메뉴 건너뛰기




Volumn 51, Issue 3, 2008, Pages 345-352

Neutralization of hemorrhagic snake venom metalloproteinase HR1a from Protobothrops flavoviridis by human monoclonal antibody

Author keywords

Hemorrhagic metalloproteinase; Human monoclonal antibody; KM MouseTM; Snake venom

Indexed keywords

HUMAN MONOCLONAL ANTIBODY; METALLOPROTEINASE; SNAKE VENOM;

EID: 39049091450     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2007.10.009     Document Type: Article
Times cited : (19)

References (19)
  • 1
    • 0028146808 scopus 로고
    • Hemorrhagic metalloproteinases from snake venoms
    • Bjarnason J.B., and Fox J.W. Hemorrhagic metalloproteinases from snake venoms. Pharmacol. Ther. 62 (1994) 325-372
    • (1994) Pharmacol. Ther. , vol.62 , pp. 325-372
    • Bjarnason, J.B.1    Fox, J.W.2
  • 2
    • 0028221522 scopus 로고
    • Modulation of enzyme activity by antibody binding to an alkaline phosphatase- epitope hybrid protein
    • Brennan C., Christianson K., Surowy T., and Mandecki W. Modulation of enzyme activity by antibody binding to an alkaline phosphatase- epitope hybrid protein. Protein Eng. 7 (1994) 509-514
    • (1994) Protein Eng. , vol.7 , pp. 509-514
    • Brennan, C.1    Christianson, K.2    Surowy, T.3    Mandecki, W.4
  • 3
    • 0022341031 scopus 로고
    • An inhibitory monoclonal antibody to rabbit brain acetylcholinesterase. Studies on interaction with the enzyme
    • Brimijoin S., Mintz KP., and Prendergast FG. An inhibitory monoclonal antibody to rabbit brain acetylcholinesterase. Studies on interaction with the enzyme. Mol. Pharmacol. 28 (1985) 539-545
    • (1985) Mol. Pharmacol. , vol.28 , pp. 539-545
    • Brimijoin, S.1    Mintz, KP.2    Prendergast, FG.3
  • 4
    • 0037189557 scopus 로고    scopus 로고
    • ADAM13 disintegrin and cysteine-rich domains bind to the second heparin-binding domain of fibronectin
    • Gaultier A., Cousin H., Darribere T., and Alfandari D. ADAM13 disintegrin and cysteine-rich domains bind to the second heparin-binding domain of fibronectin. J. Biol. Chem. 277 (2002) 23336-23344
    • (2002) J. Biol. Chem. , vol.277 , pp. 23336-23344
    • Gaultier, A.1    Cousin, H.2    Darribere, T.3    Alfandari, D.4
  • 5
    • 0028922451 scopus 로고
    • The primary structure of a hemorrhagic factor, HR2b, from the venom of Okinawa habu (Trimeresurus flavoviridis)
    • Iha M., Qi ZQ., Kannki T., Tomihara Y., and Yonaha K. The primary structure of a hemorrhagic factor, HR2b, from the venom of Okinawa habu (Trimeresurus flavoviridis). Toxicon 33 (1995) 229-239
    • (1995) Toxicon , vol.33 , pp. 229-239
    • Iha, M.1    Qi, ZQ.2    Kannki, T.3    Tomihara, Y.4    Yonaha, K.5
  • 8
    • 0034838815 scopus 로고    scopus 로고
    • Purification, cDNA cloning and characterization of the vascular apoptosis-inducing protein, HV1, from Trimeresurus flavoviridis
    • Masuda S., Hayashi H., Atoda H., Morita T., and Araki S. Purification, cDNA cloning and characterization of the vascular apoptosis-inducing protein, HV1, from Trimeresurus flavoviridis. Eur. J. Biochem. 268 (2001) 3339-3345
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3339-3345
    • Masuda, S.1    Hayashi, H.2    Atoda, H.3    Morita, T.4    Araki, S.5
  • 9
    • 0024344059 scopus 로고
    • Primary structure of hemorrhagic protein, HR2a, isolated from the venom of Trimeresurus flavoviridis
    • Miyata T., Takeya H., Ozeki Y., Arakawa M., Tokunaga F., Iwanaga S., and Omori-Satoh T. Primary structure of hemorrhagic protein, HR2a, isolated from the venom of Trimeresurus flavoviridis. J. Biochem. 105 (1989) 847-853
    • (1989) J. Biochem. , vol.105 , pp. 847-853
    • Miyata, T.1    Takeya, H.2    Ozeki, Y.3    Arakawa, M.4    Tokunaga, F.5    Iwanaga, S.6    Omori-Satoh, T.7
  • 10
    • 0000763346 scopus 로고
    • Hemorrhagic, necrotizing and edema-forming effects of snake venoms
    • Lee C.-Y. (Ed), Springer, Berlin, New York
    • Ohsaka A. Hemorrhagic, necrotizing and edema-forming effects of snake venoms. In: Lee C.-Y. (Ed). Handbook of Experimental Pharmacology vol. 52 (1979), Springer, Berlin, New York 480-546
    • (1979) Handbook of Experimental Pharmacology , vol.52 , pp. 480-546
    • Ohsaka, A.1
  • 11
    • 0141705378 scopus 로고    scopus 로고
    • Monoclonal antibodies inducing conformational changes on the antigen molecule
    • Roguin L.P., and Retegui L.A. Monoclonal antibodies inducing conformational changes on the antigen molecule. Scand. J. Immunol. 58 (2003) 387-394
    • (2003) Scand. J. Immunol. , vol.58 , pp. 387-394
    • Roguin, L.P.1    Retegui, L.A.2
  • 12
    • 0018957965 scopus 로고
    • Lack of a hemorrhagic principle in Habu snake venom, Trimeresurus flavoviridis, from the Okinawa Islands
    • Sadahiro S., and Omori-Satoh T. Lack of a hemorrhagic principle in Habu snake venom, Trimeresurus flavoviridis, from the Okinawa Islands. Toxicon 18 (1980) 366-368
    • (1980) Toxicon , vol.18 , pp. 366-368
    • Sadahiro, S.1    Omori-Satoh, T.2
  • 13
    • 0032488637 scopus 로고    scopus 로고
    • Allosteric control of acetylcholinesterase activity by monoclonal antibodies
    • Saxena A., Hur R., and Doctor BP. Allosteric control of acetylcholinesterase activity by monoclonal antibodies. Biochemistry 37 (1998) 145-154
    • (1998) Biochemistry , vol.37 , pp. 145-154
    • Saxena, A.1    Hur, R.2    Doctor, BP.3
  • 14
    • 33745731954 scopus 로고    scopus 로고
    • Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold
    • Takeda S., Igarashi T., Mori H., and Araki S. Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C-shaped scaffold. EMBO J. 25 (2006) 2388-2396
    • (2006) EMBO J. , vol.25 , pp. 2388-2396
    • Takeda, S.1    Igarashi, T.2    Mori, H.3    Araki, S.4
  • 17
    • 0032981072 scopus 로고    scopus 로고
    • Nucleotide sequence of a cDNA encoding a common precursor of disintegrin flavostatin and hemorrhagic factor HR2a from the venom of Trimeresurus flavoviridis
    • Yamada D., Shin Y., and Morita T. Nucleotide sequence of a cDNA encoding a common precursor of disintegrin flavostatin and hemorrhagic factor HR2a from the venom of Trimeresurus flavoviridis. FEBS Lett. 451 (1999) 299-302
    • (1999) FEBS Lett. , vol.451 , pp. 299-302
    • Yamada, D.1    Shin, Y.2    Morita, T.3
  • 18
    • 0025753422 scopus 로고
    • Characterization of three hemorrhagic factors from the venom of Okinawa habu (Trimeresurus flavoviridis)
    • Yonaha K., Iha M., Tomihara Y., Nozaki M., and Yamakawa M. Characterization of three hemorrhagic factors from the venom of Okinawa habu (Trimeresurus flavoviridis). Toxicon 29 (1991) 703-711
    • (1991) Toxicon , vol.29 , pp. 703-711
    • Yonaha, K.1    Iha, M.2    Tomihara, Y.3    Nozaki, M.4    Yamakawa, M.5
  • 19
    • 0029105096 scopus 로고
    • Molecular cloning and expression of catrocollastatin, a snake-venom protein from Crotalus atrox (western diamondback rattlesnake) which inhibits platelet adhesion to collagen
    • Zhou Q., Smith JB., and Grossman MH. Molecular cloning and expression of catrocollastatin, a snake-venom protein from Crotalus atrox (western diamondback rattlesnake) which inhibits platelet adhesion to collagen. Biochem. J. 307 (1995) 411-417
    • (1995) Biochem. J. , vol.307 , pp. 411-417
    • Zhou, Q.1    Smith, JB.2    Grossman, MH.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.