메뉴 건너뛰기




Volumn 20, Issue 2, 2003, Pages 111-114

Screening of serine proteinase inhibitors from marine organisms

Author keywords

Inhibitors; Invertebrates; Marine organisms; Serine proteinases; Tunicate

Indexed keywords


EID: 23544446413     PISSN: 08644551     EISSN: 10272852     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (38)
  • 1
    • 0021273620 scopus 로고
    • Evolution of proteolytic enzymes
    • Neurat H. Evolution of proteolytic enzymes. Science 1984;224:350-7.
    • (1984) Science , vol.224 , pp. 350-357
    • Neurat, H.1
  • 3
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • Perona JJ, Craik CS. Structural basis of substrate specificity in the serine proteases. Protein Sci 1995;4:337-60.
    • (1995) Protein Sci , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 4
    • 0034615564 scopus 로고    scopus 로고
    • Structural basis of the endoproteinase'protein inhibitor interaction
    • Bode W, Huber R. Structural basis of the endoproteinase'protein inhibitor interaction. Biochim Biophys Acta 2000;1477: 241-52.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 241-252
    • Bode, W.1    Huber, R.2
  • 5
    • 0342445397 scopus 로고    scopus 로고
    • What can the structures of enzyme-inhibitors tell us about the structures of enzyme substrate complexes?
    • Laskowski M Jr, Qasim MA. What can the structures of enzyme-inhibitors tell us about the structures of enzyme substrate complexes? Biochim Biophys Acta 2000; 1477:324-37.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 324-337
    • Laskowski Jr, M.1    Qasim, M.A.2
  • 6
    • 0033918229 scopus 로고    scopus 로고
    • Alpha-1-antitrypsin deficiency, the serpinopathies and conformational disease
    • Parma JS, Lomas DA. Alpha-1-antitrypsin deficiency, the serpinopathies and conformational disease. J Royal Coll Phys London 2000;34(3):295-300.
    • (2000) J Royal Coll Phys London , vol.34 , Issue.3 , pp. 295-300
    • Parma, J.S.1    Lomas, D.A.2
  • 7
    • 0036795040 scopus 로고    scopus 로고
    • Emerging therapies in severe sepsis
    • Finney SJ, Evans TW. Emerging therapies in severe sepsis. Thorax 2002;57(2): 118-1114.
    • (2002) Thorax , vol.57 , Issue.2 , pp. 118-1114
    • Finney, S.J.1    Evans, T.W.2
  • 8
    • 11244313537 scopus 로고    scopus 로고
    • Leucaena leucocephala serine proteinase inhibitor: Primary structure and action on blood coagulation, kinin release and rat paw edema
    • Oliva MLV, Souza-Pinto JC, Batista IFC, Araújo MS, Silveira VF, Auerswald EA, et al. Leucaena leucocephala serine proteinase inhibitor: primary structure and action on blood coagulation, kinin release and rat paw edema. Biochim Biophys Acta 2000; 1477:64-74.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 64-74
    • Oliva, M.L.V.1    Souza-Pinto, J.C.2    Batista, I.F.C.3    Araújo, M.S.4    Silveira, V.F.5    Auerswald, E.A.6
  • 10
    • 0035115958 scopus 로고    scopus 로고
    • Novel roles of kallistatin, a specific tissue kallikrein inhibitor, in vascular remodeling
    • Chao J, Miao RQ, Chen V, Chen LM, Chao L. Novel roles of kallistatin, a specific tissue kallikrein inhibitor, in vascular remodeling. Biol Chem 2001;382(1):15-21.
    • (2001) Biol Chem , vol.382 , Issue.1 , pp. 15-21
    • Chao, J.1    Miao, R.Q.2    Chen, V.3    Chen, L.M.4    Chao, L.5
  • 11
    • 0035118319 scopus 로고    scopus 로고
    • Aprotinin and the systemic inflammatory response after cardiopulmonary bypass
    • Mojcik CF, Levy JH. Aprotinin and the systemic inflammatory response after cardiopulmonary bypass. Ann Throrax Surg 2001;71(2):745-54.
    • (2001) Ann Throrax Surg , vol.71 , Issue.2 , pp. 745-754
    • Mojcik, C.F.1    Levy, J.H.2
  • 13
    • 0032054020 scopus 로고    scopus 로고
    • Moser M, Auerswald E, Mentele R, Eckerson C, Fritz H, Fink E. Bdellastasin, a serine proteinase inhibitor of the antistasin family from the medical leech (Hirudo medicinalis)-primary structure, expression in yeast, and characterization of native and recombinant inhibitor. Eur J Biochem 1998;253(1):212-20.
    • Moser M, Auerswald E, Mentele R, Eckerson C, Fritz H, Fink E. Bdellastasin, a serine proteinase inhibitor of the antistasin family from the medical leech (Hirudo medicinalis)-primary structure, expression in yeast, and characterization of native and recombinant inhibitor. Eur J Biochem 1998;253(1):212-20.
  • 14
    • 0015263278 scopus 로고
    • Polyvalent isoinhibitoren für trypsin, chymotrypsin, plasmin und kallikreine aus seeanemonen (Anemonia sulcata). Isolierung, hemmverhalten und aminosäurezusammensetzung
    • Fritz H, Brey B, Béress L. Polyvalent isoinhibitoren für trypsin, chymotrypsin, plasmin und kallikreine aus seeanemonen (Anemonia sulcata). Isolierung, hemmverhalten und aminosäurezusammensetzung. Hoppe-Seyler's Z Phys Chem 1972; 353:19-30.
    • (1972) Hoppe-Seyler's Z Phys Chem , vol.353 , pp. 19-30
    • Fritz, H.1    Brey, B.2    Béress, L.3
  • 16
    • 0023433076 scopus 로고
    • The covalent structure of the elastase inhibitor from Anemonia sulcata - a "nonclassical" Kazal-type protein
    • Tschesche H, Kolkenbrock H, Bode W. The covalent structure of the elastase inhibitor from Anemonia sulcata - a "nonclassical" Kazal-type protein. Biol Chem Hoppe-Seyler 1987;368:1297-304.
    • (1987) Biol Chem Hoppe-Seyler , vol.368 , pp. 1297-1304
    • Tschesche, H.1    Kolkenbrock, H.2    Bode, W.3
  • 17
    • 0000858538 scopus 로고
    • The broad-specificity proteinase inhibitor 5 II from the sea anemone Anemonia sulcata
    • Wunderer G, Machleidt W; Fritz H. The broad-specificity proteinase inhibitor 5 II from the sea anemone Anemonia sulcata. Methods in Enzymology 1981;80:816-20.
    • (1981) Methods in Enzymology , vol.80 , pp. 816-820
    • Wunderer, G.1    Machleidt, W.2    Fritz, H.3
  • 19
    • 85044705249 scopus 로고    scopus 로고
    • Low molecular cytolysins and trypsin inhibitors from sea anemone Radianthus macrodactylus. Isolation and partial characterization
    • Zykova TA, Monastyirnaia MM, Apalikov OV, Shvets TV, Kzlovskaia EP. Low molecular cytolysins and trypsin inhibitors from sea anemone Radianthus macrodactylus. Isolation and partial characterization. Bioorg Khim 1998;24(7):509-516.
    • (1998) Bioorg Khim , vol.24 , Issue.7 , pp. 509-516
    • Zykova, T.A.1    Monastyirnaia, M.M.2    Apalikov, O.V.3    Shvets, T.V.4    Kzlovskaia, E.P.5
  • 20
    • 0020526625 scopus 로고
    • Hemolysins and proteinase inhibitors from sea anemones of the Gulf of Aqaq
    • Mebs D, Liebrich M, Reul A, Samejima Y. Hemolysins and proteinase inhibitors from sea anemones of the Gulf of Aqaq. Toxicon 1983;21:257-64.
    • (1983) Toxicon , vol.21 , pp. 257-264
    • Mebs, D.1    Liebrich, M.2    Reul, A.3    Samejima, Y.4
  • 21
    • 0018825666 scopus 로고
    • Isolation of proteinase inhibitor, toxic and hemolytic polypeptides from a sea anemone, Stoichactis sp
    • Mebs D, Gebauer E. Isolation of proteinase inhibitor, toxic and hemolytic polypeptides from a sea anemone, Stoichactis sp. Toxicon 1980;18:97-106.
    • (1980) Toxicon , vol.18 , pp. 97-106
    • Mebs, D.1    Gebauer, E.2
  • 22
    • 0027467611 scopus 로고
    • The NMR solution structure of a Kunitz-type proteinase inhibitor from the sea anemone Stichodactyla helianthus
    • Antuch W, Berndt KD, Chávez MA, Delfín J, Wuethrich K. The NMR solution structure of a Kunitz-type proteinase inhibitor from the sea anemone Stichodactyla helianthus. Eur J Biochem 1993;212:675-84.
    • (1993) Eur J Biochem , vol.212 , pp. 675-684
    • Antuch, W.1    Berndt, K.D.2    Chávez, M.A.3    Delfín, J.4    Wuethrich, K.5
  • 23
    • 16744365596 scopus 로고    scopus 로고
    • Purification, characterization and immobilization of proteinase inhibitors from Stichodactyla helianthus
    • Delfín J, Martínez I, Antuch W, Morera V, González Y, Rodríguez R, et al. Purification, characterization and immobilization of proteinase inhibitors from Stichodactyla helianthus. Toxicon 1996;34:1367-76.
    • (1996) Toxicon , vol.34 , pp. 1367-1376
    • Delfín, J.1    Martínez, I.2    Antuch, W.3    Morera, V.4    González, Y.5    Rodríguez, R.6
  • 24
    • 0031440963 scopus 로고    scopus 로고
    • Isolation and amino acid sequences of two Kunitz-type protease inhibitors from sea anemone Anthopleura aff. xanthogrammica
    • Minagua S, Ishida M, Shimakura K, Nagashima Y, Shiomi K. Isolation and amino acid sequences of two Kunitz-type protease inhibitors from sea anemone Anthopleura aff. xanthogrammica. Comp Biochem Phys 1997;118B(2):381-6.
    • (1997) Comp Biochem Phys , vol.118 B , Issue.2 , pp. 381-386
    • Minagua, S.1    Ishida, M.2    Shimakura, K.3    Nagashima, Y.4    Shiomi, K.5
  • 25
    • 34147096629 scopus 로고    scopus 로고
    • Purification and partial characterization of a proteinase inhibitor from sea anemone Condylactis gigantea
    • Chávez MA, Gil Sh, Fernández A, Huerta V, Pascual I, Abreu L, et al. Purification and partial characterization of a proteinase inhibitor from sea anemone Condylactis gigantea. Toxicon 1998;36:1275.
    • (1998) Toxicon , vol.36 , pp. 1275
    • Chávez, M.A.1    Gil, S.2    Fernández, A.3    Huerta, V.4    Pascual, I.5    Abreu, L.6
  • 26
    • 0017122851 scopus 로고
    • Further characterization of trypsin inhibitors in the polychaete Sabellastarte indica Savingny
    • Gauwerky C, Corman G, Uhlenbruek J. Further characterization of trypsin inhibitors in the polychaete Sabellastarte indica Savingny. J Clin Biochem 1976;14:245-51.
    • (1976) J Clin Biochem , vol.14 , pp. 245-251
    • Gauwerky, C.1    Corman, G.2    Uhlenbruek, J.3
  • 27
    • 0035085233 scopus 로고    scopus 로고
    • Structure, localization and potential role of a novel molluscan trypsin inhibitor in Lymnaea
    • Nagle GT, Jong-Brink M, Painter SD, Li KW. Structure, localization and potential role of a novel molluscan trypsin inhibitor in Lymnaea. Eur J of Biochem 2001;268(5): 1213-21.
    • (2001) Eur J of Biochem , vol.268 , Issue.5 , pp. 1213-1221
    • Nagle, G.T.1    Jong-Brink, M.2    Painter, S.D.3    Li, K.W.4
  • 28
    • 0025349323 scopus 로고
    • Disulfide bridge structure of ascidian-trypsin inhibitor I: Similarity of Kazal-type inhibitors
    • Kumazaki T, Ishii S. Disulfide bridge structure of ascidian-trypsin inhibitor I: similarity of Kazal-type inhibitors. J Biochem (Tokyo) 1990;107(3):414-9.
    • (1990) J Biochem (Tokyo) , vol.107 , Issue.3 , pp. 414-419
    • Kumazaki, T.1    Ishii, S.2
  • 29
    • 0030057879 scopus 로고    scopus 로고
    • Shishikura F, Abe T, Ohtake S, Tanaka K. Purification and characterization of a 58 000-Da proteinase inhibitor from hemolynph of a solitary ascidian Holocynthia roretzi. Comp Biochem Phys B, Biochem Mol Biol 1996;114(1):1-9.
    • Shishikura F, Abe T, Ohtake S, Tanaka K. Purification and characterization of a 58 000-Da proteinase inhibitor from hemolynph of a solitary ascidian Holocynthia roretzi. Comp Biochem Phys B, Biochem Mol Biol 1996;114(1):1-9.
  • 32
    • 77956987594 scopus 로고
    • Titration of trypsin, plasmin and thrombin with p-nitrophenyl-p′-guanidinobenzoate HCl
    • Chase T, Shaw E. Titration of trypsin, plasmin and thrombin with p-nitrophenyl-p′-guanidinobenzoate HCl. Methods in Enzymology 1970;19:20-7.
    • (1970) Methods in Enzymology , vol.19 , pp. 20-27
    • Chase, T.1    Shaw, E.2
  • 33
    • 0001396685 scopus 로고
    • The slow-binding and slow, tight-binding inhibition of enzyme-catalyzed reactions
    • Morrison JF. The slow-binding and slow, tight-binding inhibition of enzyme-catalyzed reactions. TIBS 1982;7:102-5.
    • (1982) TIBS , vol.7 , pp. 102-105
    • Morrison, J.F.1
  • 34
    • 0024779439 scopus 로고
    • Isolation and characterization of plant inhibitors directed against plasma kallikrein and factor XII
    • Oliva ML, Sampaio MU, Sampaio CAM. Isolation and characterization of plant inhibitors directed against plasma kallikrein and factor XII. Adv Exp Med Biol 1988;247A: 467-71.
    • (1988) Adv Exp Med Biol , vol.247 A , pp. 467-471
    • Oliva, M.L.1    Sampaio, M.U.2    Sampaio, C.A.M.3
  • 35
    • 77149160700 scopus 로고    scopus 로고
    • Microsoft Corp (1992) GraFit Software. Version 3.1 Erithacus Sofware Ltd
    • Microsoft Corp (1992) GraFit Software. Version 3.1 Erithacus Sofware Ltd.
  • 36
    • 0024837758 scopus 로고
    • Estimation of plasma kallikrein in sickle cell anemia, and its relation to the coagulation and fibrinolytic systems
    • Lourenço DM, Sampaio MU, Sampaio CAM. Estimation of plasma kallikrein in sickle cell anemia, and its relation to the coagulation and fibrinolytic systems. Adv Exp Med Biol 1990;247B:553-7.
    • (1990) Adv Exp Med Biol , vol.247 B , pp. 553-557
    • Lourenço, D.M.1    Sampaio, M.U.2    Sampaio, C.A.M.3
  • 37
    • 0031845470 scopus 로고    scopus 로고
    • Glycosaminoglycans in two mollusks, Aplysia californica and Helix aspersa, and the leech, Nephelopsis obscura
    • Hovingh P, Linker A. Glycosaminoglycans in two mollusks, Aplysia californica and Helix aspersa, and the leech, Nephelopsis obscura. Comp Biochem Phys B 1998;119: 691-6.
    • (1998) Comp Biochem Phys B , vol.119 , pp. 691-696
    • Hovingh, P.1    Linker, A.2
  • 38
    • 0014601864 scopus 로고
    • Cardiovascular effect of a prostaglandin isolated from a gorgonia Plexaura homomalla
    • Nakano J. Cardiovascular effect of a prostaglandin isolated from a gorgonia Plexaura homomalla. J Pharmacy Pharm 1969;21(11):782-3.
    • (1969) J Pharmacy Pharm , vol.21 , Issue.11 , pp. 782-783
    • Nakano, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.