메뉴 건너뛰기




Volumn 16, Issue 8, 2009, Pages 852-859

Influence of quaternary conformation on the biological activities of the Asp49-phospholipases A2s from snake venoms

Author keywords

Oligomerization; Phospholipase a2; Quaternary conformation; Snake venom

Indexed keywords

PHOSPHOLIPASE A2; SNAKE VENOM;

EID: 68849086384     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986609788923301     Document Type: Article
Times cited : (15)

References (75)
  • 1
    • 33751028489 scopus 로고    scopus 로고
    • 2 superfamily and its group numbering system. Biochim. Biophys.
    • 2 superfamily and its group numbering system. Biochim. Biophys. Ada, 2006, 1761(11), 1246-1259.
    • (2006) Ada , vol.1761 , Issue.11 , pp. 1246-1259
    • Schaloske, R.H.1    Dennis, E.A.2
  • 4
    • 4344706187 scopus 로고    scopus 로고
    • The ins and outs of lysophosphatidic acid signaling.
    • Moolenar W. H. van Meeteren L. A. Giepmans B. N. The ins and outs of lysophosphatidic acid signaling. Bioessays, 2004, 26(8), 870-881.
    • (2004) Bioessays , vol.26 , Issue.8 , pp. 870-881
    • Moolenar, W.H.1    Meeteren, V.L.A.2    Giepmans, B.N.3
  • 6
    • 0025091499 scopus 로고
    • 2 from snake venom to human secreted forms.
    • 2 from snake venom to human secreted forms. J. Mol. Evol., 1990, 31(3), 228-238.
    • (1990) J. Mol. Evol. , vol.31 , Issue.3 , pp. 228-238
    • Davidson, F.F.1    Dennis, E.A.2
  • 7
    • 0028338536 scopus 로고
    • 2
    • Dennis E. A. Diversity of group types, regulation, and function of phospholipase A2. J. Biol. Chem., 1994, 269(18), 13057-13060. (Pubitemid 24206060)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.18 , pp. 13057-13060
    • Dennis, E.A.1
  • 8
    • 0034739463 scopus 로고    scopus 로고
    • The expanding superfamily of phospholipase A (2) enzymes: Classification and characterization.
    • Six D. A. Dennis E. A. The expanding superfamily of phospholipase A (2) enzymes: classification and characterization. Biochim. Biophys. Ada, 2000, 1488 (1-2), 1-19.
    • (2000) Biochim. Biophys. Ada , vol.1488 , Issue.1-2 , pp. 1-19
    • Six, D.A.1    Dennis, E.A.2
  • 9
    • 0030201175 scopus 로고    scopus 로고
    • 2 - a structural review
    • 2 - a structural review. Toxicon, 1996, 34(8), 827-828.
    • (1996) Toxicon , vol.34 , Issue.8 , pp. 827-828
    • Arni, R.K.1    Ward, R.J.2
  • 11
  • 15
    • 9744253792 scopus 로고    scopus 로고
    • Structure, function and interfacial allosterism in phospholipase A2: Insight from the anion-assisted dimer.
    • Bahnson B. J. Structure, function and interfacial allosterism in phospholipase A2: insight from the anion-assisted dimer. Arch. Biochem. Biophys., 2005, 433(1), 96-106.
    • (2005) Arch. Biochem. Biophys. , vol.433 , Issue.1 , pp. 96-106
    • Bahnson, B.J.1
  • 16
    • 0037207142 scopus 로고    scopus 로고
    • 2 at 1.5 Å resolution provides an insight into the catalytic mechanism
    • DOI 10.1021/bi020485z
    • Edwards S. H. Thompson D. Baker S. F. Wood S. P. Wilton D. C. The crystal structure of the H48Q active site mutant of human group IIA secreted phospholipase A2 at 1.5 Å resolution provides an insight into the catalytic mechanism. Biochemistry, 2002, 41(52), 15468-15476. (Pubitemid 36062452)
    • (2002) Biochemistry , vol.41 , Issue.52 , pp. 15468-15476
    • Edwards, S.H.1    Thompson, D.2    Baker, S.F.3    Wood, S.P.4    Wilton, D.C.5
  • 17
    • 0027248903 scopus 로고
    • The divalent cation is obligatory for the binding of ligands to the catalytic site of secreted phospholipase A2.
    • Yu B. Z. Berg O. G. Jain M. K. The divalent cation is obligatory for the binding of ligands to the catalytic site of secreted phospholipase A2. Biochemistry, 1993, 32(25), 6485-6492.
    • (1993) Biochemistry , vol.32 , Issue.25 , pp. 6485-6492
    • Yu, B.Z.1    Berg, O.G.2    Jain, M.K.3
  • 18
    • 0031792001 scopus 로고    scopus 로고
    • At the interface: Crystal structures of phospholipases A2.
    • Ward R. J. de Azevedo Jr. W. F. Arni R. K. At the interface: crystal structures of phospholipases A2. Toxicon, 1998, 36(11), 1623-1633.
    • (1998) Toxicon , vol.36 , Issue.11 , pp. 1623-1633
    • Ward, R.J.1    Azevedo, Jr.W.F.2    Arni, R.K.3
  • 19
    • 0017355161 scopus 로고
    • The presynaptic neuromuscular blocking action of taipoxin. A comparison with β bungarotoxin and crotoxin
    • DOI 10.1016/0041-0101(77)90108-8
    • Chang C. C. Lee J. D. Eaker D. Fohlman J. The presynaptic neuromuscular blocking action of taipoxin. A comparison with β-bungarotoxin and crotoxin. Toxicon, 1977, 15(6), 571-576. (Pubitemid 8151048)
    • (1977) Toxicon , vol.15 , Issue.6 , pp. 571-576
    • Chan, C.C.1    Lee, J.D.2    Eaker, D.3    Fohlman, J.4
  • 21
    • 0018522325 scopus 로고
    • Postsynaptic effects of crotoxin and of its isolated subunits.
    • Bon C. Changeux J. P. Jeng T. W. Fraenkel-Conrat, H. Postsynaptic effects of crotoxin and of its isolated subunits. Eur. J. Biochem., 1979, 99(3), 471-481.
    • (1979) Eur. J. Biochem. , vol.99 , Issue.3 , pp. 471-481
    • Bon, C.1    Changeux, J.P.2    Jeng, T.W.3    Fraenkel-Conrat, H.4
  • 23
    • 0019410258 scopus 로고
    • 2 fron elapid snake venoms
    • DOI 10.1016/0041-008X(81)90209-X
    • Fletcher J. E. Rapuano B. E. Condrea E. Yang C. C. Rosenberg P. Relationship between catalysis and toxicological properties of three phospholipases A2 from elapid snake venoms. Toxic. Appl. Pharmacol., 1981, 59(2), 375-388. (Pubitemid 11073746)
    • (1981) Toxicology and Applied Pharmacology , vol.59 , Issue.2 , pp. 375-388
    • Fletcher, J.E.1    Rapuano, B.E.2    Condrea, E.3
  • 24
    • 0032522765 scopus 로고    scopus 로고
    • 2 from Bothrops asper snake venom: Synthetic Lys49 myotoxin II-(115-129)- peptide identifies its bactericidal region
    • DOI 10.1046/j.1432-1327.1998.2530452.x
    • Paramo L. Lomonte B. Pizarro-Cerda, J. Bengoechea J. A.; Gorvel J. P. Moreno E. Bactericidal activity of Lys49 and Asp49 myotoxic phospholipases A2 from Bothrops asper snake venomsynthetic Lys49 myotoxin II-(115-129)-peptide identifies its bactericidal region. Eur. J. Biochem., 1998, 255(2), 452-461. (Pubitemid 28191847)
    • (1998) European Journal of Biochemistry , vol.253 , Issue.2 , pp. 452-461
    • Paramo, L.1    Lomonte, B.2    Pizarro-cerda, J.3    Bengoechea, J.-A.4    Gorvel, J.-P.5    Moreno, E.6
  • 25
    • 0027232904 scopus 로고
    • Purification and characterisation of a snake venom phospholipase A2: A potent inhibitor of platelet aggregation
    • DOI 10.1016/0049-3848(93)90089-7
    • Yuan Y. Jackson S. P. Mitchell C. A. Salem H. H. Purification and characterisation of a snake venom phospholipase A2: a potent inhibitor of platelet aggregation. Thromb. Res., 1993, 70(6), 471-481. (Pubitemid 23200814)
    • (1993) Thrombosis Research , vol.70 , Issue.6 , pp. 471-481
    • Yuan, Y.1    Jackson, S.P.2    Mitchell, C.A.3    Salem, H.H.4
  • 26
    • 0027248052 scopus 로고
    • 2 purified from porcine pancreas and snake venoms
    • DOI 10.1016/0041-0101(93)90254-G
    • Lloret S. Moreno E. Oedema formation and degranulation of mast cells by phospholipase A2 purified from porcine pancreas and snake venoms. Toxicon, 1993, 57(8), 949-956. (Pubitemid 23235048)
    • (1993) Toxicon , vol.31 , Issue.8 , pp. 949-956
    • Lloret, S.1    Moreno, J.J.2
  • 27
    • 0019412190 scopus 로고
    • 2
    • Condrea E. Yang C. C. Rosenberg P. Lack of correlation between anticoagulant activity and phospholipid hydrolysis by snake venom phospholipases A2. Thromb. Haemost, 1981, 45(1), 82-85. (Pubitemid 11155236)
    • (1981) Thrombosis and Haemostasis , vol.45 , Issue.1 , pp. 82-85
    • Condrea, E.1    Yang, C.-C.2    Rosenberg, P.3
  • 28
    • 0021042493 scopus 로고
    • 2 by modification of carboxylate groups
    • DOI 10.1016/0006-2952(83)90298-8
    • Rosenberg P. Condrea E. Rapuano B. E. Soons K. R. Yang C. C. Dissociation of pharmacological and enzymatic activities of snake venom phospholipases A2 by modification of carboxylate groups. Biochem. Pharmacol, 1983, 52(23), 3525-3530. (Pubitemid 14205359)
    • (1983) Biochemical Pharmacology , vol.32 , Issue.23 , pp. 3525-3530
    • Rosenberg, P.1    Condrea, E.2    Rapuano, B.E.3
  • 29
    • 0018897416 scopus 로고
    • 2 from Hemachatus haemachatus snake venom-II. Pharmacological properties in relationship to enzymatic activity
    • DOI 10.1016/0006-2952(80)90609-7
    • Fletcher J. E. Rapuano B. E. Condrea E. Yang C. C Ryan M.; Rosenberg P. Comparison of a relatively toxic phospholipase A2 from Naja nigricollis snake venom with that of a relatively nontoxic phospholipase A2 from Hemachatus haemachatus snake venom-II: pharmacological properties in relationship to enzymatic activity. Biochem. Pharmacol., 1980, 29(11), 1565-1574. (Pubitemid 10101911)
    • (1980) Biochemical Pharmacology , vol.29 , Issue.11 , pp. 1565-1574
    • Fletcher, J.E.1    Rapuano, B.2    Condrea, E.3
  • 30
    • 0021208133 scopus 로고
    • Release of slow reacting substance from the guineapig lung by phospholipases A2 of Vipera russelli snake venom.
    • Huang H. C. Release of slow reacting substance from the guineapig lung by phospholipases A2 of Vipera russelli snake venom. Toxicon, 1984, 22(3), 359-372.
    • (1984) Toxicon , vol.22 , Issue.3 , pp. 359-372
    • Huang, H.C.1
  • 32
    • 0025869880 scopus 로고
    • Inside a living cell.
    • Goodsell D. S. Inside a living cell. Trends Biochem. Sci., 1991, 16(6), 203-206.
    • (1991) Trends Biochem. Sci. , vol.16 , Issue.6 , pp. 203-206
    • Goodsell, D.S.1
  • 34
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions.
    • Jones S. Thornton J. M. Principles of protein-protein interactions. Proc. Natl. Acad. Sci. USA, 1996, 95(1), 13-20.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.1 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 39
    • 0033965390 scopus 로고    scopus 로고
    • 2 from Agkistrodon halys Pallas: Implications for its association, hemolytic and anticoagulant activities
    • DOI 10.1016/S0041-0101(99)00193-2, PII S0041010199001932
    • 2 from Agkistrodon halys Pallas: implications for its association, hemolytic and anticoagulant activities. Toxicon, 2000, 58(7), 901-916. (Pubitemid 30084732)
    • (2000) Toxicon , vol.38 , Issue.7 , pp. 901-916
    • Zhao, K.1    Zhou, Y.2    Lin, Z.3
  • 42
    • 0035998319 scopus 로고    scopus 로고
    • 2 from the venom of Naja Kaouthia
    • DOI 10.1016/S0041-0101(02)00085-5, PII S0041010102000855
    • 2 from the venom of Naja kaouthia. Toxicon, 2002, 40(7), 917-922. (Pubitemid 34663684)
    • (2002) Toxicon , vol.40 , Issue.7 , pp. 917-922
    • Gu, L.1    Wang, Z.2    Song, S.3    Shu, Y.4    Lin, Z.5
  • 46
    • 0029089655 scopus 로고
    • A hypothetical structural role for proline residues in the flanking segments of protein-protein interaction sties.
    • Kini R. Evans H. J. A hypothetical structural role for proline residues in the flanking segments of protein-protein interaction sties. Biochem. Biophys. Res. Commun., 1995, 212(3), 1115-1124.
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , Issue.3 , pp. 1115-1124
    • Kini, R.1    Evans, H.J.2
  • 50
    • 17444440841 scopus 로고    scopus 로고
    • Crystal structure of vipoxin at 2.0 Å: An example of regulation of a toxic function generated by molecular evolution
    • DOI 10.1016/S0014-5793(97)00853-3, PII S0014579397008533
    • Perbandt M. Wilson J. C. Eschenburg S. Mancheva I.; Aleksiev B. Genov N. Willingmann P. Weber W. Singh T. P.; Betzel Ch. Crystal structure of vipoxin at 2.0 A: an example of regulation of a toxic function generated by molecular evolution. Febs Lett., 1997, 412(3), 573-577. (Pubitemid 27337112)
    • (1997) FEBS Letters , vol.412 , Issue.3 , pp. 573-577
    • Perbandt, M.1    Wilson, J.C.2    Eschenburg, S.3    Mancheva, I.4    Aleksiev, B.5    Genov, N.6    Willingmann, P.7    Weber, W.8    Singh, T.P.9    Betzel, Ch.10
  • 52
    • 0017132404 scopus 로고
    • 2 from the venom of Bulgarian viper (Vipera ammodytes ammodytes).
    • 2 from the venom of Bulgarian viper (Vipera ammodytes ammodytes). Toxicon, 1976, 14(6), 477-485.
    • (1976) Toxicon , vol.14 , Issue.6 , pp. 477-485
    • Aleksiev, B.1    Tchorbanov, B.2
  • 55
    • 0000716861 scopus 로고
    • Neurotoxicaction of a protein complex from the venom of the Bulgarian viper (Vipera ammodytes ammodytes).
    • Blinov N. O. Tchorbanov B. P. Grishin E. V. Aleksiev B. V. Neurotoxic action of a protein complex from the venom of the Bulgarian viper (Vipera ammodytes ammodytes). Compt. Rend. Acad. Bulg. Sci., 1979, 52(1), 663-666.
    • (1979) Compt. Rend. Acad. Bulg. Sci. , vol.52 , Issue.1 , pp. 663-666
    • Blinov, N.O.1    Tchorbanov, B.P.2    Grishin, E.V.3    Aleksiev, B.V.4
  • 58
    • 0036296032 scopus 로고    scopus 로고
    • 2 and alpha-tocopherol at 1.8 A Å resolution
    • DOI 10.1016/S0022-2836(02)00473-4
    • Chandra V. Jasti J. Kaur P. Betzel Ch. Srinivasan A. Singh T. P. First structural evidence of a specific inhibition of phospholipase A2 by alpha-tocopherol (vitamin E) and its implications in inflammation: crystal structure of the complex formed between phospholipase A2 and alpha-tocopherol at 1.8 Å resolution. J. Mol Biol., 2002, 320(2), 215-222. (Pubitemid 34722213)
    • (2002) Journal of Molecular Biology , vol.320 , Issue.2 , pp. 215-222
    • Chandra, V.1    Jasti, J.2    Kaur, P.3    Betzel, Ch.4    Srinivasan, A.5    Singh, T.P.6
  • 59
    • 0036714237 scopus 로고    scopus 로고
    • 2 inhibition for the synthesis of prostaglandins by the plant alkaloid aristolochic acid from a 1.7 Å crystal structure
    • DOI 10.1021/bi0258593
    • Chandra V. Jasti J. Kaur P. Srinivasan A. Betzel Ch. Singh T. P. Structural basis of phospholipase A2 inhibition for the synthesis of prostaglandins by the plant alkaloid aristolochic acid from a 1.7 Å crystal structure. Biochemistry, 2002, 41(36), 10914-10919. (Pubitemid 35001203)
    • (2002) Biochemistry , vol.41 , Issue.36 , pp. 10914-10919
    • Chandra, V.1    Jasti, J.2    Kaur, P.3    Srinivasan, A.4    Betzel, Ch.5    Singh, T.P.6
  • 60
    • 0037174871 scopus 로고    scopus 로고
    • 2 and a potent peptide inhibitor Phe-Leu-Ser-Tyr-Lys at 1.8 Å resolution
    • DOI 10.1074/jbc.M206130200
    • Chandra V. Jasti J. Kaur P. Dey S. Perbandt M. Srinivasan A. Betzel Ch. Singh T. P. Crystal structure of a complex formed between a snake venom phospholipase A (2) and a potent peptide inhibitor Phe-Leu-Ser-Tyr-Lys at 1.8 Å resolution. J. Biol. Chem., 2002, 277(43), 41079-41085. (Pubitemid 35215698)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 41079-41085
    • Chandra, V.1    Jasti, J.2    Kaur, P.3    Dey, S.4    Perbandt, M.5    Srinivasan, A.6    Betzel, Ch.7    Singh, T.P.8
  • 63
    • 0037103457 scopus 로고    scopus 로고
    • Structural and functional characterization of an acidic platelet aggregation inhibitor and hypotensive phospholipase A (2) from Bothrops jararacussu snake venom.
    • Andrião-Escarso, S. H. Soares A. M. Fontes M. R. M. Fuly A. L.; Corrêa, F. M. A. Rosa J. C. Greene L. J. Giglio J. R. Structural and functional characterization of an acidic platelet aggregation inhibitor and hypotensive phospholipase A (2) from Bothrops jararacussu snake venom. Biochem. Pharmacol, 2002, 64(4), 723-732.
    • (2002) Biochem. Pharmacol , vol.64 , Issue.4 , pp. 723-732
    • Andrião-Escarso, S.H.1    Soares, A.M.2    Fontes, M.R.M.3    Fuly, A.L.4    Corrêa, F.M.A.5    Rosa, J.C.6    Greene, L.J.7    Giglio, J.R.8
  • 64
    • 33644837979 scopus 로고    scopus 로고
    • Structure of BthA-I complexed with p-bromophenacyl bromide: Possible correlations with lack of pharmacological activity.
    • Magro A. J. Takeda A. A. Soares A. M. Fontes M. R. M. Structure of BthA-I complexed with p-bromophenacyl bromide: possible correlations with lack of pharmacological activity. Acta Crystallogr., 2005, D61 (12), 1670-1677.
    • (2005) Acta Crystallogr. , vol.D61 , Issue.12 , pp. 1670-1677
    • Magro, A.J.1    Takeda, A.A.2    Soares, A.M.3    Fontes, M.R.M.4
  • 65
    • 0024312040 scopus 로고
    • A model to explain the pharmacological effects of snake venom phospholipases A2.
    • Kini R. M. Evans H. J. A model to explain the pharmacological effects of snake venom phospholipases A2. Toxicon, 1989, 27(6), 613-635.
    • (1989) Toxicon , vol.27 , Issue.6 , pp. 613-635
    • Kini, R.M.1    Evans, H.J.2
  • 66
    • 1042287118 scopus 로고    scopus 로고
    • Chemical modifications of phospholipases A2 from snake venoms: Effects on catalytic and pharmacological properties.
    • Soares A. M. Giglio J. R. Chemical modifications of phospholipases A2 from snake venoms: effects on catalytic and pharmacological properties. Toxicon, 2003, 42(8), 855-868.
    • (2003) Toxicon , vol.42 , Issue.8 , pp. 855-868
    • Soares, A.M.1    Giglio, J.R.2
  • 67
    • 0037319939 scopus 로고    scopus 로고
    • 2 piratoxin III from Bothrops pirajai reveals unprecedented structural displacement of the calcium-binding loop: Possible relationship to cooperative substrate binding
    • DOI 10.1107/S0907444902021467
    • Rigden D. J. Hwa L. W. Marangoni S. Toyama M.H. Polikarpov, I. The structure of the D49 phospholipase A2 piratoxin III from Bothrops pirajai reveals unprecedented structural displacement of the calcium-binding loop: possible relationship to cooperative substrate binding. Acta Crystallogr., 2003, D59 (2), 255-262. (Pubitemid 36224846)
    • (2003) Acta Crystallographica Section D: Biological Crystallography , vol.59 , Issue.2 , pp. 255-262
    • Rigden, D.J.1    Hwa, L.W.2    Marangoni, S.3    Toyama, M.H.4    Polikarpov, I.5
  • 68
    • 12944283257 scopus 로고    scopus 로고
    • Structure of agkistrodotoxin in an orthorhombic crystal form with six molecules per asymmetric unit
    • DOI 10.1107/S0907444999012603
    • Tang L. Zhou Y. C. Lin Z. J. Structure of agkistrodotoxin in an orthorhombic crystal form with six molecules per asymmetric unit. Acta Crystallogr., 1999, D55 (12), 1986-1996. (Pubitemid 30023193)
    • (1999) Acta Crystallographica Section D: Biological Crystallography , vol.55 , Issue.12 , pp. 1986-1996
    • Tang, L.1    Zhou, Y.-C.2    Lin, Z.-J.3
  • 70
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • DOI 10.1016/0022-2836(88)90606-7
    • Janin J. Miller S. Chothia C. Surface, subunit interfaces and interior of oligomeric proteins. J. Mol Biol., 1988, 204 (1), 155-164. (Pubitemid 19011740)
    • (1988) Journal of Molecular Biology , vol.204 , Issue.1 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 71
    • 0024846203 scopus 로고
    • The structure of interfaces between subunits of dimeric and tetrameric proteins
    • Miller S. The structure of interfaces between subunits of dimeric and tetrameric proteins. Protein Eng., 1989, 3(2), 77-83. (Pubitemid 20055082)
    • (1989) Protein Engineering , vol.3 , Issue.2 , pp. 77-83
    • Miller, S.1
  • 72
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel E. Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol., 2007, 372(3), 774-797. (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 73
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterization and functional significance of transient protein-protein interactions.
    • Nooren I. M. A. Thornton J. M. Structural characterization and functional significance of transient protein-protein interactions. J. Mol. Biol., 2003, 325(5), 991-1018.
    • (2003) J. Mol. Biol. , vol.325 , Issue.5 , pp. 991-1018
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 74
    • 0037841804 scopus 로고    scopus 로고
    • Evolution of the protein repertoire
    • DOI 10.1126/science.1085371
    • Chothia C. Gough J. Vogel C. Teichmann S. A. Evolution of the protein repertoire. Science, 2003, 300(5626), 1701-1703. (Pubitemid 36712556)
    • (2003) Science , vol.300 , Issue.5626 , pp. 1701-1703
    • Chothia, C.1    Gough, J.2    Vogel, C.3    Teichmann, S.A.4
  • 75
    • 0242354129 scopus 로고    scopus 로고
    • The origin of new genes: Glimpses from the young and old
    • DOI 10.1038/nrg1204
    • Long M. Betrán, E. Thornton K. Wang W. The origin of new genes: glimpses from the young and old. Nat. Rev. Genet., 2003, 4(11), 865-875. (Pubitemid 37345613)
    • (2003) Nature Reviews Genetics , vol.4 , Issue.11 , pp. 865-875
    • Long, M.1    Betran, E.2    Thornton, K.3    Wang, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.