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Volumn 108, Issue 2, 2011, Pages 79-83

The Pharmacological Role of Phosphatases (Acid and Alkaline Phosphomonoesterases) in Snake Venoms related to Release of Purines - a Multitoxin

Author keywords

[No Author keywords available]

Indexed keywords

ACID PHOSPHATASE; ADENOSINE; ADENOSINE 3' PHOSPHATE; ADENOSINE A3 RECEPTOR; ADENOSINE PHOSPHATE; ALKALINE PHOSPHATASE; DEOXYRIBONUCLEASE; INOSINE; PURINE DERIVATIVE; RIBONUCLEASE; SNAKE VENOM;

EID: 78651442122     PISSN: 17427835     EISSN: 17427843     Source Type: Journal    
DOI: 10.1111/j.1742-7843.2010.00630.x     Document Type: Review
Times cited : (20)

References (57)
  • 1
    • 0000404720 scopus 로고
    • Snake Venoms, Handbook of Exp. Pharmacol.
    • In: Lee CY (ed.). Springer-Verlag, Berlin.
    • Bieber AL. Metal and nonprotein constituents in snake venoms. In: Lee CY (ed.). Snake Venoms, Handbook of Exp. Pharmacol.Springer-Verlag, Berlin. 1979; 295-306.
    • (1979) Metal and nonprotein constituents in snake venoms , pp. 295-306
    • Bieber, A.L.1
  • 2
    • 0036135117 scopus 로고    scopus 로고
    • Ophidian envenomation strategies and the role of purines
    • Aird SD. Ophidian envenomation strategies and the role of purines. Toxicon 2002;40:335-93.
    • (2002) Toxicon , vol.40 , pp. 335-393
    • Aird, S.D.1
  • 3
    • 11144273861 scopus 로고    scopus 로고
    • Taxonomic distribution and quantitative analysis of free purine and pyrimidine nucleosides in snake venoms
    • Aird SD. Taxonomic distribution and quantitative analysis of free purine and pyrimidine nucleosides in snake venoms. Comp Biochem Physiol B Biochem Mol Biol 2005;140:109-26.
    • (2005) Comp Biochem Physiol B Biochem Mol Biol , vol.140 , pp. 109-126
    • Aird, S.D.1
  • 4
    • 0025931518 scopus 로고
    • Snake venom variability: methods of study, results and interpretation
    • Chippaux JP, Williams V, White J. Snake venom variability: methods of study, results and interpretation. Toxicon 1991;29:1279-303.
    • (1991) Toxicon , vol.29 , pp. 1279-1303
    • Chippaux, J.P.1    Williams, V.2    White, J.3
  • 5
    • 0026608648 scopus 로고
    • Variation in the composition of the venom from a single specimen of Pseudonaja textilis (common brown snake) over one year
    • Williams V, White J. Variation in the composition of the venom from a single specimen of Pseudonaja textilis (common brown snake) over one year. Toxicon 1992;30:202-6.
    • (1992) Toxicon , vol.30 , pp. 202-206
    • Williams, V.1    White, J.2
  • 6
    • 0036843052 scopus 로고    scopus 로고
    • Influences on venom yield in Australian tigersnakes (Notechis scutatus) and brownsnakes (Pseudonaja textilis: Elapidae, Serpentes)
    • Mirtschin PJ, Shine R, Nias TJ, Dunstan NL, Hough BJ, Mirtschin M. Influences on venom yield in Australian tigersnakes (Notechis scutatus) and brownsnakes (Pseudonaja textilis: Elapidae, Serpentes). Toxicon 2002;40:1581-92.
    • (2002) Toxicon , vol.40 , pp. 1581-1592
    • Mirtschin, P.J.1    Shine, R.2    Nias, T.J.3    Dunstan, N.L.4    Hough, B.J.5    Mirtschin, M.6
  • 7
    • 0036490361 scopus 로고    scopus 로고
    • Geographic and ontogenic variability in the venom of the neotropical rattlesnake Crotalus durissus: pathophysiological and therapeutic implications
    • Saravia P, Rojas E, Arce V, Guevara C, Lopez JC, Chaves E et al. Geographic and ontogenic variability in the venom of the neotropical rattlesnake Crotalus durissus: pathophysiological and therapeutic implications. Rev Biol Trop 2002;50:337-46.
    • (2002) Rev Biol Trop , vol.50 , pp. 337-346
    • Saravia, P.1    Rojas, E.2    Arce, V.3    Guevara, C.4    Lopez, J.C.5    Chaves, E.6
  • 8
    • 0036191479 scopus 로고    scopus 로고
    • Variations in biochemical and pharmacological properties of Indian cobra (Naja naja naja) venom due to geographical distribution
    • Shashidharamurthy R, Jagadeesha DK, Girish KS, Kemparaju K. Variations in biochemical and pharmacological properties of Indian cobra (Naja naja naja) venom due to geographical distribution. Mol Cell Biochem 2002;229:93-101.
    • (2002) Mol Cell Biochem , vol.229 , pp. 93-101
    • Shashidharamurthy, R.1    Jagadeesha, D.K.2    Girish, K.S.3    Kemparaju, K.4
  • 9
    • 0035034440 scopus 로고    scopus 로고
    • Prey specificity, comparative lethality and compositional differences of coral snake venoms
    • Jorge da Silva N Jr, Aird SD. Prey specificity, comparative lethality and compositional differences of coral snake venoms. Comp Biochem Physiol C Toxicol Pharmacol 2001;128:425-56.
    • (2001) Comp Biochem Physiol C Toxicol Pharmacol , vol.128 , pp. 425-456
    • Jorge da Silva Jr, N.1    Aird, S.D.2
  • 10
    • 8144222740 scopus 로고    scopus 로고
    • Feeding behavior and venom toxicity of coral snake Micrurus nigrocinctus (Serpentes: Elapidae) on its natural prey in captivity
    • Urdaneta AH, Bolanos F, Gutierrez JM. Feeding behavior and venom toxicity of coral snake Micrurus nigrocinctus (Serpentes: Elapidae) on its natural prey in captivity. Comp Biochem Physiol C Toxicol Pharmacol 2004;138:485-92.
    • (2004) Comp Biochem Physiol C Toxicol Pharmacol , vol.138 , pp. 485-492
    • Urdaneta, A.H.1    Bolanos, F.2    Gutierrez, J.M.3
  • 11
    • 33749384362 scopus 로고    scopus 로고
    • Denmotoxin, a three-finger toxin from the colubrid snake Boiga dendrophila (Mangrove Catsnake) with bird-specific activity
    • Pawlak J, Mackessy SP, Fry BG, Bhatia M, Mourier G, Fruchart-Gaillard C et al. Denmotoxin, a three-finger toxin from the colubrid snake Boiga dendrophila (Mangrove Catsnake) with bird-specific activity. J Biol Chem 2006;281:29030-41.
    • (2006) J Biol Chem , vol.281 , pp. 29030-29041
    • Pawlak, J.1    Mackessy, S.P.2    Fry, B.G.3    Bhatia, M.4    Mourier, G.5    Fruchart-Gaillard, C.6
  • 12
    • 0023125054 scopus 로고
    • The origin of snakes and evolution of the venom apparatus
    • Kochva EA. The origin of snakes and evolution of the venom apparatus. Toxicon 1987;25:65-106.
    • (1987) Toxicon , vol.25 , pp. 65-106
    • Kochva, E.A.1
  • 13
    • 15544369378 scopus 로고    scopus 로고
    • From genome to "venome": molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins
    • Fry BG. From genome to "venome": molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins. Genome Res 2005;1:403-20.
    • (2005) Genome Res , vol.1 , pp. 403-420
    • Fry, B.G.1
  • 14
    • 0004129553 scopus 로고    scopus 로고
    • Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism
    • In: Kini RM (ed.). John Wiley and Sons, New York.
    • 2-A complex multifunctional puzzle. In: Kini RM (ed.). Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism. John Wiley and Sons, New York, 1997; 1-28.
    • (1997) 2-A complex multifunctional puzzle , pp. 1-28
    • Kini, R.M.1
  • 15
    • 0033731921 scopus 로고    scopus 로고
    • Snake venom metalloproteinases: their role in the pathogenesis of local tissue damage
    • Gutierrez JM, Rucavado A. Snake venom metalloproteinases: their role in the pathogenesis of local tissue damage. Biochimie 2000;82:841-50.
    • (2000) Biochimie , vol.82 , pp. 841-850
    • Gutierrez, J.M.1    Rucavado, A.2
  • 16
    • 78651429523 scopus 로고    scopus 로고
    • Enzymes from Snake Venoms
    • In: Bailey GS (ed.). Alaken Press, Ft. Collins.
    • Rael ED. Venom Phosphatases and 5'Nucleotidase. In: Bailey GS (ed.). Enzymes from Snake VenomsAlaken Press, Ft. Collins, 1998; 405-22.
    • (1998) Venom Phosphatases and 5'Nucleotidase , pp. 405-422
    • Rael, E.D.1
  • 17
    • 10644233811 scopus 로고    scopus 로고
    • The in vitro and in vivo pharmacological activity of Boiga dendrophila (mangrove catsnake) venom
    • Lumsden NG, Fry BG, Ventura S, Kini RM, Hodgson WC. The in vitro and in vivo pharmacological activity of Boiga dendrophila (mangrove catsnake) venom. Auton Autacoid Pharmacol 2004;2:107-13.
    • (2004) Auton Autacoid Pharmacol , vol.2 , pp. 107-113
    • Lumsden, N.G.1    Fry, B.G.2    Ventura, S.3    Kini, R.M.4    Hodgson, W.C.5
  • 18
    • 0031754497 scopus 로고    scopus 로고
    • Receptors for purines and pyrimidines
    • Ralevic V, Burnstock G. Receptors for purines and pyrimidines. Pharmacol Rev 1998;5:413-92.
    • (1998) Pharmacol Rev , vol.5 , pp. 413-492
    • Ralevic, V.1    Burnstock, G.2
  • 19
    • 33747423674 scopus 로고    scopus 로고
    • Purinergic signalling--an overview
    • Burnstock G. Purinergic signalling--an overview. Novartis Found Symp 2006;276:26-48.
    • (2006) Novartis Found Symp , vol.276 , pp. 26-48
    • Burnstock, G.1
  • 20
    • 36349022149 scopus 로고    scopus 로고
    • Adenosine and ATP receptors
    • Sawynok J. Adenosine and ATP receptors. Handb Exp Pharmacol 2007;177:309-28.
    • (2007) Handb Exp Pharmacol , vol.177 , pp. 309-328
    • Sawynok, J.1
  • 21
    • 0016148838 scopus 로고
    • Correlations between the enzymatic activities and the factors active on blood coagulation and platelet aggregation from the venom of Vipera aspis
    • Boffa MC, Boffa GA. Correlations between the enzymatic activities and the factors active on blood coagulation and platelet aggregation from the venom of Vipera aspis. Biochim Biophys Acta 1974;35:275-90.
    • (1974) Biochim Biophys Acta , vol.35 , pp. 275-290
    • Boffa, M.C.1    Boffa, G.A.2
  • 22
    • 0021038657 scopus 로고
    • Inhibition of platelet aggregation by 5'-nucleotidase purified from Trimeresurus gramineus snake venom
    • Ouyang C, Huang TF. Inhibition of platelet aggregation by 5'-nucleotidase purified from Trimeresurus gramineus snake venom. Toxicon 1983;2:491-501.
    • (1983) Toxicon , vol.2 , pp. 491-501
    • Ouyang, C.1    Huang, T.F.2
  • 23
    • 0022998890 scopus 로고
    • Platelet aggregation inhibitor from Agkistrodon acutus snake venom
    • Ouyang C, Huang TF. Platelet aggregation inhibitor from Agkistrodon acutus snake venom. Toxicon 1986;2:1099-106.
    • (1986) Toxicon , vol.2 , pp. 1099-1106
    • Ouyang, C.1    Huang, T.F.2
  • 24
    • 33747761323 scopus 로고    scopus 로고
    • Anticoagulant effect of Naja naja venom 5'nucleotidase: demonstration through the use of novel specific inhibitor, vanillic acid
    • Dhananjaya BL, Nataraju A, Rajesh R, Raghavendra Gowda CD, Sharath BK, Vishwanath BS et al. Anticoagulant effect of Naja naja venom 5'nucleotidase: demonstration through the use of novel specific inhibitor, vanillic acid. Toxicon 2006;4:411-21.
    • (2006) Toxicon , vol.4 , pp. 411-421
    • Dhananjaya, B.L.1    Nataraju, A.2    Rajesh, R.3    Raghavendra Gowda, C.D.4    Sharath, B.K.5    Vishwanath, B.S.6
  • 25
    • 0002370964 scopus 로고
    • Snake venoms, Handbook of Exp. Pharmacol
    • In: Hornburg H (ed.). Springer-Verlag, Berlin.
    • Iwanaga S, Suzuki T. Enzymes in snake venom. In: Hornburg H (ed.). Snake venoms, Handbook of Exp. Pharmacol. Springer-Verlag, Berlin, 1979; 52: 61-158.
    • (1979) Enzymes in snake venom , vol.52 , pp. 61-158
    • Iwanaga, S.1    Suzuki, T.2
  • 26
    • 84913296545 scopus 로고
    • Phosphatases
    • Uzawa SJ. Phosphatases. Biochem 1932;15:19.
    • (1932) Biochem , vol.15 , pp. 19
    • Uzawa, S.J.1
  • 27
    • 0013866250 scopus 로고
    • Acid and alkaline phosphomonoesterase activities in snake venoms
    • Tu AT, Chua A. Acid and alkaline phosphomonoesterase activities in snake venoms. Comp Biochem Physiol 1966;17: 297-307.
    • (1966) Comp Biochem Physiol , vol.17 , pp. 297-307
    • Tu, A.T.1    Chua, A.2
  • 28
    • 0007575469 scopus 로고
    • Studies on sea snake venom. VI. Pharmacological properties of Laticauda semifasciata venom and purification of toxic components, acid phosphomonoesterase and Phospholipase A in the venom
    • Uwatoko-Setoguchi Y. Studies on sea snake venom. VI. Pharmacological properties of Laticauda semifasciata venom and purification of toxic components, acid phosphomonoesterase and Phospholipase A in the venom. Acta Med Univ Kagoshima 1970;12:73-96.
    • (1970) Acta Med Univ Kagoshima , vol.12 , pp. 73-96
    • Uwatoko-Setoguchi, Y.1
  • 30
    • 73649209802 scopus 로고
    • A specific and nonspecific alkaline monophosphatase in the venom of Bothrops atrox and their occurrence in the purified venom phosphodiesterase
    • Sulkowski E, Bjork W, Laskowski M Sr. A specific and nonspecific alkaline monophosphatase in the venom of Bothrops atrox and their occurrence in the purified venom phosphodiesterase. J Biol Chem 1963;238:2477-86.
    • (1963) J Biol Chem , vol.238 , pp. 2477-2486
    • Sulkowski, E.1    Bjork, W.2    Laskowski Sr, M.3
  • 31
    • 0007534852 scopus 로고
    • Studies on snake venom. IV. Purification of alkaline phosphatases in cobra venoms
    • Suzuki T, Iwanaga S. Studies on snake venom. IV. Purification of alkaline phosphatases in cobra venoms. J Pharm Soc Jpn 1958;78:368-75.
    • (1958) J Pharm Soc Jpn , vol.78 , pp. 368-375
    • Suzuki, T.1    Iwanaga, S.2
  • 32
    • 0001250437 scopus 로고
    • Studies on snake venom. III. Purification of some enzymes in Japanese Mamushi venom (Agistrodon halys blomhoffii, Boie)
    • Suzuki T, Iwanaga S. Studies on snake venom. III. Purification of some enzymes in Japanese Mamushi venom (Agistrodon halys blomhoffii, Boie). J Pharm Soc Jap 1958;78:362-7.
    • (1958) J Pharm Soc Jap , vol.78 , pp. 362-367
    • Suzuki, T.1    Iwanaga, S.2
  • 33
    • 0028057102 scopus 로고
    • Detection of alkaline phosphatase in venom by blotting methods
    • Acosta A, Rael ED, Maddux NL, Lieb CS. Detection of alkaline phosphatase in venom by blotting methods. Toxicon 1994;32:227-31.
    • (1994) Toxicon , vol.32 , pp. 227-231
    • Acosta, A.1    Rael, E.D.2    Maddux, N.L.3    Lieb, C.S.4
  • 34
    • 0019470929 scopus 로고
    • Acid and alkaline phosphomonoesterases in Egyptian snake venoms
    • Hassan F, El-Hawary MF, El-Ghazawy A. Acid and alkaline phosphomonoesterases in Egyptian snake venoms. Z Ernahrungswiss 1981;20:44-54.
    • (1981) Z Ernahrungswiss , vol.20 , pp. 44-54
    • Hassan, F.1    El-Hawary, M.F.2    El-Ghazawy, A.3
  • 35
    • 0026808338 scopus 로고
    • Citrate is an endogenous inhibitor of snake venom enzymes by metal-ion chelation
    • Francis B, Seebart C, Kaiser II. Citrate is an endogenous inhibitor of snake venom enzymes by metal-ion chelation. Toxicon 1992;30:1239-46.
    • (1992) Toxicon , vol.30 , pp. 1239-1246
    • Francis, B.1    Seebart, C.2    Kaiser, I.I.3
  • 36
    • 0023609364 scopus 로고
    • The purification of acid phosphatase from honey bee venom (Apis mellifica)
    • Barboni E, Kemeny DM, Campos S, Vernon CA. The purification of acid phosphatase from honey bee venom (Apis mellifica). Toxicon 1987;25:1097-103.
    • (1987) Toxicon , vol.25 , pp. 1097-1103
    • Barboni, E.1    Kemeny, D.M.2    Campos, S.3    Vernon, C.A.4
  • 38
    • 0018088785 scopus 로고
    • Hemorrhagic toxins from rattlesnake (Crotalus atrox) venom. Pathogenesis of hemorrhage induced by three purified toxins
    • Ownby CL, Bjarnason J, Tu AT. Hemorrhagic toxins from rattlesnake (Crotalus atrox) venom. Pathogenesis of hemorrhage induced by three purified toxins. Am J Pathol 1978;93: 201-18.
    • (1978) Am J Pathol , vol.93 , pp. 201-18
    • Ownby, C.L.1    Bjarnason, J.2    Tu, A.T.3
  • 39
    • 0022497150 scopus 로고
    • Interactions between membranes and cytolytic peptides
    • Bernheimer AW, Rudy B. Interactions between membranes and cytolytic peptides. Biochim Biophys Acta 1986;864:123-41.
    • (1986) Biochim Biophys Acta , vol.864 , pp. 123-141
    • Bernheimer, A.W.1    Rudy, B.2
  • 40
    • 0034899916 scopus 로고    scopus 로고
    • Identification of the myotoxic site of the Lys49 phospholipase A(2) from Agkistrodon piscivorus piscivorus snake venom: synthetic C-terminal peptides from Lys49, but not from Asp49 myotoxins, exert membrane-damaging activities
    • Nunez CE, Angulo Y, Lomonte B. Identification of the myotoxic site of the Lys49 phospholipase A(2) from Agkistrodon piscivorus piscivorus snake venom: synthetic C-terminal peptides from Lys49, but not from Asp49 myotoxins, exert membrane-damaging activities. Toxicon 2001;39:1587-94.
    • (2001) Toxicon , vol.39 , pp. 1587-1594
    • Nunez, C.E.1    Angulo, Y.2    Lomonte, B.3
  • 41
    • 0037103746 scopus 로고    scopus 로고
    • Cytotoxic potency of cardiotoxin from Naja sputatrix: development of a new cytolytic assay
    • Ma D, Armugam A, Jeyaseelan K. Cytotoxic potency of cardiotoxin from Naja sputatrix: development of a new cytolytic assay. Biochem J 2002;366:35-43.
    • (2002) Biochem J , vol.366 , pp. 35-43
    • Ma, D.1    Armugam, A.2    Jeyaseelan, K.3
  • 43
    • 0031045689 scopus 로고    scopus 로고
    • 2-purinoceptors by adenosine stimulates L-arginine transport (system y+) and nitric oxide synthesis in human fetal endothelial cells
    • 2-purinoceptors by adenosine stimulates L-arginine transport (system y+) and nitric oxide synthesis in human fetal endothelial cells. J Physiol 1997;499:135-40.
    • (1997) J Physiol , vol.499 , pp. 135-140
    • Sobrevia, L.1    Yudilevich, D.L.2    Mann, G.E.3
  • 44
    • 0031800306 scopus 로고    scopus 로고
    • Adenosine endogenously released during early reperfusion mitigates postischemic myocardial dysfunction by inhibiting platelet adhesion
    • Seligmann C, Kupatt C, Becker BF, Zahler S, Beblo S. Adenosine endogenously released during early reperfusion mitigates postischemic myocardial dysfunction by inhibiting platelet adhesion. J Cardiovasc Pharmacol 1998;32:156-63.
    • (1998) J Cardiovasc Pharmacol , vol.32 , pp. 156-163
    • Seligmann, C.1    Kupatt, C.2    Becker, B.F.3    Zahler, S.4    Beblo, S.5
  • 45
    • 0027337474 scopus 로고
    • 3 adenosine receptor is the unique adenosine receptor which facilitates release of allergic mediators in mast cells
    • 3 adenosine receptor is the unique adenosine receptor which facilitates release of allergic mediators in mast cells. J Biol Chem 1993;268:16887-90.
    • (1993) J Biol Chem , vol.268 , pp. 16887-16890
    • Ramkumar, V.1    Stiles, G.L.2    Beaven, M.A.3    Ali, H.4
  • 46
    • 0025326815 scopus 로고
    • Cardiovascular purinoreceptors
    • Olsson RA, Pearson JD. Cardiovascular purinoreceptors. Physiol Rev 1990;70:761-845.
    • (1990) Physiol Rev , vol.70 , pp. 761-845
    • Olsson, R.A.1    Pearson, J.D.2
  • 47
    • 33846191193 scopus 로고    scopus 로고
    • Mediators of tubuloglomerular feedback regulation of glomerular filtration: ATP and adenosine
    • Castrop H. Mediators of tubuloglomerular feedback regulation of glomerular filtration: ATP and adenosine. Acta Physiol (Oxf) 2007;189:3-14.
    • (2007) Acta Physiol (Oxf) , vol.189 , pp. 3-14
    • Castrop, H.1
  • 48
    • 0020072995 scopus 로고
    • Sedative and anticonvulsant effects of adenosine analogs in mouse and rat
    • Dunwiddie TV, Worth T. Sedative and anticonvulsant effects of adenosine analogs in mouse and rat. J Pharmacol Exp Ther 1982;220:70-6.
    • (1982) J Pharmacol Exp Ther , vol.220 , pp. 70-76
    • Dunwiddie, T.V.1    Worth, T.2
  • 49
    • 0020639488 scopus 로고
    • Central effects of adenosine analogs on locomotor activity in mice and antagonism of caffeine
    • Barraco RA, Coffin VL, Altman HJ, Phillips JW. Central effects of adenosine analogs on locomotor activity in mice and antagonism of caffeine. Brain Res 1983;272:392-5.
    • (1983) Brain Res , vol.272 , pp. 392-395
    • Barraco, R.A.1    Coffin, V.L.2    Altman, H.J.3    Phillips, J.W.4
  • 50
    • 0022491760 scopus 로고
    • Retardation of associative learning in the rabbit by an adenosine analog as measured by classical conditioning of the nictitating membrane response
    • Winsky L, Harvey JA. Retardation of associative learning in the rabbit by an adenosine analog as measured by classical conditioning of the nictitating membrane response. J Neurosci 1986;6: 2684-90.
    • (1986) J Neurosci , vol.6 , pp. 2684-90
    • Winsky, L.1    Harvey, J.A.2
  • 51
    • 0024403529 scopus 로고
    • Adenosine analogs inhibit fighting in isolated male mice
    • Palmour RM, Lipowski CJ, Simon CK, Ervin FR. Adenosine analogs inhibit fighting in isolated male mice. Life Sci 1989;44:1293-301.
    • (1989) Life Sci , vol.44 , pp. 1293-1301
    • Palmour, R.M.1    Lipowski, C.J.2    Simon, C.K.3    Ervin, F.R.4
  • 54
    • 0030610258 scopus 로고    scopus 로고
    • 3 receptor activation produces nociceptive behaviour and edema by release of histamine and 5-hydroxytryptamine
    • 3 receptor activation produces nociceptive behaviour and edema by release of histamine and 5-hydroxytryptamine. Eur J Pharmacol 1997;333:1-7.
    • (1997) Eur J Pharmacol , vol.333 , pp. 1-7
    • Sawynok, J.1    Zarrindast, M.R.2    Reid, A.R.3    Doak, G.J.4
  • 55
    • 0032540196 scopus 로고    scopus 로고
    • Adenosine receptor activation and nociception
    • Sawynok J. Adenosine receptor activation and nociception. Eur J Pharmacol 1998;347:1-11.
    • (1998) Eur J Pharmacol , vol.347 , pp. 1-11
    • Sawynok, J.1
  • 56
    • 0033965558 scopus 로고    scopus 로고
    • Adenosine and inosine increase cutaneous vasopermeability by activating A(3) receptors on mast cells
    • Tilley SL, Wagoner VA, Salvatore CA, Jacobson MA, Koller BH. Adenosine and inosine increase cutaneous vasopermeability by activating A(3) receptors on mast cells. J Clin Invest 2000;105:361-7.
    • (2000) J Clin Invest , vol.105 , pp. 361-367
    • Tilley, S.L.1    Wagoner, V.A.2    Salvatore, C.A.3    Jacobson, M.A.4    Koller, B.H.5


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