메뉴 건너뛰기




Volumn 162, Issue 2, 2008, Pages 123-133

5′-p-Fluorosulfonyl benzoyl adenosine inhibits an ecto-ATP-diphosphohydrolase in the tegument surface of Taenia crassiceps cysticerci

Author keywords

Apyrase; ATP diphosphohydrolase; Cestode; Cysticerci; Parasite; Taenia crassiceps

Indexed keywords

5' 4 FLUOROSULFONYLBENZOYLADENOSINE; ADENOSINE DERIVATIVE; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; APYRASE; CYTIDINE DIPHOSPHATE; CYTIDINE TRIPHOSPHATE; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; THYMIDINE TRIPHOSPHATE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE; URIDINE TRIPHOSPHATE; 5' (4 FLUOROSULFONYLBENZOYL)ADENOSINE; 5'-(4-FLUOROSULFONYLBENZOYL)ADENOSINE; ADENOSINE; CD39 ANTIGEN; DRUG DERIVATIVE; ENZYME INHIBITOR; LEUKOCYTE ANTIGEN;

EID: 54049084490     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2008.08.002     Document Type: Article
Times cited : (7)

References (70)
  • 1
    • 0023895790 scopus 로고
    • Neurocysticercosis in México
    • Flisser A. Neurocysticercosis in México. Parasitol Today (1988) 131-137
    • (1988) Parasitol Today , pp. 131-137
    • Flisser, A.1
  • 2
    • 0036900278 scopus 로고    scopus 로고
    • Neurocysticercosis: an update
    • Carpio A. Neurocysticercosis: an update. Lancet Infect Dis 2 (2002) 751-762
    • (2002) Lancet Infect Dis , vol.2 , pp. 751-762
    • Carpio, A.1
  • 3
    • 0032583188 scopus 로고    scopus 로고
    • Basis for substrate specificity of the Toxoplasma gondii nucleoside triphosphate hydrolase
    • Nakaar V., Beckers C.J.M., Polotsky V., and Joiner K.A. Basis for substrate specificity of the Toxoplasma gondii nucleoside triphosphate hydrolase. Mol Biochem Parasitol 97 (1998) 209-220
    • (1998) Mol Biochem Parasitol , vol.97 , pp. 209-220
    • Nakaar, V.1    Beckers, C.J.M.2    Polotsky, V.3    Joiner, K.A.4
  • 5
    • 0034653502 scopus 로고    scopus 로고
    • Ectonucleotide diphosphohydrolase activities in Entamoeba histolytica
    • Barros F.S., De Menezes L.F., Pinheiro A.A.S., et al. Ectonucleotide diphosphohydrolase activities in Entamoeba histolytica. Arch Biochem Biophys 375 (2000) 304-314
    • (2000) Arch Biochem Biophys , vol.375 , pp. 304-314
    • Barros, F.S.1    De Menezes, L.F.2    Pinheiro, A.A.S.3
  • 6
  • 8
    • 0242266131 scopus 로고    scopus 로고
    • Ecto-ATPase activity on the surface of Trypanosoma cruzi and its possible role in the parasite-host cell interaction
    • Bisaggio D.F.R., Peres-Sampaio C.E., Meyer-Fernandes J.R., and Souto-Padrón T. Ecto-ATPase activity on the surface of Trypanosoma cruzi and its possible role in the parasite-host cell interaction. Parasitol Res 91 (2003) 273-282
    • (2003) Parasitol Res , vol.91 , pp. 273-282
    • Bisaggio, D.F.R.1    Peres-Sampaio, C.E.2    Meyer-Fernandes, J.R.3    Souto-Padrón, T.4
  • 9
  • 10
    • 0027411290 scopus 로고
    • Characterization and localization of an ATP-diphosphohydrolase on the external surface of the tegumento of Schistosoma mansoni
    • Vasconcelos E.G., Nascimento P.S., Meirelles M.N.L., Verjovski-Almeida S., and Ferreira S.T. Characterization and localization of an ATP-diphosphohydrolase on the external surface of the tegumento of Schistosoma mansoni. Mol Biochem Parasitol 58 (1993) 205-214
    • (1993) Mol Biochem Parasitol , vol.58 , pp. 205-214
    • Vasconcelos, E.G.1    Nascimento, P.S.2    Meirelles, M.N.L.3    Verjovski-Almeida, S.4    Ferreira, S.T.5
  • 11
    • 0037767919 scopus 로고    scopus 로고
    • Molecular characterization and immunolocalization of Schistosoma mansoni ATP-diphosphohydrolase
    • DeMarco R., Kowaltowski A.T., Mortara R.A., and Verjovski-Almeida S. Molecular characterization and immunolocalization of Schistosoma mansoni ATP-diphosphohydrolase. Bioch Biophys Res Commun 307 (2003) 831-838
    • (2003) Bioch Biophys Res Commun , vol.307 , pp. 831-838
    • DeMarco, R.1    Kowaltowski, A.T.2    Mortara, R.A.3    Verjovski-Almeida, S.4
  • 12
    • 0036720235 scopus 로고    scopus 로고
    • Nucleotidase cascades are catalyzed by secreted proteins of the parasitic nematode Trichinella spiralis
    • Gounaris K. Nucleotidase cascades are catalyzed by secreted proteins of the parasitic nematode Trichinella spiralis. Infect Immun 70 (2002) 4917-4924
    • (2002) Infect Immun , vol.70 , pp. 4917-4924
    • Gounaris, K.1
  • 13
    • 41549104603 scopus 로고    scopus 로고
    • Use of Giardia, which appears to have a single nucleotide-sugar transporter for UDP-GlcNAc, to identify the UDP-Glc transporter of Entamoeba
    • Banerjee S., Cui J., Robbins P.W., and Samuelson J. Use of Giardia, which appears to have a single nucleotide-sugar transporter for UDP-GlcNAc, to identify the UDP-Glc transporter of Entamoeba. Mol Biochem Parasitol 159 (2008) 44-53
    • (2008) Mol Biochem Parasitol , vol.159 , pp. 44-53
    • Banerjee, S.1    Cui, J.2    Robbins, P.W.3    Samuelson, J.4
  • 14
    • 0028036717 scopus 로고
    • Tandemly repeated genes enconde nucleoside triphosphate hydrolase isoforms secreted into the parasitophorous vacuole of Toxoplasma gondii
    • Bermudes D., Peck K.R., Afifi M.A., Beckers C.J.M., and Joiner K.A. Tandemly repeated genes enconde nucleoside triphosphate hydrolase isoforms secreted into the parasitophorous vacuole of Toxoplasma gondii. J Biol Chem 269 (1994) 29252-29260
    • (1994) J Biol Chem , vol.269 , pp. 29252-29260
    • Bermudes, D.1    Peck, K.R.2    Afifi, M.A.3    Beckers, C.J.M.4    Joiner, K.A.5
  • 15
    • 0029811585 scopus 로고    scopus 로고
    • Partial purification and immunohistochemical localization of an ATP diphosphohydrolase from Schistosoma mansoni. Immunological cross reactivities with potato apyrase and Toxoplasma gondii nucleoside triphosphate hydrolase
    • Vasconcelos E.G., Ferreira S.T., Carvalho T.M., et al. Partial purification and immunohistochemical localization of an ATP diphosphohydrolase from Schistosoma mansoni. Immunological cross reactivities with potato apyrase and Toxoplasma gondii nucleoside triphosphate hydrolase. J Biol Chem 271 (1996) 22139-22145
    • (1996) J Biol Chem , vol.271 , pp. 22139-22145
    • Vasconcelos, E.G.1    Ferreira, S.T.2    Carvalho, T.M.3
  • 16
    • 0036181538 scopus 로고    scopus 로고
    • Characterization and cytochemical localization of an ATP diphosphohydrolase from Leishmania amazonensis promastigotes
    • Coimbra E.S., Goncalves-Da-Costa S.C., Corte-Real S., et al. Characterization and cytochemical localization of an ATP diphosphohydrolase from Leishmania amazonensis promastigotes. Parasitology 124 (2002) 137-143
    • (2002) Parasitology , vol.124 , pp. 137-143
    • Coimbra, E.S.1    Goncalves-Da-Costa, S.C.2    Corte-Real, S.3
  • 17
    • 15144358598 scopus 로고    scopus 로고
    • A method for the isolation of tegument syncytium mitochondria from Taenia crassiceps cysticerci and partial characterization of their aerobic metabolism
    • Del Arenal-Mena I.P., Cea-Bonilla A., Moreno-Sánchez R., and Escamilla J.E. A method for the isolation of tegument syncytium mitochondria from Taenia crassiceps cysticerci and partial characterization of their aerobic metabolism. J Parasitol 84 (1998) 461-468
    • (1998) J Parasitol , vol.84 , pp. 461-468
    • Del Arenal-Mena, I.P.1    Cea-Bonilla, A.2    Moreno-Sánchez, R.3    Escamilla, J.E.4
  • 18
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering material
    • Bensadoun A., and Weinstein D. Assay of proteins in the presence of interfering material. Anal Biochem 70 (1976) 241-250
    • (1976) Anal Biochem , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 22
    • 0027518532 scopus 로고
    • The competition plot: a simple test of whether two reactions occur at the same active site
    • Chevillard C., Cárdenas M.L., and Cornish-Bowden A. The competition plot: a simple test of whether two reactions occur at the same active site. Biochem J 289 (1993) 599-604
    • (1993) Biochem J , vol.289 , pp. 599-604
    • Chevillard, C.1    Cárdenas, M.L.2    Cornish-Bowden, A.3
  • 23
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger H., and von Jagow G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal Biochem 199 (1991) 223-231
    • (1991) Anal Biochem , vol.199 , pp. 223-231
    • Schägger, H.1    von Jagow, G.2
  • 24
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of proteins complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schägger H., Cramer W.A., and von Jagow G. Analysis of molecular masses and oligomeric states of proteins complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal Biochem 217 (1994) 220-230
    • (1994) Anal Biochem , vol.217 , pp. 220-230
    • Schägger, H.1    Cramer, W.A.2    von Jagow, G.3
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0032544580 scopus 로고    scopus 로고
    • The transmembrane domains of ectoapyrase (CD39) affect its enzymatic activity and quaternary structure
    • Wang T.F., Ou Y., and Guidotti G. The transmembrane domains of ectoapyrase (CD39) affect its enzymatic activity and quaternary structure. J Biol Chem 273 (1998) 24814-24821
    • (1998) J Biol Chem , vol.273 , pp. 24814-24821
    • Wang, T.F.1    Ou, Y.2    Guidotti, G.3
  • 27
    • 23944459512 scopus 로고    scopus 로고
    • Either the carboxyl- or the amino-terminal region of the human ecto-ATPase (E-NTPDase 2) confers detergent and temperature sensitivity to the chicken ecto-ATP-diphosphohydrolase (E-NTPDase 8)
    • Mukasa T., Lee Y., and Knowles A.F. Either the carboxyl- or the amino-terminal region of the human ecto-ATPase (E-NTPDase 2) confers detergent and temperature sensitivity to the chicken ecto-ATP-diphosphohydrolase (E-NTPDase 8). Biochemistry 44 (2005) 11160-11170
    • (2005) Biochemistry , vol.44 , pp. 11160-11170
    • Mukasa, T.1    Lee, Y.2    Knowles, A.F.3
  • 30
    • 23844541406 scopus 로고    scopus 로고
    • Modified cell ELISA to determined the solubilization of cell surface proteins: applications in GPI-anchored protein purification
    • Bumgarner G.W., Zampell J.C., Nagarajan S., et al. Modified cell ELISA to determined the solubilization of cell surface proteins: applications in GPI-anchored protein purification. J Biochem Biophys Methods 64 (2005) 99-109
    • (2005) J Biochem Biophys Methods , vol.64 , pp. 99-109
    • Bumgarner, G.W.1    Zampell, J.C.2    Nagarajan, S.3
  • 31
    • 0014268295 scopus 로고
    • Studies on the mitochondrial adenosine triphosphatase system. III. Isolation from the oligomycin-sensitive adenosine triphosphatase complex of the factors which bind F1 and determine oligomycin sensitivity of bound F1
    • Tzagoloff A., McLennan D.H., and Byington K.H. Studies on the mitochondrial adenosine triphosphatase system. III. Isolation from the oligomycin-sensitive adenosine triphosphatase complex of the factors which bind F1 and determine oligomycin sensitivity of bound F1. Biochemistry 7 (1968) 1596-1602
    • (1968) Biochemistry , vol.7 , pp. 1596-1602
    • Tzagoloff, A.1    McLennan, D.H.2    Byington, K.H.3
  • 32
    • 0026074512 scopus 로고
    • Calcium pumps of the plasma membrane
    • Carafoli E. Calcium pumps of the plasma membrane. Physiol Rev 71 (1991) 129-153
    • (1991) Physiol Rev , vol.71 , pp. 129-153
    • Carafoli, E.1
  • 33
    • 0029953638 scopus 로고    scopus 로고
    • Inhibition of ATP-diphosphohydrolase (apyrase) of Torpedo electric organ by 5′-p-fluorosulfonyl benzoyladenosine
    • Martí E., Gómez de Aranda I., and Solsona C. Inhibition of ATP-diphosphohydrolase (apyrase) of Torpedo electric organ by 5′-p-fluorosulfonyl benzoyladenosine. Biochim Biophys Acta 1282 (1996) 17-24
    • (1996) Biochim Biophys Acta , vol.1282 , pp. 17-24
    • Martí, E.1    Gómez de Aranda, I.2    Solsona, C.3
  • 34
    • 0034982214 scopus 로고    scopus 로고
    • Characterisation of an ATP diphosphohydrolase (apyrase, EC 3.6.1.5) activity in Trichomonas vaginalis
    • De Aguiar Matos J.A., Pires-Borges F., Tasca T., et al. Characterisation of an ATP diphosphohydrolase (apyrase, EC 3.6.1.5) activity in Trichomonas vaginalis. Int J Parasitol 31 (2001) 770-775
    • (2001) Int J Parasitol , vol.31 , pp. 770-775
    • De Aguiar Matos, J.A.1    Pires-Borges, F.2    Tasca, T.3
  • 35
    • 1242340484 scopus 로고    scopus 로고
    • Characterization of an ectonucleoside triphosphate diphosphohydrolase 1 activity in alkaline phosphatase-depleted rat osseous plate membranes: possible functional involvement in the calcification process
    • Demenis M.A., Furriel R.P.M., and Leone F.A. Characterization of an ectonucleoside triphosphate diphosphohydrolase 1 activity in alkaline phosphatase-depleted rat osseous plate membranes: possible functional involvement in the calcification process. Biochim Biophys Acta 1646 (2003) 216-225
    • (2003) Biochim Biophys Acta , vol.1646 , pp. 216-225
    • Demenis, M.A.1    Furriel, R.P.M.2    Leone, F.A.3
  • 36
    • 0032518553 scopus 로고    scopus 로고
    • Divalent cation dependence and inhibition of Schistosoma mansoni ATP diphosphohydrolase by fluorosulfonylbenzoyl adenosine
    • Torres C.R., Vasconcelos E.G., Ferreira S.T., and Verjovski-Almeida S. Divalent cation dependence and inhibition of Schistosoma mansoni ATP diphosphohydrolase by fluorosulfonylbenzoyl adenosine. Eur J Biochem 251 (1998) 516-521
    • (1998) Eur J Biochem , vol.251 , pp. 516-521
    • Torres, C.R.1    Vasconcelos, E.G.2    Ferreira, S.T.3    Verjovski-Almeida, S.4
  • 37
    • 0037044649 scopus 로고    scopus 로고
    • 5′-p-Fluorosulfonylbenzoyl adenosine inhibits progesterone synthesis in human placental mitochondria
    • Flores-Herrera O., Uribe A., García-Pérez C., Milan R., and Martinez F. 5′-p-Fluorosulfonylbenzoyl adenosine inhibits progesterone synthesis in human placental mitochondria. Biochim Biophys Acta 1585 (2002) 11-18
    • (2002) Biochim Biophys Acta , vol.1585 , pp. 11-18
    • Flores-Herrera, O.1    Uribe, A.2    García-Pérez, C.3    Milan, R.4    Martinez, F.5
  • 38
    • 33747101327 scopus 로고    scopus 로고
    • Leishmania amazonensis: biological and biochemical characterization of ecto-nucleoside triphosphate diphosphohydrolase activities
    • Pinheiro C.M., Martins-Duarte E.S., Ferraro R.B., et al. Leishmania amazonensis: biological and biochemical characterization of ecto-nucleoside triphosphate diphosphohydrolase activities. Exp Parasitol 114 (2006) 16-25
    • (2006) Exp Parasitol , vol.114 , pp. 16-25
    • Pinheiro, C.M.1    Martins-Duarte, E.S.2    Ferraro, R.B.3
  • 39
    • 73649151319 scopus 로고
    • Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase
    • Kitz R., and Wilson I.B. Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase. J Biol Chem 237 (1962) 3245-3249
    • (1962) J Biol Chem , vol.237 , pp. 3245-3249
    • Kitz, R.1    Wilson, I.B.2
  • 40
    • 27244461941 scopus 로고    scopus 로고
    • A Mg-dependent ecto-ATPase in Leishmania amazonensis and its possible role in adenosine acquisition and virulence
    • Berrêdo-Pinho M., Peres-Sampaio C.E., Chrispin P.P.M., et al. A Mg-dependent ecto-ATPase in Leishmania amazonensis and its possible role in adenosine acquisition and virulence. Arch Biochem Biophys 391 (2001) 16-24
    • (2001) Arch Biochem Biophys , vol.391 , pp. 16-24
    • Berrêdo-Pinho, M.1    Peres-Sampaio, C.E.2    Chrispin, P.P.M.3
  • 41
    • 2942717168 scopus 로고    scopus 로고
    • A Mg-dependent ecto-ATPase is increased in the infective stages of Trypanosoma cruzi
    • Meyer-Fernandes J.R., Saad-Nehme J., Peres-Sampaio C.E., et al. A Mg-dependent ecto-ATPase is increased in the infective stages of Trypanosoma cruzi. Pararitol Res 93 (2004) 41-50
    • (2004) Pararitol Res , vol.93 , pp. 41-50
    • Meyer-Fernandes, J.R.1    Saad-Nehme, J.2    Peres-Sampaio, C.E.3
  • 42
    • 0037089425 scopus 로고    scopus 로고
    • Differential catalytic properties and vascular topography of murine nucleoside triphosphate diphosphohydrolase 1 (NTPDase 1) and NTPDase 2 have implications for thromboregulation
    • Sevigny J., Sundberg C., Braun N., et al. Differential catalytic properties and vascular topography of murine nucleoside triphosphate diphosphohydrolase 1 (NTPDase 1) and NTPDase 2 have implications for thromboregulation. Blood 99 (2002) 2801-2809
    • (2002) Blood , vol.99 , pp. 2801-2809
    • Sevigny, J.1    Sundberg, C.2    Braun, N.3
  • 43
    • 0025897435 scopus 로고
    • Identification and localization of ATP-diphosphohydrolase (apyrase) in bovine aorta: relevance to vascular tone and platelet aggregation
    • Cote Y.P., Picher M., St-Jean P., Beliveau R., Potier M., and Beaudoin A.R. Identification and localization of ATP-diphosphohydrolase (apyrase) in bovine aorta: relevance to vascular tone and platelet aggregation. Biochim Biophys Acta 1078 (1991) 187-191
    • (1991) Biochim Biophys Acta , vol.1078 , pp. 187-191
    • Cote, Y.P.1    Picher, M.2    St-Jean, P.3    Beliveau, R.4    Potier, M.5    Beaudoin, A.R.6
  • 44
    • 0033152013 scopus 로고    scopus 로고
    • Inhibition of an ecto-ATP-diphosphohydrolase by azide
    • Knowles A.F., and Nagy A.K. Inhibition of an ecto-ATP-diphosphohydrolase by azide. Eur J Biochem 262 (1999) 349-357
    • (1999) Eur J Biochem , vol.262 , pp. 349-357
    • Knowles, A.F.1    Nagy, A.K.2
  • 45
    • 0036094468 scopus 로고    scopus 로고
    • Purification, characterization, cloning, and expression of the chicken liver ecto-ATP-diphosphohydrolase
    • Knowles A.F., Nagy A.K., Strobel R.S., and Wu-Weis M. Purification, characterization, cloning, and expression of the chicken liver ecto-ATP-diphosphohydrolase. Eur J Biochem 262 (2002) 2373-2382
    • (2002) Eur J Biochem , vol.262 , pp. 2373-2382
    • Knowles, A.F.1    Nagy, A.K.2    Strobel, R.S.3    Wu-Weis, M.4
  • 46
    • 0018801320 scopus 로고
    • Affinity labeling of catalytic subunit of bovine heart muscle cyclic AMP-dependent protein kinase by 5′-p-fluorosulfonylbenzoyl adenosine
    • Hixson C.S., and Krebs E.G. Affinity labeling of catalytic subunit of bovine heart muscle cyclic AMP-dependent protein kinase by 5′-p-fluorosulfonylbenzoyl adenosine. J Biol Chem 254 (1979) 7509-7514
    • (1979) J Biol Chem , vol.254 , pp. 7509-7514
    • Hixson, C.S.1    Krebs, E.G.2
  • 47
    • 0001951142 scopus 로고    scopus 로고
    • Proposed nomenclature for two novel nucleotide hydrolyzing enzyme families expressed on the surface
    • Van Duffel L., and Lemmens R. (Eds), Sharker Publishing BV, Maastricht, Germany
    • Zimmerman H., Beaudoin A.R., Bollen M., et al. Proposed nomenclature for two novel nucleotide hydrolyzing enzyme families expressed on the surface. In: Van Duffel L., and Lemmens R. (Eds). Ecto-ATPases and related ectonucleotidases (2000), Sharker Publishing BV, Maastricht, Germany 1-8
    • (2000) Ecto-ATPases and related ectonucleotidases , pp. 1-8
    • Zimmerman, H.1    Beaudoin, A.R.2    Bollen, M.3
  • 48
    • 0035033156 scopus 로고    scopus 로고
    • Ectonucleotidases: some recent developments and a note on nomenclature
    • Zimmerman H. Ectonucleotidases: some recent developments and a note on nomenclature. Drug Dev Res 52 (2001) 44-56
    • (2001) Drug Dev Res , vol.52 , pp. 44-56
    • Zimmerman, H.1
  • 49
    • 12644288616 scopus 로고    scopus 로고
    • Identification and characterization of CD39 vascular ATP-diphosphohydrolase
    • Kaczmarek E., Kosiak K., Sévigny J., et al. Identification and characterization of CD39 vascular ATP-diphosphohydrolase. J Biol Chem 271 (1996) 33116-33122
    • (1996) J Biol Chem , vol.271 , pp. 33116-33122
    • Kaczmarek, E.1    Kosiak, K.2    Sévigny, J.3
  • 51
    • 0003740712 scopus 로고    scopus 로고
    • The C-terminal cysteine-rich region dictates specific catalytic properties in chimeras of the ecto-nucleotidases NTPDase-1 and NTPDase-2
    • Heine P., Braun N., Sévigny J., Robson S.C., Servos J., and Zimmerman H. The C-terminal cysteine-rich region dictates specific catalytic properties in chimeras of the ecto-nucleotidases NTPDase-1 and NTPDase-2. Eur J Biochem 262 (2001) 102-107
    • (2001) Eur J Biochem , vol.262 , pp. 102-107
    • Heine, P.1    Braun, N.2    Sévigny, J.3    Robson, S.C.4    Servos, J.5    Zimmerman, H.6
  • 52
    • 0030721511 scopus 로고    scopus 로고
    • An ecto-ATPase and a ecto-ATP diphosphohydrolase are expressed in rat brain
    • Kegel B., Braun N., Heine P., Maliszewski C.R., and Zimmerman H. An ecto-ATPase and a ecto-ATP diphosphohydrolase are expressed in rat brain. Neuropharmacology 36 (1997) 1189-1200
    • (1997) Neuropharmacology , vol.36 , pp. 1189-1200
    • Kegel, B.1    Braun, N.2    Heine, P.3    Maliszewski, C.R.4    Zimmerman, H.5
  • 53
    • 0031012542 scopus 로고    scopus 로고
    • Complementary DNA cloning and sequencing of the chicken mucle ecto-ATPase-homology with the lymphoid cell activation antigen CD39
    • Kirley T.L. Complementary DNA cloning and sequencing of the chicken mucle ecto-ATPase-homology with the lymphoid cell activation antigen CD39. J Biol Chem 272 (1997) 1076-1081
    • (1997) J Biol Chem , vol.272 , pp. 1076-1081
    • Kirley, T.L.1
  • 54
    • 0032862590 scopus 로고    scopus 로고
    • Functional expression of a cDNA encoding a human ecto-ATPase
    • Mateo J., Harden T.K., and Boyer J.L. Functional expression of a cDNA encoding a human ecto-ATPase. Br J Pharmacol 128 (1999) 396-402
    • (1999) Br J Pharmacol , vol.128 , pp. 396-402
    • Mateo, J.1    Harden, T.K.2    Boyer, J.L.3
  • 55
    • 0032575263 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases
    • Smith T.M., and Kirley T.L. Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases. Biochim Biophys Acta 1386 (1998) 65-78
    • (1998) Biochim Biophys Acta , vol.1386 , pp. 65-78
    • Smith, T.M.1    Kirley, T.L.2
  • 56
    • 0033524467 scopus 로고    scopus 로고
    • Site-directed mutagenesis of a human brain ecto-apyrase: evidences that the E-type ATPases are related to the actin/heat shock 70/sugar kinase superfamily
    • Smith T.M., and Kirley T.L. Site-directed mutagenesis of a human brain ecto-apyrase: evidences that the E-type ATPases are related to the actin/heat shock 70/sugar kinase superfamily. Biochemistry 38 (1999) 321-328
    • (1999) Biochemistry , vol.38 , pp. 321-328
    • Smith, T.M.1    Kirley, T.L.2
  • 57
    • 0037065699 scopus 로고    scopus 로고
    • Transmembrane domains confer different substrate specificities and adenosine diphosphate hydrolysis mechanisms on CD39, CD39L1, and chimeras
    • Grinthal A., and Guidotti G. Transmembrane domains confer different substrate specificities and adenosine diphosphate hydrolysis mechanisms on CD39, CD39L1, and chimeras. Biochemistry 41 (2002) 1947-1956
    • (2002) Biochemistry , vol.41 , pp. 1947-1956
    • Grinthal, A.1    Guidotti, G.2
  • 58
    • 0034635168 scopus 로고    scopus 로고
    • Substitution of His59 converts CD39 apyrase into an ADPase in a quaternary astructure dependent manner
    • Grinthal A., and Guidotti G. Substitution of His59 converts CD39 apyrase into an ADPase in a quaternary astructure dependent manner. Biochemistry 39 (2000) 9-16
    • (2000) Biochemistry , vol.39 , pp. 9-16
    • Grinthal, A.1    Guidotti, G.2
  • 59
    • 0034805154 scopus 로고    scopus 로고
    • Soluble apyrase release ADP during ATP hydrolysis
    • Chen W., and Guidotti G. Soluble apyrase release ADP during ATP hydrolysis. Biochem Biophys Res Comm 282 (2001) 90-95
    • (2001) Biochem Biophys Res Comm , vol.282 , pp. 90-95
    • Chen, W.1    Guidotti, G.2
  • 60
    • 0038070596 scopus 로고    scopus 로고
    • Determination of native oligomeric state and substrate specificity of rat NTPDase1 and NTPDase2 after heterologous expresión in Xenopus oocytes
    • Failer B.U., Aschrafi A., Schmalzing G., and Zimmerman H. Determination of native oligomeric state and substrate specificity of rat NTPDase1 and NTPDase2 after heterologous expresión in Xenopus oocytes. Eur J Biochem 270 (2003) 1802-1809
    • (2003) Eur J Biochem , vol.270 , pp. 1802-1809
    • Failer, B.U.1    Aschrafi, A.2    Schmalzing, G.3    Zimmerman, H.4
  • 61
    • 0033563017 scopus 로고    scopus 로고
    • Functional characterization of rat ecto-ATPase and ecto-ATP-diphosphohydrolase after heterologous expression in CHO cells
    • Heine P., Braun N., Heilbronn A., and Zimmerman H. Functional characterization of rat ecto-ATPase and ecto-ATP-diphosphohydrolase after heterologous expression in CHO cells. Eur J Biochem 262 (1999) 102-107
    • (1999) Eur J Biochem , vol.262 , pp. 102-107
    • Heine, P.1    Braun, N.2    Heilbronn, A.3    Zimmerman, H.4
  • 62
    • 0042928440 scopus 로고    scopus 로고
    • Purification and characterization of NTPDase-1 (ecto-apyrase) and NTPDase-2 (ecto-ATPase) from porcine brain cortex synaptosomes
    • Kukulski F., and Komoszynski M. Purification and characterization of NTPDase-1 (ecto-apyrase) and NTPDase-2 (ecto-ATPase) from porcine brain cortex synaptosomes. Eur J Biochem 270 (2003) 3447-3454
    • (2003) Eur J Biochem , vol.270 , pp. 3447-3454
    • Kukulski, F.1    Komoszynski, M.2
  • 63
    • 0035253835 scopus 로고    scopus 로고
    • Nucleotide receptors: an emerging family of regulatory molecules in blood cells
    • Di Virgilio F., Chiozzi P., Ferrari D., et al. Nucleotide receptors: an emerging family of regulatory molecules in blood cells. Blood 97 (2001) 587-600
    • (2001) Blood , vol.97 , pp. 587-600
    • Di Virgilio, F.1    Chiozzi, P.2    Ferrari, D.3
  • 64
    • 0035843178 scopus 로고    scopus 로고
    • Identification of the platelet ADP receptor targeted by antithrombotic drugs
    • Hollopeter G., Jantzen H.M., Vincent D., et al. Identification of the platelet ADP receptor targeted by antithrombotic drugs. Nature 409 (2001) 202-207
    • (2001) Nature , vol.409 , pp. 202-207
    • Hollopeter, G.1    Jantzen, H.M.2    Vincent, D.3
  • 65
    • 0035040532 scopus 로고    scopus 로고
    • Molecular approach to adenoside receptors: receptor-mediated mechanisms of tissue protection
    • Linden J. Molecular approach to adenoside receptors: receptor-mediated mechanisms of tissue protection. Annu Rev Pharmacol Toxicol 41 (2001) 775-787
    • (2001) Annu Rev Pharmacol Toxicol , vol.41 , pp. 775-787
    • Linden, J.1
  • 66
    • 0020509934 scopus 로고
    • A next function for platelet: IgE-dependent killing of Schistosoma
    • Joseph M., Auriault C., Capron A., Vorng H., and Viens P. A next function for platelet: IgE-dependent killing of Schistosoma. Nature 303 (1983) 810-812
    • (1983) Nature , vol.303 , pp. 810-812
    • Joseph, M.1    Auriault, C.2    Capron, A.3    Vorng, H.4    Viens, P.5
  • 67
    • 0022619361 scopus 로고
    • Rat resistance to Schistosomiasis: platelet-mediated cytotoxicity induced by C-reactive protein
    • Bout D., Joseph M., Pontet M., Vorng H., Deslée D., and Capron A. Rat resistance to Schistosomiasis: platelet-mediated cytotoxicity induced by C-reactive protein. Science 31 (1986) 153-156
    • (1986) Science , vol.31 , pp. 153-156
    • Bout, D.1    Joseph, M.2    Pontet, M.3    Vorng, H.4    Deslée, D.5    Capron, A.6
  • 68
    • 0019497464 scopus 로고
    • Present concept on the mechanism of platelet aggregation
    • Vargaftig B.B., Chignard M., and Benveniste J. Present concept on the mechanism of platelet aggregation. Biochem Pharmacol 30 (1981) 263-271
    • (1981) Biochem Pharmacol , vol.30 , pp. 263-271
    • Vargaftig, B.B.1    Chignard, M.2    Benveniste, J.3
  • 69
    • 0031914973 scopus 로고    scopus 로고
    • Molecular basis for ADP-induced platelet activation. I. Evidence for three distinct ADP receptors on human platelets
    • Daniel J.L., Dangelmainer C., Jin J., Ashby B., Smith J.B., and Kunapuli S.P. Molecular basis for ADP-induced platelet activation. I. Evidence for three distinct ADP receptors on human platelets. J Biol Chem 273 (1998) 2024-2039
    • (1998) J Biol Chem , vol.273 , pp. 2024-2039
    • Daniel, J.L.1    Dangelmainer, C.2    Jin, J.3    Ashby, B.4    Smith, J.B.5    Kunapuli, S.P.6
  • 70
    • 0035865519 scopus 로고    scopus 로고
    • Adenosinediphosphate strongly potentiates the ability of the chemokines MDC, TARC, and SDF-1 to stimulate platelet function
    • Gear A.R., Suttitanamongkol S., Viisoreanu D., Polanowska-Grabowska R.K., Raha S., and Camerini D. Adenosinediphosphate strongly potentiates the ability of the chemokines MDC, TARC, and SDF-1 to stimulate platelet function. Blood 97 (2001) 937-945
    • (2001) Blood , vol.97 , pp. 937-945
    • Gear, A.R.1    Suttitanamongkol, S.2    Viisoreanu, D.3    Polanowska-Grabowska, R.K.4    Raha, S.5    Camerini, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.