메뉴 건너뛰기




Volumn 341, Issue 2, 2006, Pages 522-531

A catalog for transcripts in the venom gland of the Agkistrodon acutus: Identification of the toxins potentially involved in coagulopathy

Author keywords

Agkistrodon acutus; Coagulopathy; Expressed sequence tags; Toxins; Transcriptome; Venom gland

Indexed keywords

BRADYKININ; CELL PROTEIN; CYTOKINE; DISINTEGRIN; LECTIN; METALLOPROTEINASE; NUCLEASE; NUCLEOTIDASE; PHOSPHOLIPASE A2; SERINE PROTEINASE; TOXIN; VENOM;

EID: 31444455234     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.01.006     Document Type: Article
Times cited : (61)

References (33)
  • 1
    • 0036896057 scopus 로고    scopus 로고
    • Snake venom as therapeutic agents: From toxin to drug development
    • S.K. Pal, A. Gomes, S.C. Dasgupta, and A. Gomes Snake venom as therapeutic agents: from toxin to drug development Indian J. Exp. Biol. 40 2002 1353 1358
    • (2002) Indian J. Exp. Biol. , vol.40 , pp. 1353-1358
    • Pal, S.K.1    Gomes, A.2    Dasgupta, S.C.3    Gomes, A.4
  • 2
    • 1842737126 scopus 로고    scopus 로고
    • Hemorrhagic activity and mechanism of FIIa, a fibrinolytic enzyme from Agkistrodon acutus venom
    • Q.Q. Wang, J.S. Chen, X.X. Liang, P.X. Qiu, Y.W. Wang, and G.M. Yan Hemorrhagic activity and mechanism of FIIa, a fibrinolytic enzyme from Agkistrodon acutus venom Acta Pharmacol. Sin. 25 2004 514 521
    • (2004) Acta Pharmacol. Sin. , vol.25 , pp. 514-521
    • Wang, Q.Q.1    Chen, J.S.2    Liang, X.X.3    Qiu, P.X.4    Wang, Y.W.5    Yan, G.M.6
  • 3
    • 0035038901 scopus 로고    scopus 로고
    • Thrombolysis effect with FIIa from Agkistrodon acutus venom in different thrombosis model
    • J.H. Chen, X.X. Liang, P.X. Qiu, and G.M. Yan Thrombolysis effect with FIIa from Agkistrodon acutus venom in different thrombosis model Acta Pharmacol. Sin. 22 2001 420 422
    • (2001) Acta Pharmacol. Sin. , vol.22 , pp. 420-422
    • Chen, J.H.1    Liang, X.X.2    Qiu, P.X.3    Yan, G.M.4
  • 4
    • 19544367266 scopus 로고    scopus 로고
    • Snake venoms and coagulopathy
    • J. White Snake venoms and coagulopathy Toxicon 45 2005 951 967
    • (2005) Toxicon , vol.45 , pp. 951-967
    • White, J.1
  • 5
    • 0346431970 scopus 로고    scopus 로고
    • Purification, partial characterization and crystallization of acucetin, a protein containing both disintegrin-like and cysteine-rich domains released by auto-proteolysis of a P-III-type metalloproteinase AaH-IV from Agkistrodon acutus venom
    • J. Zang, Z. Zhu, Y. Yu, M. Teng, L. Niu, Q. Huang, Q. Liu, and Q. Hao Purification, partial characterization and crystallization of acucetin, a protein containing both disintegrin-like and cysteine-rich domains released by auto-proteolysis of a P-III-type metalloproteinase AaH-IV from Agkistrodon acutus venom Acta Crystallogr. D Biol. Crystallogr. 59 2003 2310 2312
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 2310-2312
    • Zang, J.1    Zhu, Z.2    Yu, Y.3    Teng, M.4    Niu, L.5    Huang, Q.6    Liu, Q.7    Hao, Q.8
  • 7
    • 15444369454 scopus 로고    scopus 로고
    • Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases
    • Z. Zhu, Z. Liang, T. Zhang, Z. Zhu, W. Xu, M. Teng, and L. Niu Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases J. Biol. Chem. 280 2005 10524 10529
    • (2005) J. Biol. Chem. , vol.280 , pp. 10524-10529
    • Zhu, Z.1    Liang, Z.2    Zhang, T.3    Zhu, Z.4    Xu, W.5    Teng, M.6    Niu, L.7
  • 8
    • 1542314288 scopus 로고    scopus 로고
    • CDNA cloning, sequence analysis, and recombinant expression of akitonin beta, a C-type lectin-like protein from Agkistrodon acutus
    • X.D. Zha, J. Liu, and K.S. Xu cDNA cloning, sequence analysis, and recombinant expression of akitonin beta, a C-type lectin-like protein from Agkistrodon acutus Acta Pharmacol. Sin. 25 2004 372 377
    • (2004) Acta Pharmacol. Sin. , vol.25 , pp. 372-377
    • Zha, X.D.1    Liu, J.2    Xu, K.S.3
  • 11
    • 0034615556 scopus 로고    scopus 로고
    • Snake venom proteases affecting hemostasis and thrombosis
    • T. Matsui, Y. Fujimura, and K. Titani Snake venom proteases affecting hemostasis and thrombosis Biochim. Biophys. Acta 1477 2000 146 156
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 146-156
    • Matsui, T.1    Fujimura, Y.2    Titani, K.3
  • 12
    • 0029055393 scopus 로고
    • Snake venom metalloendopeptidases: Reprolysins
    • J.B. Bjarnason, and J.W. Fox Snake venom metalloendopeptidases: reprolysins Methods Enzymol. 248 1995 345 368
    • (1995) Methods Enzymol. , vol.248 , pp. 345-368
    • Bjarnason, J.B.1    Fox, J.W.2
  • 13
    • 0037121083 scopus 로고    scopus 로고
    • A survey of gene expression and diversity in the venom glands of the pitviper snake Bothrops insularis through the generation of expressed sequence tags (ESTs)
    • L. Junqueira-de-Azevedo Ide, and P.L. Ho A survey of gene expression and diversity in the venom glands of the pitviper snake Bothrops insularis through the generation of expressed sequence tags (ESTs) Gene 299 2002 279 291
    • (2002) Gene , vol.299 , pp. 279-291
    • Junqueira-De-Azevedo Ide, L.1    Ho, P.L.2
  • 15
    • 9744281932 scopus 로고    scopus 로고
    • Molecular diversity and accelerated evolution of C-type lectin-like proteins from snake venom
    • T. Ogawa, T. Chijiwa, N. Oda-Ueda, and M. Ohno Molecular diversity and accelerated evolution of C-type lectin-like proteins from snake venom Toxicon 45 2005 1 14
    • (2005) Toxicon , vol.45 , pp. 1-14
    • Ogawa, T.1    Chijiwa, T.2    Oda-Ueda, N.3    Ohno, M.4
  • 17
    • 3242764595 scopus 로고    scopus 로고
    • Bitis gabonica (Gaboon viper) snake venom gland: Toward a catalog for the full-length transcripts (cDNA) and proteins
    • I.M. Francischetti, V. My-Pham, J. Harrison, M.K. Garfield, and J.M. Ribeiro Bitis gabonica (Gaboon viper) snake venom gland: toward a catalog for the full-length transcripts (cDNA) and proteins Gene 337 2004 55 69
    • (2004) Gene , vol.337 , pp. 55-69
    • Francischetti, I.M.1    My-Pham, V.2    Harrison, J.3    Garfield, M.K.4    Ribeiro, J.M.5
  • 18
    • 19544374479 scopus 로고    scopus 로고
    • Structures and functions of snake venom CLPs (C-type lectin-like proteins) with anticoagulant-, procoagulant-, and platelet-modulating activities
    • T. Morita Structures and functions of snake venom CLPs (C-type lectin-like proteins) with anticoagulant-, procoagulant-, and platelet-modulating activities Toxicon 45 2005 1099 1114
    • (2005) Toxicon , vol.45 , pp. 1099-1114
    • Morita, T.1
  • 19
    • 0037352457 scopus 로고    scopus 로고
    • Purification, N-terminal sequencing, partial characterization, crystallization and preliminary crystallographic analysis of two glycosylated serine proteinases from Agkistrodon acutus venom
    • Z. Zhu, P. Gong, M. Teng, and L. Niu Purification, N-terminal sequencing, partial characterization, crystallization and preliminary crystallographic analysis of two glycosylated serine proteinases from Agkistrodon acutus venom Acta Crystallogr. D Biol. Crystallogr. 59 2003 547 550
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 547-550
    • Zhu, Z.1    Gong, P.2    Teng, M.3    Niu, L.4
  • 21
    • 0036135117 scopus 로고    scopus 로고
    • Ophidian envenomation strategies and the role of purines
    • S.D. Aird Ophidian envenomation strategies and the role of purines Toxicon 40 2002 335 393
    • (2002) Toxicon , vol.40 , pp. 335-393
    • Aird, S.D.1
  • 22
    • 0029283601 scopus 로고
    • Disintegrins: Potent inhibitors of platelet aggregation
    • P. Perutelli Disintegrins: potent inhibitors of platelet aggregation Recenti Prog. Med. 86 1995 168 174
    • (1995) Recenti Prog. Med. , vol.86 , pp. 168-174
    • Perutelli, P.1
  • 24
    • 19544381172 scopus 로고    scopus 로고
    • Hemorrhage induced by snake venom metalloproteinases: Biochemical and biophysical mechanisms involved in microvessel damage
    • J.M. Gutierrez, A. Rucavado, T. Escalante, and C. Diaz Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage Toxicon 45 2005 997 1011
    • (2005) Toxicon , vol.45 , pp. 997-1011
    • Gutierrez, J.M.1    Rucavado, A.2    Escalante, T.3    Diaz, C.4
  • 26
    • 0036754450 scopus 로고    scopus 로고
    • Muscarinic toxin-like proteins from Taiwan banded krait (Bungarus multicinctus) venom: Purification, characterization and gene organization
    • C. Chung, B.N. Wu, C.C. Yang, and L.S. Chang Muscarinic toxin-like proteins from Taiwan banded krait (Bungarus multicinctus) venom: purification, characterization and gene organization Biol. Chem. 383 2002 1397 1406
    • (2002) Biol. Chem. , vol.383 , pp. 1397-1406
    • Chung, C.1    Wu, B.N.2    Yang, C.C.3    Chang, L.S.4
  • 27
    • 19544373621 scopus 로고    scopus 로고
    • Structure-function relationships and mechanism of anticoagulant phospholipase A2 enzymes from snake venoms
    • R.M. Kini Structure-function relationships and mechanism of anticoagulant phospholipase A2 enzymes from snake venoms Toxicon 45 2005 1147 1161
    • (2005) Toxicon , vol.45 , pp. 1147-1161
    • Kini, R.M.1
  • 28
  • 29
    • 19544365720 scopus 로고    scopus 로고
    • The Bradykinin-potentiating peptides from venom gland and brain of Bothrops jararaca contain highly site specific inhibitors of the somatic angiotensin-converting enzyme
    • M.A. Hayashi, and A.C. Camargo The Bradykinin-potentiating peptides from venom gland and brain of Bothrops jararaca contain highly site specific inhibitors of the somatic angiotensin-converting enzyme Toxicon 45 2005 1163 1170
    • (2005) Toxicon , vol.45 , pp. 1163-1170
    • Hayashi, M.A.1    Camargo, A.C.2
  • 30
    • 14644422690 scopus 로고    scopus 로고
    • Using bradykinin-potentiating peptide structures to develop new antihypertensive drugs
    • J.H. Fernandez, G. Neshich, and A.C. Camargo Using bradykinin- potentiating peptide structures to develop new antihypertensive drugs Genet. Mol. Res. 3 2004 554 563
    • (2004) Genet. Mol. Res. , vol.3 , pp. 554-563
    • Fernandez, J.H.1    Neshich, G.2    Camargo, A.C.3
  • 31
    • 0028244635 scopus 로고
    • Molecular cloning and chemical synthesis of a novel antibacterial peptide derived from pig myeloid cells
    • M. Zanetti, P. Storici, A. Tossi, M. Scocchi, and R. Gennaro Molecular cloning and chemical synthesis of a novel antibacterial peptide derived from pig myeloid cells J. Biol. Chem. 269 1994 7855 7858
    • (1994) J. Biol. Chem. , vol.269 , pp. 7855-7858
    • Zanetti, M.1    Storici, P.2    Tossi, A.3    Scocchi, M.4    Gennaro, R.5
  • 32
    • 0032080135 scopus 로고    scopus 로고
    • Detection of growth factors and proto-oncogene mRNA in the growing tip of red deer (Cervus elaphus) antler using reverse-transcriptase polymerase chain reaction (RT-PCR)
    • S.M. Francis, and J.M. Suttie Detection of growth factors and proto-oncogene mRNA in the growing tip of red deer (Cervus elaphus) antler using reverse-transcriptase polymerase chain reaction (RT-PCR) J. Exp. Zool. 281 1998 36 42
    • (1998) J. Exp. Zool. , vol.281 , pp. 36-42
    • Francis, S.M.1    Suttie, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.