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Volumn 430, Issue 1, 2013, Pages 144-149

Anti-elastolytic activity of a honeybee (Apis cerana) chymotrypsin inhibitor

Author keywords

Anti elastolytic factor; Apis cerana; Bee; Chymotrypsin inhibitor; Elastase inhibitor

Indexed keywords

CHYMOTRYPSIN INHIBITOR;

EID: 84872383355     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.11.056     Document Type: Article
Times cited : (32)

References (30)
  • 1
    • 33745895610 scopus 로고    scopus 로고
    • A century of advances in bumblebee domestication and the economic and environmental aspects of its commercialization for pollination
    • Velthuis H.H.W., van Doorn A. A century of advances in bumblebee domestication and the economic and environmental aspects of its commercialization for pollination. Apidologie 2006, 37:421-451.
    • (2006) Apidologie , vol.37 , pp. 421-451
    • Velthuis, H.H.W.1    van Doorn, A.2
  • 2
    • 77954655921 scopus 로고    scopus 로고
    • Bugs as drugs, part 1: insects. The " new" alternative medicine for the 21st century?
    • Cherniack E.P. Bugs as drugs, part 1: insects. The " new" alternative medicine for the 21st century?. Alternat. Med. Rev. 2010, 15:124-135.
    • (2010) Alternat. Med. Rev. , vol.15 , pp. 124-135
    • Cherniack, E.P.1
  • 3
    • 2142680844 scopus 로고
    • Honeybee venom: a rich source of pharmacologically active peptides
    • Hider R.C. Honeybee venom: a rich source of pharmacologically active peptides. Endeavour 1988, 12:60-65.
    • (1988) Endeavour , vol.12 , pp. 60-65
    • Hider, R.C.1
  • 4
    • 34447312502 scopus 로고    scopus 로고
    • Therapeutic application of anti-arthritis, pain-releasing, and anti-cancer effects of bee venom and its constituent compounds
    • Son D.J., Lee J.W., Lee Y.H., Song H.S., Lee C.K., Hong J.T. Therapeutic application of anti-arthritis, pain-releasing, and anti-cancer effects of bee venom and its constituent compounds. Pharmacol. Ther. 2007, 115:246-270.
    • (2007) Pharmacol. Ther. , vol.115 , pp. 246-270
    • Son, D.J.1    Lee, J.W.2    Lee, Y.H.3    Song, H.S.4    Lee, C.K.5    Hong, J.T.6
  • 7
    • 84863138374 scopus 로고    scopus 로고
    • Antifibrinolytic role of a bee venom serine protease inhibitor that acts as a plasmin inhibitor
    • Choo Y.M., Lee K.S., Yoon H.J., Qiu Y., Wan H., Sohn M.R., Sohn H.D., Jin B.R. Antifibrinolytic role of a bee venom serine protease inhibitor that acts as a plasmin inhibitor. PLoS One 2012, 7:e32269.
    • (2012) PLoS One , vol.7
    • Choo, Y.M.1    Lee, K.S.2    Yoon, H.J.3    Qiu, Y.4    Wan, H.5    Sohn, M.R.6    Sohn, H.D.7    Jin, B.R.8
  • 8
    • 0021453880 scopus 로고
    • The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: the primary structure
    • Babin D.R., Peanasky R.J., Goss S.M. The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: the primary structure. Arch. Biochem. Biophys. 1984, 232:143-161.
    • (1984) Arch. Biochem. Biophys. , vol.232 , pp. 143-161
    • Babin, D.R.1    Peanasky, R.J.2    Goss, S.M.3
  • 9
    • 0028773905 scopus 로고
    • The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase
    • Huang K., Strynadka N.C.J., Bernard V.D., Peanasky R.J., James M.N.G. The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase. Structure 1994, 2:679-689.
    • (1994) Structure , vol.2 , pp. 679-689
    • Huang, K.1    Strynadka, N.C.J.2    Bernard, V.D.3    Peanasky, R.J.4    James, M.N.G.5
  • 10
    • 0005945807 scopus 로고    scopus 로고
    • Primary structure and properties of the cathepsin G/chymotrypsin inhibitor from the larval hemolymph of Apis mellifera
    • Bania J., Stachowiak D., Polanowski A. Primary structure and properties of the cathepsin G/chymotrypsin inhibitor from the larval hemolymph of Apis mellifera. Eur. J. Biochem. 1999, 262:680-687.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 680-687
    • Bania, J.1    Stachowiak, D.2    Polanowski, A.3
  • 11
    • 0034129479 scopus 로고    scopus 로고
    • NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors
    • Cierpicki T., Bania J., Otlewski J. NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors. Protein Sci. 2000, 9:976-984.
    • (2000) Protein Sci. , vol.9 , pp. 976-984
    • Cierpicki, T.1    Bania, J.2    Otlewski, J.3
  • 12
    • 0034088301 scopus 로고    scopus 로고
    • Trichuris suis: a secretory chymotrypsin/elastase inhibitor with potential as an immunomodulator
    • Rhoads M.L., Fetterer R.H., Hill D.E., Urban J.F. Trichuris suis: a secretory chymotrypsin/elastase inhibitor with potential as an immunomodulator. Exp. Parasitol. 2000, 95:36-44.
    • (2000) Exp. Parasitol. , vol.95 , pp. 36-44
    • Rhoads, M.L.1    Fetterer, R.H.2    Hill, D.E.3    Urban, J.F.4
  • 13
    • 0027972373 scopus 로고
    • Isolation and characterization of hirustasin, an antistasin-type serine-proteinase inhibitor from the medical leech Hirudo medicinalis
    • Söllner C., Mentele R., Eckerskorn C., Fritz H., Sommerhoff C.P. Isolation and characterization of hirustasin, an antistasin-type serine-proteinase inhibitor from the medical leech Hirudo medicinalis. Eur. J. Biochem. 1994, 219:937-943.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 937-943
    • Söllner, C.1    Mentele, R.2    Eckerskorn, C.3    Fritz, H.4    Sommerhoff, C.P.5
  • 14
    • 0034805614 scopus 로고    scopus 로고
    • Purification and characterization of a chymotrypsin inhibitor from the venom of Ophiophagus hannah (king cobra)
    • Chang L.S., Chung C., Huang H.B., Lin S.R. Purification and characterization of a chymotrypsin inhibitor from the venom of Ophiophagus hannah (king cobra). Biochem. Biophys. Res. Commun. 2001, 283:862-867.
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 862-867
    • Chang, L.S.1    Chung, C.2    Huang, H.B.3    Lin, S.R.4
  • 15
    • 1342279424 scopus 로고    scopus 로고
    • Purification, characterization and primary structure of a chymotrypsin inhibitor from Naja atra venom
    • Zhou X.D., Jin Y., Lu Q.M., Li D.S., Zhu S.W., Wang W.Y., Xiong Y.L. Purification, characterization and primary structure of a chymotrypsin inhibitor from Naja atra venom. Comp. Biochem. Physiol. B 2004, 237:219-220.
    • (2004) Comp. Biochem. Physiol. B , vol.237 , pp. 219-220
    • Zhou, X.D.1    Jin, Y.2    Lu, Q.M.3    Li, D.S.4    Zhu, S.W.5    Wang, W.Y.6    Xiong, Y.L.7
  • 16
    • 52049091018 scopus 로고    scopus 로고
    • Isolation, expression and characterization of a novel dual serine protease inhibitor, OH-TCI, from king cobra venom
    • He Y.Y., Liu S.B., Lee W.H., Qian J.Q., Zhang Y. Isolation, expression and characterization of a novel dual serine protease inhibitor, OH-TCI, from king cobra venom. Peptides 2008, 29:1692-1699.
    • (2008) Peptides , vol.29 , pp. 1692-1699
    • He, Y.Y.1    Liu, S.B.2    Lee, W.H.3    Qian, J.Q.4    Zhang, Y.5
  • 17
    • 39649105868 scopus 로고    scopus 로고
    • A novel serine protease inhibitor from Bungarus fasciatus venom
    • Lu J., Yang H., Yu H., Gao W., Lai R., Liu J., Liang X. A novel serine protease inhibitor from Bungarus fasciatus venom. Peptides 2008, 29:369-374.
    • (2008) Peptides , vol.29 , pp. 369-374
    • Lu, J.1    Yang, H.2    Yu, H.3    Gao, W.4    Lai, R.5    Liu, J.6    Liang, X.7
  • 19
    • 84857551964 scopus 로고    scopus 로고
    • Simukunin from the salivary glands of the black fly Simulium vittatum inhibits enzymes that regulate clotting and inflammatory responses
    • Tsujimoto H., Kotsyfakis M., Francischetti L.M.B., Eum J.H., Strand M.R., Champagne D.E. Simukunin from the salivary glands of the black fly Simulium vittatum inhibits enzymes that regulate clotting and inflammatory responses. PLoS One 2012, 7:e29964.
    • (2012) PLoS One , vol.7
    • Tsujimoto, H.1    Kotsyfakis, M.2    Francischetti, L.M.B.3    Eum, J.H.4    Strand, M.R.5    Champagne, D.E.6
  • 25
    • 84872396373 scopus 로고    scopus 로고
    • The honeybee genome sequencing consortium, Insights into social insects from the genome of the honeybee Apis mellifera, Nature 443
    • The honeybee genome sequencing consortium, Insights into social insects from the genome of the honeybee Apis mellifera, Nature 443 (2006) 931-949.
    • (2006) , pp. 931-949
  • 26
    • 84857059735 scopus 로고    scopus 로고
    • Role of the endogenous elastase inhibitor, elafin, in cardiovascular injury from epithelium to endothelium
    • Alam S.R., Newby D.E., Henriksen P.A. Role of the endogenous elastase inhibitor, elafin, in cardiovascular injury from epithelium to endothelium. Biochem. Pharmacol. 2012, 83:695-704.
    • (2012) Biochem. Pharmacol. , vol.83 , pp. 695-704
    • Alam, S.R.1    Newby, D.E.2    Henriksen, P.A.3
  • 27
    • 0035038211 scopus 로고    scopus 로고
    • A defective viral genome maintained in Escherichia coli for the generation of baculovirus expression vectors
    • Je Y.H., Chang J.H., Choi J.Y., Roh J.Y., Jin B.R., O'Reilly D.R., Kang S.K. A defective viral genome maintained in Escherichia coli for the generation of baculovirus expression vectors. Biotechnol. Lett. 2001, 23:575-582.
    • (2001) Biotechnol. Lett. , vol.23 , pp. 575-582
    • Je, Y.H.1    Chang, J.H.2    Choi, J.Y.3    Roh, J.Y.4    Jin, B.R.5    O'Reilly, D.R.6    Kang, S.K.7
  • 29
    • 84872414897 scopus 로고    scopus 로고
    • Molecular cloning and characterization of chymotrypsin inhibitor and chitin-binding protein homologs from the bumblebee Bombus terrestris
    • Qiu Y., Yoon H.J., Jin B.R. Molecular cloning and characterization of chymotrypsin inhibitor and chitin-binding protein homologs from the bumblebee Bombus terrestris. Int. J. Indust. Entomol. 2012, 25:115-121.
    • (2012) Int. J. Indust. Entomol. , vol.25 , pp. 115-121
    • Qiu, Y.1    Yoon, H.J.2    Jin, B.R.3
  • 30
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M., Kato I. Protein inhibitors of proteinases. Annu. Rev. Biochem. 1980, 49:593-626.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.