메뉴 건너뛰기




Volumn 5, Issue 2, 2009, Pages 197-204

The P2X7 receptor and intracellular pathogens: A continuing struggle

Author keywords

Apoptosis; ATP; Ecto ATPases; PLD; Purinergic receptors; SNPs

Indexed keywords


EID: 67349167990     PISSN: 15739538     EISSN: 15739546     Source Type: Journal    
DOI: 10.1007/s11302-009-9130-x     Document Type: Review
Times cited : (50)

References (94)
  • 1
    • 11444261151 scopus 로고    scopus 로고
    • Sabotage and exploitation in macrophages parasitized by intracellular protozoans
    • Denkers EY, Butcher BA (2005) Sabotage and exploitation in macrophages parasitized by intracellular protozoans. Trends Parasitol 21(1):35-41
    • (2005) Trends Parasitol , vol.21 , Issue.1 , pp. 35-41
    • Denkers, E.Y.1    Butcher, B.A.2
  • 2
    • 16544363794 scopus 로고    scopus 로고
    • Hijacking of eukaryotic functions by intracellular bacterial pathogens
    • Alonso A, Garcia-del Portillo F (2004) Hijacking of eukaryotic functions by intracellular bacterial pathogens. Int Microbiol 7(3):181-191
    • (2004) Int Microbiol , vol.7 , Issue.3 , pp. 181-191
    • Alonso, A.1    Garcia-del Portillo, F.2
  • 3
    • 32944462309 scopus 로고    scopus 로고
    • Anti-immunology: Evasion of the host immune system by bacterial and viral pathogens
    • Finlay BB, McFadden G (2006) Anti-immunology: Evasion of the host immune system by bacterial and viral pathogens. Cell 124(4):767-782
    • (2006) Cell , vol.124 , Issue.4 , pp. 767-782
    • Finlay, B.B.1    McFadden, G.2
  • 4
    • 0036397097 scopus 로고    scopus 로고
    • Macrophage-mediated innate host defense against protozoan parasites
    • Stafford JL, Neumann NF, Belosevic M (2002) Macrophage-mediated innate host defense against protozoan parasites. Crit Rev Microbiol 28(3):187-248
    • (2002) Crit Rev Microbiol , vol.28 , Issue.3 , pp. 187-248
    • Stafford, J.L.1    Neumann, N.F.2    Belosevic, M.3
  • 5
    • 0036853070 scopus 로고    scopus 로고
    • Evasion of innate immunity by parasitic protozoa
    • Sacks D, Sher A (2002) Evasion of innate immunity by parasitic protozoa. Nat Immunol 3(11):1041-1047
    • (2002) Nat Immunol , vol.3 , Issue.11 , pp. 1041-1047
    • Sacks, D.1    Sher, A.2
  • 6
    • 35349016235 scopus 로고    scopus 로고
    • Recognition of microorganisms and activation of the immune response
    • Medzhitov R (2007) Recognition of microorganisms and activation of the immune response. Nature 449(7164):819-826
    • (2007) Nature , vol.449 , Issue.7164 , pp. 819-826
    • Medzhitov, R.1
  • 7
    • 35348992048 scopus 로고    scopus 로고
    • Manipulation of host-cell pathways by bacterial pathogens
    • Bhavsar AP, Guttman JA, Finlay BB (2007) Manipulation of host-cell pathways by bacterial pathogens. Nature 449(7164):827-834
    • (2007) Nature , vol.449 , Issue.7164 , pp. 827-834
    • Bhavsar, A.P.1    Guttman, J.A.2    Finlay, B.B.3
  • 9
    • 0042978825 scopus 로고    scopus 로고
    • Role of lipid-mediated signal transduction in bacterial internalization
    • Brumell JH, Grinstein S (2003) Role of lipid-mediated signal transduction in bacterial internalization. Cell Microbiol 5(5):287-297
    • (2003) Cell Microbiol , vol.5 , Issue.5 , pp. 287-297
    • Brumell, J.H.1    Grinstein, S.2
  • 10
    • 0032992211 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis phagosome
    • Deretic V, Fratti RA (1999) Mycobacterium tuberculosis phagosome. Mol Microbiol 31(6):1603-1609
    • (1999) Mol Microbiol , vol.31 , Issue.6 , pp. 1603-1609
    • Deretic, V.1    Fratti, R.A.2
  • 11
    • 0033865327 scopus 로고    scopus 로고
    • Intracellular survival by Chlamydia
    • Wyrick PB (2000) Intracellular survival by Chlamydia. Cell Microbiol 2(4):275-282
    • (2000) Cell Microbiol , vol.2 , Issue.4 , pp. 275-282
    • Wyrick, P.B.1
  • 12
    • 0041856096 scopus 로고    scopus 로고
    • Toxoplasma gondii: Perfecting an intracellular life style
    • Sibley LD (2003) Toxoplasma gondii: Perfecting an intracellular life style. Traffic 4(9):581-586
    • (2003) Traffic , vol.4 , Issue.9 , pp. 581-586
    • Sibley, L.D.1
  • 13
    • 0345151828 scopus 로고    scopus 로고
    • Toxoplasma gondii resides in a vacuole that avoids fusion with host cell endocytic and exocytic vesicular trafficking pathways
    • Mordue DG, Hakansson S, Niesman I, Sibley LD (1999) Toxoplasma gondii resides in a vacuole that avoids fusion with host cell endocytic and exocytic vesicular trafficking pathways. Exp Parasitol 92(2):87-99
    • (1999) Exp Parasitol , vol.92 , Issue.2 , pp. 87-99
    • Mordue, D.G.1    Hakansson, S.2    Niesman, I.3    Sibley, L.D.4
  • 14
    • 33845412832 scopus 로고    scopus 로고
    • Intracellular survival of Burkholderia cenocepacia in macrophages is associated with a delay in the maturation of bacteria-containing vacuoles
    • Lamothe J, Huynh KK, Grinstein S, Valvano MA (2007) Intracellular survival of Burkholderia cenocepacia in macrophages is associated with a delay in the maturation of bacteria-containing vacuoles. Cell Microbiol 9(1):40-53
    • (2007) Cell Microbiol , vol.9 , Issue.1 , pp. 40-53
    • Lamothe, J.1    Huynh, K.K.2    Grinstein, S.3    Valvano, M.A.4
  • 15
    • 0033957426 scopus 로고    scopus 로고
    • ATP-induced killing of virulent Mycobacterium tuberculosis within human macrophages requires phospholipase D
    • Kusner DJ, Adams J (2000) ATP-induced killing of virulent Mycobacterium tuberculosis within human macrophages requires phospholipase D. J Immunol 164(1):379-388
    • (2000) J Immunol , vol.164 , Issue.1 , pp. 379-388
    • Kusner, D.J.1    Adams, J.2
  • 16
    • 0035873728 scopus 로고    scopus 로고
    • ATP-mediated killing of Mycobacterium bovis bacille Calmette-Guérin within human macrophages Is calcium dependent and associated with the acidification of mycobacteria-containing phagosomes
    • Stober CB, Lammas DA, Li CM, Kumararatne DS, Lightman SL, McArdle CA (2001) ATP-mediated killing of Mycobacterium bovis bacille Calmette-Guérin within human macrophages Is calcium dependent and associated with the acidification of mycobacteria-containing phagosomes. J Immunol 166(10):6276-6286
    • (2001) J Immunol , vol.166 , Issue.10 , pp. 6276-6286
    • Stober, C.B.1    Lammas, D.A.2    Li, C.M.3    Kumararatne, D.S.4    Lightman, S.L.5    McArdle, C.A.6
  • 18
    • 35748978219 scopus 로고    scopus 로고
    • Effect of the purinergic receptor P2X7 on Chlamydia infection in cervical epithelial cells and vaginally infected mice
    • Darville T, Welter-Stahl L, Cruz C, Sater AA, Andrews CW Jr, Ojcius DM (2007) Effect of the purinergic receptor P2X7 on Chlamydia infection in cervical epithelial cells and vaginally infected mice. J Immunol 179(6):3707-3714
    • (2007) J Immunol , vol.179 , Issue.6 , pp. 3707-3714
    • Darville, T.1    Welter-Stahl, L.2    Cruz, C.3    Sater, A.A.4    Andrews Jr., C.W.5    Ojcius, D.M.6
  • 20
    • 0032411042 scopus 로고    scopus 로고
    • Roles of reactive oxygen species: Signaling and regulation of cellular functions
    • Gamaley IA, Klyubin IV (1999) Roles of reactive oxygen species: signaling and regulation of cellular functions. Int Rev Cytol 188:203-255
    • (1999) Int Rev Cytol , vol.188 , pp. 203-255
    • Gamaley, I.A.1    Klyubin, I.V.2
  • 21
    • 0001952829 scopus 로고    scopus 로고
    • Redox signaling: Hydrogen peroxide as intracellular messenger
    • Rhee SG (1999) Redox signaling: Hydrogen peroxide as intracellular messenger. Exp Mol Med 31(2):53-59
    • (1999) Exp Mol Med , vol.31 , Issue.2 , pp. 53-59
    • Rhee, S.G.1
  • 22
    • 0034141845 scopus 로고    scopus 로고
    • Adenosine triphosphate-induced oxygen radical production and CD11b up-regulation: Ca(++) mobilization and actin reorganization in human eosinophils
    • Dichmann S, Idzko M, Zimpfer U, Hofmann C, Ferrari D, Luttmann W, Virchow C, Di Virgilio F, Norgauer J (2000) Adenosine triphosphate-induced oxygen radical production and CD11b up-regulation: Ca(++) mobilization and actin reorganization in human eosinophils. Blood 95(3):973-978
    • (2000) Blood , vol.95 , Issue.3 , pp. 973-978
    • Dichmann, S.1    Idzko, M.2    Zimpfer, U.3    Hofmann, C.4    Ferrari, D.5    Luttmann, W.6    Virchow, C.7    Di Virgilio, F.8    Norgauer, J.9
  • 24
    • 0035338445 scopus 로고    scopus 로고
    • P2X(7) nucleotide receptor mediation of membrane pore formation and superoxide generation in human promyelocytes and neutrophils
    • Suh BC, Kim JS, Namgung U, Ha H, Kim KT (2001) P2X(7) nucleotide receptor mediation of membrane pore formation and superoxide generation in human promyelocytes and neutrophils. J Immunol 166(11):6754-6763
    • (2001) J Immunol , vol.166 , Issue.11 , pp. 6754-6763
    • Suh, B.C.1    Kim, J.S.2    Namgung, U.3    Ha, H.4    Kim, K.T.5
  • 25
    • 33947660448 scopus 로고    scopus 로고
    • Nucleotide receptor signalling and the generation of reactive oxygen species
    • Guerra AN, Gavala ML, Chung HS, Bertics PJ (2007) Nucleotide receptor signalling and the generation of reactive oxygen species. Purinergic Signal 3:39-51
    • (2007) Purinergic Signal , vol.3 , pp. 39-51
    • Guerra, A.N.1    Gavala, M.L.2    Chung, H.S.3    Bertics, P.J.4
  • 27
    • 0031425953 scopus 로고    scopus 로고
    • Extracellular ATP activates transcription factor NF-kappaB through the P2Z purinoreceptor by selectively targeting NF-kappaB p65
    • Ferrari D, Wesselborg S, Bauer MKA, Schulze-Osthoff K (1997) Extracellular ATP activates transcription factor NF-kappaB through the P2Z purinoreceptor by selectively targeting NF-kappaB p65. J Cell Biol 139(7):1635-1643
    • (1997) J Cell Biol , vol.139 , Issue.7 , pp. 1635-1643
    • Ferrari, D.1    Wesselborg, S.2    Bauer, M.K.A.3    Schulze-Osthoff, K.4
  • 28
    • 34047261260 scopus 로고    scopus 로고
    • ATP activates a reactive oxygen species-dependent oxidative stress response and secretion of proinflammatory cytokines in macrophages
    • Cruz CM, Rinna A, Forman HJ, Ventura AL, Persechini PM, Ojcius DM (2007) ATP activates a reactive oxygen species-dependent oxidative stress response and secretion of proinflammatory cytokines in macrophages. J Biol Chem 282(5):2871-2879
    • (2007) J Biol Chem , vol.282 , Issue.5 , pp. 2871-2879
    • Cruz, C.M.1    Rinna, A.2    Forman, H.J.3    Ventura, A.L.4    Persechini, P.M.5    Ojcius, D.M.6
  • 29
    • 43149114461 scopus 로고    scopus 로고
    • Requirement of reactive oxygen species-dependent activation of ASK1-p38 MAPK pathway for extracellular ATP-induced apoptosis in macrophage
    • Noguchi T, Ishii K, Fukutomi H, Naguro I, Matsuzawa A, Takeda K, Ichijo H (2008) Requirement of reactive oxygen species-dependent activation of ASK1-p38 MAPK pathway for extracellular ATP-induced apoptosis in macrophage. J Biol Chem 283(12):7657-7665
    • (2008) J Biol Chem , vol.283 , Issue.12 , pp. 7657-7665
    • Noguchi, T.1    Ishii, K.2    Fukutomi, H.3    Naguro, I.4    Matsuzawa, A.5    Takeda, K.6    Ichijo, H.7
  • 30
    • 0034881926 scopus 로고    scopus 로고
    • Inhibition of apoptosis by intracellular protozoan parasites
    • Heussler VT, Kuenzi P, Rottenberg S (2001) Inhibition of apoptosis by intracellular protozoan parasites. Int J Parasitol 31(11):1166-1176
    • (2001) Int J Parasitol , vol.31 , Issue.11 , pp. 1166-1176
    • Heussler, V.T.1    Kuenzi, P.2    Rottenberg, S.3
  • 31
    • 12144258602 scopus 로고    scopus 로고
    • Survival of protozoan intracellular parasites in host cells
    • Leiriao P, Rodrigues CD, Albuquerque SS, Mota MM (2004) Survival of protozoan intracellular parasites in host cells. EMBO Rep 5(12):1142-1147
    • (2004) EMBO Rep , vol.5 , Issue.12 , pp. 1142-1147
    • Leiriao, P.1    Rodrigues, C.D.2    Albuquerque, S.S.3    Mota, M.M.4
  • 32
    • 0035479324 scopus 로고    scopus 로고
    • Intracellular protozoan parasites and apoptosis: Diverse strategies to modulate parasite-host interactions
    • Luder CG, Gross U, Lopes MF (2001) Intracellular protozoan parasites and apoptosis: Diverse strategies to modulate parasite-host interactions. Trends Parasitol 17(10):480-486
    • (2001) Trends Parasitol , vol.17 , Issue.10 , pp. 480-486
    • Luder, C.G.1    Gross, U.2    Lopes, M.F.3
  • 33
    • 4844226351 scopus 로고    scopus 로고
    • Chlamydia and apoptosis: Life and death decisions of an intracellular pathogen
    • Byrne GI, Ojcius DM (2004) Chlamydia and apoptosis: Life and death decisions of an intracellular pathogen. Nat Rev Microbiol 2(10):802-808
    • (2004) Nat Rev Microbiol , vol.2 , Issue.10 , pp. 802-808
    • Byrne, G.I.1    Ojcius, D.M.2
  • 34
    • 34247218700 scopus 로고    scopus 로고
    • Host-cell survival and death during Chlamydia infection
    • Ying S, Pettengill M, Ojcius DM, Hacker G (2007) Host-cell survival and death during Chlamydia infection. Curr Immunol Rev 3(1):31-40
    • (2007) Curr Immunol Rev , vol.3 , Issue.1 , pp. 31-40
    • Ying, S.1    Pettengill, M.2    Ojcius, D.M.3    Hacker, G.4
  • 35
    • 0030341154 scopus 로고    scopus 로고
    • Drug use and behavior change
    • Osborn JE (1996) Drug use and behavior change. Am J Public Health 86(12):1698-1699
    • (1996) Am J Public Health , vol.86 , Issue.12 , pp. 1698-1699
    • Osborn, J.E.1
  • 36
    • 0032575705 scopus 로고    scopus 로고
    • A matter of life and cell death
    • Evan G, Littlewood T (1998) A matter of life and cell death. Science 281(5381):1317-1322
    • (1998) Science , vol.281 , Issue.5381 , pp. 1317-1322
    • Evan, G.1    Littlewood, T.2
  • 37
    • 0031577506 scopus 로고    scopus 로고
    • Apoptosis. Clues in the p53 murder mystery
    • Wyllie A (1997) Apoptosis. Clues in the p53 murder mystery. Nature 389(6648):237-238
    • (1997) Nature , vol.389 , Issue.6648 , pp. 237-238
    • Wyllie, A.1
  • 40
    • 33845943950 scopus 로고    scopus 로고
    • Toxoplasma gondii inhibits apoptosis in infected cells by caspase inactivation and NF-kappaB activation
    • Kim JY, Ahn MH, Jun HS, Jung JW, Ryu JS, Min DY (2006) Toxoplasma gondii inhibits apoptosis in infected cells by caspase inactivation and NF-kappaB activation. Yonsei Med J 47(6):862-869
    • (2006) Yonsei Med J , vol.47 , Issue.6 , pp. 862-869
    • Kim, J.Y.1    Ahn, M.H.2    Jun, H.S.3    Jung, J.W.4    Ryu, J.S.5    Min, D.Y.6
  • 42
    • 0032918670 scopus 로고    scopus 로고
    • Trypanosoma cruzi does not induce apoptosis in murine fibroblasts
    • Clark RK, Kuhn RE (1999) Trypanosoma cruzi does not induce apoptosis in murine fibroblasts. Parasitology 118(Pt 2):167-175
    • (1999) Parasitology , vol.118 , Issue.PART 2 , pp. 167-175
    • Clark, R.K.1    Kuhn, R.E.2
  • 43
    • 0028294578 scopus 로고
    • Intracellular infection by Leishmania donovani inhibits macrophage apoptosis
    • Moore KJ, Matlashewski G (1994) Intracellular infection by Leishmania donovani inhibits macrophage apoptosis. J Immunol 152(6):2930-2937
    • (1994) J Immunol , vol.152 , Issue.6 , pp. 2930-2937
    • Moore, K.J.1    Matlashewski, G.2
  • 47
    • 0030840444 scopus 로고    scopus 로고
    • ATP-induced killing of mycobacteria by human macrophages is mediated by purinergic P2Z(P2X7) receptors
    • Lammas DA, Stober C, Harvey CJ, Kendrick N, Panchalingam S, Kumararatne DS (1997) ATP-induced killing of mycobacteria by human macrophages is mediated by purinergic P2Z(P2X7) receptors. Immunity 7:433-444
    • (1997) Immunity , vol.7 , pp. 433-444
    • Lammas, D.A.1    Stober, C.2    Harvey, C.J.3    Kendrick, N.4    Panchalingam, S.5    Kumararatne, D.S.6
  • 48
    • 0028136987 scopus 로고
    • Apoptosis, but not necrosis, of infected monocytes is coupled with killing of intracellular bacillus Calmette-Guérin
    • Molloy A, Laochumroonvorapong P, Kaplan G (1994) Apoptosis, but not necrosis, of infected monocytes is coupled with killing of intracellular bacillus Calmette-Guérin. J Exp Med 180:1499-1509
    • (1994) J Exp Med , vol.180 , pp. 1499-1509
    • Molloy, A.1    Laochumroonvorapong, P.2    Kaplan, G.3
  • 49
    • 40749157178 scopus 로고    scopus 로고
    • ATP scavenging by the intracellular pathogen Porphyromonas gingivalis inhibits P2X7-mediated host-cell apoptosis
    • Yilmaz O, Yao L, Maeda K, Rose TM, Lewis EL, Duman M, Lamont RJ, Ojcius DM (2008) ATP scavenging by the intracellular pathogen Porphyromonas gingivalis inhibits P2X7-mediated host-cell apoptosis. Cell Microbiol 10(4):863-875
    • (2008) Cell Microbiol , vol.10 , Issue.4 , pp. 863-875
    • Yilmaz, O.1    Yao, L.2    Maeda, K.3    Rose, T.M.4    Lewis, E.L.5    Duman, M.6    Lamont, R.J.7    Ojcius, D.M.8
  • 50
    • 0033021431 scopus 로고    scopus 로고
    • Secretion of ATP-utilizing enzymes, nucleoside diphosphate kinase and ATPase, by Mycobacterium bovis BCG: Sequestration of ATP from macrophage P2Z receptors?
    • Zaborina O, Li X, Cheng G, Kapatral V, Chakrabarty AM (1999) Secretion of ATP-utilizing enzymes, nucleoside diphosphate kinase and ATPase, by Mycobacterium bovis BCG: Sequestration of ATP from macrophage P2Z receptors? Mol Microbiol 31(5):1333-1343
    • (1999) Mol Microbiol , vol.31 , Issue.5 , pp. 1333-1343
    • Zaborina, O.1    Li, X.2    Cheng, G.3    Kapatral, V.4    Chakrabarty, A.M.5
  • 51
    • 39049143301 scopus 로고    scopus 로고
    • Leishmania-released nucleoside diphosphate kinase prevents ATP-mediated cytolysis of macrophages
    • Kolli BK, Kostal J, Zaborina O, Chakrabarty AM, Chang KP (2008) Leishmania-released nucleoside diphosphate kinase prevents ATP-mediated cytolysis of macrophages. Mol Biochem Parasitol 158(2):163-175
    • (2008) Mol Biochem Parasitol , vol.158 , Issue.2 , pp. 163-175
    • Kolli, B.K.1    Kostal, J.2    Zaborina, O.3    Chakrabarty, A.M.4    Chang, K.P.5
  • 52
    • 0033800321 scopus 로고    scopus 로고
    • Quaternary structure of nucleoside diphosphate kinases
    • Lascu L, Giartosio A, Ransac S, Erent M (2000) Quaternary structure of nucleoside diphosphate kinases. J Bioenerg Biomembr 32(3):227-236
    • (2000) J Bioenerg Biomembr , vol.32 , Issue.3 , pp. 227-236
    • Lascu, L.1    Giartosio, A.2    Ransac, S.3    Erent, M.4
  • 53
    • 0030904532 scopus 로고    scopus 로고
    • The nucleoside diphosphate kinase of Mycobacterium smegmatis: Identification of proteins that modulate specificity of nucleoside triphosphate synthesis by the enzyme
    • Shankar S, Hershberger CD, Chakrabarty AM (1997) The nucleoside diphosphate kinase of Mycobacterium smegmatis: Identification of proteins that modulate specificity of nucleoside triphosphate synthesis by the enzyme. Mol Microbiol 24(3):477-487
    • (1997) Mol Microbiol , vol.24 , Issue.3 , pp. 477-487
    • Shankar, S.1    Hershberger, C.D.2    Chakrabarty, A.M.3
  • 54
    • 0036606212 scopus 로고    scopus 로고
    • X-ray structure of Mycobacterium tuberculosis nucleoside diphosphate kinase
    • Chen Y, Morera S, Mocan J, Lascu I, Janin J (2002) X-ray structure of Mycobacterium tuberculosis nucleoside diphosphate kinase. Proteins 47(4):556-557
    • (2002) Proteins , vol.47 , Issue.4 , pp. 556-557
    • Chen, Y.1    Morera, S.2    Mocan, J.3    Lascu, I.4    Janin, J.5
  • 55
    • 6344237576 scopus 로고    scopus 로고
    • Amino acid residues involved in autophosphorylation and phosphotransfer activities are distinct in nucleoside diphosphate kinase from Mycobacterium tuberculosis
    • Tiwari S, Kishan KV, Chakrabarti T, Chakraborti PK (2004) Amino acid residues involved in autophosphorylation and phosphotransfer activities are distinct in nucleoside diphosphate kinase from Mycobacterium tuberculosis. J Biol Chem 279(42):43595-43603
    • (2004) J Biol Chem , vol.279 , Issue.42 , pp. 43595-43603
    • Tiwari, S.1    Kishan, K.V.2    Chakrabarti, T.3    Chakraborti, P.K.4
  • 56
    • 0019629774 scopus 로고
    • A calcium regulated adenosine triphosphatase in Entamoeba histolytica
    • McLaughlin J, Muller M (1981) A calcium regulated adenosine triphosphatase in Entamoeba histolytica. Mol Biochem Parasitol 3(6):369-379
    • (1981) Mol Biochem Parasitol , vol.3 , Issue.6 , pp. 369-379
    • McLaughlin, J.1    Muller, M.2
  • 57
    • 0019726485 scopus 로고
    • Entamoeba histolytica: Localization and characterization of ca2+-dependent nucleotidases
    • Takeuchi T, Kobayashi S, Masuda M, Tanabe M, Miura S, Fujiwara T (1981) Entamoeba histolytica: Localization and characterization of ca2+ -dependent nucleotidases. Int J Parasitol 11(3):209-215
    • (1981) Int J Parasitol , vol.11 , Issue.3 , pp. 209-215
    • Takeuchi, T.1    Kobayashi, S.2    Masuda, M.3    Tanabe, M.4    Miura, S.5    Fujiwara, T.6
  • 58
    • 0023274125 scopus 로고
    • Detection of nucleoside triphosphate hydrolase as a circulating antigen in sera of mice infected with Toxoplasma gondii
    • Asai T, Kim TJ, Kobayashi M, Kojima S (1987) Detection of nucleoside triphosphate hydrolase as a circulating antigen in sera of mice infected with Toxoplasma gondii. Infect Immun 55(5):1332-1335
    • (1987) Infect Immun , vol.55 , Issue.5 , pp. 1332-1335
    • Asai, T.1    Kim, T.J.2    Kobayashi, M.3    Kojima, S.4
  • 59
    • 0032583188 scopus 로고    scopus 로고
    • Basis for substrate specificity of the Toxoplasma gondii nucleoside triphosphate hydrolase
    • Nakaar V, Beckers CJ, Polotsky V, Joiner KA (1998) Basis for substrate specificity of the Toxoplasma gondii nucleoside triphosphate hydrolase. Mol Biochem Parasitol 97(1-2):209-220
    • (1998) Mol Biochem Parasitol , vol.97 , Issue.1-2 , pp. 209-220
    • Nakaar, V.1    Beckers, C.J.2    Polotsky, V.3    Joiner, K.A.4
  • 60
    • 0035544894 scopus 로고    scopus 로고
    • Production and characterization of a monoclonal antibody against nucleoside triphosphate hydrolase from Toxoplasma gondii
    • Kikuchi T, Nagata T, Furuta T (2001) Production and characterization of a monoclonal antibody against nucleoside triphosphate hydrolase from Toxoplasma gondii. J Eukaryot Microbiol Suppl:195S-196S
    • (2001) J Eukaryot Microbiol , Issue.SUPPL.
    • Kikuchi, T.1    Nagata, T.2    Furuta, T.3
  • 61
    • 0038353220 scopus 로고    scopus 로고
    • The relationship between nucleoside triphosphate hydrolase (NTPase) isoform and Toxoplasma strain virulence in rat and human toxoplasmosis
    • Johnson M, Broady K, Angelici MC, Johnson A (2003) The relationship between nucleoside triphosphate hydrolase (NTPase) isoform and Toxoplasma strain virulence in rat and human toxoplasmosis. Microbes Infect 5(9):797-806
    • (2003) Microbes Infect , vol.5 , Issue.9 , pp. 797-806
    • Johnson, M.1    Broady, K.2    Angelici, M.C.3    Johnson, A.4
  • 62
    • 0032212406 scopus 로고    scopus 로고
    • Neospora caninum: Tachyzoites express a potent type-I nucleoside triphosphate hydrolase
    • Asai T, Howe DK, Nakajima K, Nozaki T, Takeuchi T, Sibley LD (1998) Neospora caninum: Tachyzoites express a potent type-I nucleoside triphosphate hydrolase. Exp Parasitol 90(3):277-285
    • (1998) Exp Parasitol , vol.90 , Issue.3 , pp. 277-285
    • Asai, T.1    Howe, D.K.2    Nakajima, K.3    Nozaki, T.4    Takeuchi, T.5    Sibley, L.D.6
  • 65
    • 33846785154 scopus 로고    scopus 로고
    • Trypanosoma brucei brucei: Biochemical characterization of ecto-nucleoside triphosphate diphosphohydrolase activities
    • de Souza LM, Thomaz R, Fonseca FV, Panizzutti R, Vercesi AE, Meyer-Fernandes JR (2007) Trypanosoma brucei brucei: Biochemical characterization of ecto-nucleoside triphosphate diphosphohydrolase activities. Exp Parasitol 115(4):315-323
    • (2007) Exp Parasitol , vol.115 , Issue.4 , pp. 315-323
    • de Souza, L.M.1    Thomaz, R.2    Fonseca, F.V.3    Panizzutti, R.4    Vercesi, A.E.5    Meyer-Fernandes, J.R.6
  • 68
    • 33644764769 scopus 로고    scopus 로고
    • Genetic susceptibility to mycobacterial disease in humans
    • Fernando SL, Britton WJ (2006) Genetic susceptibility to mycobacterial disease in humans. Immunol Cell Biol 84(2):125-137
    • (2006) Immunol Cell Biol , vol.84 , Issue.2 , pp. 125-137
    • Fernando, S.L.1    Britton, W.J.2
  • 69
    • 0032429154 scopus 로고    scopus 로고
    • A DNA polymorphism discovery resource for research on human genetic variation
    • Collins FS, Brooks LD, Chakravarti A (1998) A DNA polymorphism discovery resource for research on human genetic variation. Genome Res 8(12):1229-1231
    • (1998) Genome Res , vol.8 , Issue.12 , pp. 1229-1231
    • Collins, F.S.1    Brooks, L.D.2    Chakravarti, A.3
  • 70
    • 33749019111 scopus 로고    scopus 로고
    • Identification of Thr283 as a key determinant of P2X7 receptor function
    • Young MT, Pelegrin P, Surprenant A (2006) Identification of Thr283 as a key determinant of P2X7 receptor function. Br J Pharmacol 149(3):261-268
    • (2006) Br J Pharmacol , vol.149 , Issue.3 , pp. 261-268
    • Young, M.T.1    Pelegrin, P.2    Surprenant, A.3
  • 72
    • 0037196958 scopus 로고    scopus 로고
    • A loss-of-function polymorphic mutation in the cytolytic P2X7 receptor gene and chronic lymphocytic leukaemia: A molecular study
    • Wiley JS, Dao-Ung LP, Gu BJ, Sluyter R, Shemon AN, Li C, Taper J, Gallo J, Manoharan A (2002) A loss-of-function polymorphic mutation in the cytolytic P2X7 receptor gene and chronic lymphocytic leukaemia: A molecular study. Lancet 359(9312):1114-1119
    • (2002) Lancet , vol.359 , Issue.9312 , pp. 1114-1119
    • Wiley, J.S.1    Dao-Ung, L.P.2    Gu, B.J.3    Sluyter, R.4    Shemon, A.N.5    Li, C.6    Taper, J.7    Gallo, J.8    Manoharan, A.9
  • 76
    • 33644798445 scopus 로고    scopus 로고
    • The P2X7 receptor is a candidate product of murine and human lupus susceptibility loci: A hypothesis and comparison of murine allelic products
    • Elliott JI, McVey JH, Higgins CF (2005) The P2X7 receptor is a candidate product of murine and human lupus susceptibility loci: A hypothesis and comparison of murine allelic products. Arthritis Res Ther 7(3):R468-R475
    • (2005) Arthritis Res Ther , vol.7 , Issue.3
    • Elliott, J.I.1    McVey, J.H.2    Higgins, C.F.3
  • 77
    • 33846579222 scopus 로고    scopus 로고
    • Functional P2X7 receptor polymorphisms (His155Tyr, Arg307Gln, Glu496Ala) in patients with Crohn's disease
    • Haas SL, Ruether A, Singer MV, Schreiber S, Bocker U (2007) Functional P2X7 receptor polymorphisms (His155Tyr, Arg307Gln, Glu496Ala) in patients with Crohn's disease. Scand J Immunol 65(2):166-170
    • (2007) Scand J Immunol , vol.65 , Issue.2 , pp. 166-170
    • Haas, S.L.1    Ruether, A.2    Singer, M.V.3    Schreiber, S.4    Bocker, U.5
  • 78
    • 0038143359 scopus 로고    scopus 로고
    • P2X7 mediates superoxide production in primary microglia and is up-regulated in a transgenic mouse model of Alzheimer's disease
    • Parvathenani LK, Tertyshnikova S, Greco CR, Roberts SB, Robertson B, Posmantur R (2003) P2X7 mediates superoxide production in primary microglia and is up-regulated in a transgenic mouse model of Alzheimer's disease. J Biol Chem 278(15):13309-13317
    • (2003) J Biol Chem , vol.278 , Issue.15 , pp. 13309-13317
    • Parvathenani, L.K.1    Tertyshnikova, S.2    Greco, C.R.3    Roberts, S.B.4    Robertson, B.5    Posmantur, R.6
  • 80
    • 33645224970 scopus 로고    scopus 로고
    • COX-2, CB2 and P2X7-immunoreactivities are increased in activated microglial cells/macrophages of multiple sclerosis and amyotrophic lateral sclerosis spinal cord
    • Yiangou Y, Facer P, Durrenberger P, Chessell IP, Naylor A, Bountra C, Banati RR, Anand P (2006) COX-2, CB2 and P2X7-immunoreactivities are increased in activated microglial cells/macrophages of multiple sclerosis and amyotrophic lateral sclerosis spinal cord. BMC Neurol 6:12
    • (2006) BMC Neurol , vol.6 , pp. 12
    • Yiangou, Y.1    Facer, P.2    Durrenberger, P.3    Chessell, I.P.4    Naylor, A.5    Bountra, C.6    Banati, R.R.7    Anand, P.8
  • 81
    • 3242761458 scopus 로고    scopus 로고
    • Major histocompatibility complex class I shedding and programmed cell death stimulated through the proinflammatory P2X7 receptor: A candidate susceptibility gene for NOD diabetes
    • Elliott JI, Higgins CF (2004) Major histocompatibility complex class I shedding and programmed cell death stimulated through the proinflammatory P2X7 receptor: A candidate susceptibility gene for NOD diabetes. Diabetes 53(8):2012-2017
    • (2004) Diabetes , vol.53 , Issue.8 , pp. 2012-2017
    • Elliott, J.I.1    Higgins, C.F.2
  • 82
    • 18144376312 scopus 로고    scopus 로고
    • A 5′ intronic splice site polymorphism leads to a null allele of the P2X7 gene in 1-2% of the Caucasian population
    • Skarratt KK, Fuller SJ, Sluyter R, Dao-Ung LP, Gu BJ, Wiley JS (2005) A 5′ intronic splice site polymorphism leads to a null allele of the P2X7 gene in 1-2% of the Caucasian population. FEBS Lett 579(12):2675-2678
    • (2005) FEBS Lett , vol.579 , Issue.12 , pp. 2675-2678
    • Skarratt, K.K.1    Fuller, S.J.2    Sluyter, R.3    Dao-Ung, L.P.4    Gu, B.J.5    Wiley, J.S.6
  • 85
    • 36849045915 scopus 로고    scopus 로고
    • The inflammasome: A danger sensing complex triggering innate immunity
    • Petrilli V, Dostert C, Muruve DA, Tschopp J (2007) The inflammasome: A danger sensing complex triggering innate immunity. Curr Opin Immunol 19(6):615-622
    • (2007) Curr Opin Immunol , vol.19 , Issue.6 , pp. 615-622
    • Petrilli, V.1    Dostert, C.2    Muruve, D.A.3    Tschopp, J.4
  • 86
    • 34548444551 scopus 로고    scopus 로고
    • Liaisons dangereuses: P2X7 and the inflammasome
    • Di Virgilio F (2007) Liaisons dangereuses: P2X7 and the inflammasome. Trends Pharmacol Sci 28(9):465-472
    • (2007) Trends Pharmacol Sci , vol.28 , Issue.9 , pp. 465-472
    • Di Virgilio, F.1
  • 87
    • 0242662713 scopus 로고    scopus 로고
    • A loss-of-function polymorphism in the human P2X7 receptor abolishes ATP-mediated killing of mycobacteria
    • Saunders BM, Fernando SL, Sluyter R, Britton WJ, Wiley JS (2003) A loss-of-function polymorphism in the human P2X7 receptor abolishes ATP-mediated killing of mycobacteria. J Immunol 171(10):5442-5446
    • (2003) J Immunol , vol.171 , Issue.10 , pp. 5442-5446
    • Saunders, B.M.1    Fernando, S.L.2    Sluyter, R.3    Britton, W.J.4    Wiley, J.S.5
  • 88
    • 8844232668 scopus 로고    scopus 로고
    • P2X7 receptor polymorphism impairs extracellular adenosine 5′-triphosphate-induced interleukin-18 release from human monocytes
    • Sluyter R, Dalitz JG, Wiley JS (2004) P2X7 receptor polymorphism impairs extracellular adenosine 5′-triphosphate-induced interleukin-18 release from human monocytes. Genes Immun 5(7):588-591
    • (2004) Genes Immun , vol.5 , Issue.7 , pp. 588-591
    • Sluyter, R.1    Dalitz, J.G.2    Wiley, J.S.3
  • 89
    • 1542619335 scopus 로고    scopus 로고
    • Glu496 to Ala polymorphism in the P2X7 receptor impairs ATP-induced IL-1 beta release from human monocytes
    • Sluyter R, Shemon AN, Wiley JS (2004) Glu496 to Ala polymorphism in the P2X7 receptor impairs ATP-induced IL-1 beta release from human monocytes. J Immunol 172(6):3399-3405
    • (2004) J Immunol , vol.172 , Issue.6 , pp. 3399-3405
    • Sluyter, R.1    Shemon, A.N.2    Wiley, J.S.3
  • 90
    • 20844450078 scopus 로고    scopus 로고
    • Gene dosage determines the negative effects of polymorphic alleles of the P2X7 receptor on adenosine triphosphate-mediated killing of mycobacteria by human macrophages
    • Fernando SL, Saunders BM, Sluyter R, Skarratt KK, Wiley JS, Britton WJ (2005) Gene dosage determines the negative effects of polymorphic alleles of the P2X7 receptor on adenosine triphosphate-mediated killing of mycobacteria by human macrophages. J Infect Dis 192(1):149-155
    • (2005) J Infect Dis , vol.192 , Issue.1 , pp. 149-155
    • Fernando, S.L.1    Saunders, B.M.2    Sluyter, R.3    Skarratt, K.K.4    Wiley, J.S.5    Britton, W.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.