimitropoulou, C.2    Drakopanayiotakis, F.3    Antonova, G.4    Snead, C.5
  • 47
    • 34347380341 scopus 로고    scopus 로고
    • Inhibition of Hsp90 attenuates inflammation in endotoxin-induced uveitis
    • Poulaki V, Iliaki E, Mitsiades N, Mitsiades CS, Paulus YN, et al. (2007) Inhibition of Hsp90 attenuates inflammation in endotoxin-induced uveitis. FASEB J 21: 2113-2123.
    • (2007) FASEB J , vol.21 , pp. 2113-2123
    • Poulaki, V.1    Iliaki, E.2    Mitsiades, N.3    Mitsiades, C.S.4    Paulus, Y.N.5
  • 48
    • 0037331203 scopus 로고    scopus 로고
    • Geldanamycin inhibits the production of inflammatory cytokines in activated macrophages by reducing the stability and translation of cytokine transcripts
    • Wax S, Piecyk M, Maritim B, Anderson P, (2003) Geldanamycin inhibits the production of inflammatory cytokines in activated macrophages by reducing the stability and translation of cytokine transcripts. Arthritis Rheum 48: 541-550.
    • (2003) Arthritis Rheum , vol.48 , pp. 541-550
    • Wax, S.1    Piecyk, M.2    Maritim, B.3    Anderson, P.4
  • 49
    • 0031090880 scopus 로고    scopus 로고
    • The role of chemokines and accessory cells in the immunoregulation of cutaneous leishmaniasis
    • Moll H (1997) The role of chemokines and accessory cells in the immunoregulation of cutaneous leishmaniasis. Behring Inst Mitt: 73-78.
    • (1997) Behring Inst Mitt , pp. 73-78
    • Moll, H.1
  • 50
    • 0024331482 scopus 로고
    • Tumor necrosis factor plays a protective role in experimental murine cutaneous leishmaniasis
    • Titus RG, Sherry B, Cerami A, (1989) Tumor necrosis factor plays a protective role in experimental murine cutaneous leishmaniasis. J Exp Med 170: 2097-2104.
    • (1989) J Exp Med , vol.170 , pp. 2097-2104
    • Titus, R.G.1    Sherry, B.2    Cerami, A.3
  • 51
    • 0026276529 scopus 로고
    • Type 1 T helper and type 2 T helper cells: functions, regulation and role in protection and disease
    • Romagnani S, (1991) Type 1 T helper and type 2 T helper cells: functions, regulation and role in protection and disease. Int J Clin Lab Res 21: 152-158.
    • (1991) Int J Clin Lab Res , vol.21 , pp. 152-158
    • Romagnani, S.1
  • 52
    • 33744965065 scopus 로고    scopus 로고
    • Endosome sorting and autophagy are essential for differentiation and virulence of Leishmania major
    • Besteiro S, Williams RA, Morrison LS, Coombs GH, Mottram JC, (2006) Endosome sorting and autophagy are essential for differentiation and virulence of Leishmania major. J Biol Chem 281: 11384-11396.
    • (2006) J Biol Chem , vol.281 , pp. 11384-11396
    • Besteiro, S.1    Williams, R.A.2    Morrison, L.S.3    Coombs, G.H.4    Mottram, J.C.5
  • 53
    • 33748300634 scopus 로고    scopus 로고
    • Cysteine peptidases CPA and CPB are vital for autophagy and differentiation in Leishmania mexicana
    • Williams RA, Tetley L, Mottram JC, Coombs GH, (2006) Cysteine peptidases CPA and CPB are vital for autophagy and differentiation in Leishmania mexicana. Mol Microbiol 61: 655-674.
    • (2006) Mol Microbiol , vol.61 , pp. 655-674
    • Williams, R.A.1    Tetley, L.2    Mottram, J.C.3    Coombs, G.H.4
  • 54
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: a double-edged sword
    • Shintani T, Klionsky DJ, (2004) Autophagy in health and disease: a double-edged sword. Science 306: 990-995.
    • (2004) Science , vol.306 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 55
    • 0034884826 scopus 로고    scopus 로고
    • Successful treatment of refractory mucosal leishmaniasis with pentoxifylline plus antimony
    • Lessa HA, Machado P, Lima F, Cruz AA, Bacellar O, et al. (2001) Successful treatment of refractory mucosal leishmaniasis with pentoxifylline plus antimony. Am J Trop Med Hyg 65: 87-89.
    • (2001) Am J Trop Med Hyg , vol.65 , pp. 87-89
    • Lessa, H.A.1    Machado, P.2    Lima, F.3    Cruz, A.A.4    Bacellar, O.5
  • 56
    • 0031029702 scopus 로고    scopus 로고
    • Role of oxidants in microbial pathophysiology
    • Miller RA, Britigan BE, (1997) Role of oxidants in microbial pathophysiology. Clin Microbiol Rev 10: 1-18.
    • (1997) Clin Microbiol Rev , vol.10 , pp. 1-18
    • Miller, R.A.1    Britigan, B.E.2
  • 57
    • 79960206524 scopus 로고    scopus 로고
    • Lesion size correlates with Leishmania antigen-stimulated TNF-α levels in human cutaneous leishmaniasis
    • Oliveira F, Bafica A, Rosato AB, Favali CB, Costa JM, et al. (2011) Lesion size correlates with Leishmania antigen-stimulated TNF-α levels in human cutaneous leishmaniasis. Am J Trop Med Hyg 85: 70-73.
    • (2011) Am J Trop Med Hyg , vol.85 , pp. 70-73
    • Oliveira, F.1    Bafica, A.2    Rosato, A.B.3    Favali, C.B.4    Costa, J.M.5
  • 59
    • 84855457952 scopus 로고    scopus 로고
    • Hsp90 molecular chaperone inhibitors: are we there yet?
    • Neckers L, Workman P, (2012) Hsp90 molecular chaperone inhibitors: are we there yet? Clin Cancer Res 18: 64-76.
    • (2012) Clin Cancer Res , vol.18 , pp. 64-76
    • Neckers, L.1    Workman, P.2
  • 60
    • 70350548428 scopus 로고    scopus 로고
    • 17 AAG for HSP90 inhibition in cancer-from bench to bedside
    • Usmani SZ, Bona R, Li Z, (2009) 17 AAG for HSP90 inhibition in cancer-from bench to bedside. Curr Mol Med 9: 654-664.
    • (2009) Curr Mol Med , vol.9 , pp. 654-664
    • Usmani, S.Z.1    Bona, R.2    Li, Z.3


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