메뉴 건너뛰기




Volumn 287, Issue 19, 2012, Pages 15427-15438

Tri-domain bifunctional inhibitor of metallocarboxypeptidases A and serine proteases isolated from marine annelid Sabellastarte magnifica

Author keywords

[No Author keywords available]

Indexed keywords

BIFUNCTIONAL; BIFUNCTIONAL INHIBITORS; BOVINE PANCREATIC TRYPSIN; BOVINE PANCREATIC TRYPSIN INHIBITORS; C-TERMINAL DOMAINS; CYSTEINE RESIDUES; DISULFIDE BONDS; EDMAN DEGRADATION; ELASTASE; MARINE ANNELIDS; NANOMOLAR; NESTED PCR; PEPTIDE FRAGMENTS; PICHIA PASTORIS; SERINE PROTEASE; SERINE PROTEASE INHIBITOR;

EID: 84860869251     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.337261     Document Type: Article
Times cited : (24)

References (79)
  • 1
    • 20444460605 scopus 로고    scopus 로고
    • Messerschmidt, A. Bode, W., and Cygler, M., eds John Wiley & Sons Ltd., Chichester, UK
    • Vendrell, J., Aviles, F. X., and Fricker, L. D. (2006) in Handbook of Metalloproteins (Messerschmidt, A. Bode, W., and Cygler, M., eds) Vol. 3, pp. 176-189, John Wiley & Sons Ltd., Chichester, UK
    • (2006) Handbook of Metalloproteins , vol.3 , pp. 176-189
    • Vendrell, J.1    Aviles, F.X.2    Fricker, L.D.3
  • 2
    • 33947590948 scopus 로고    scopus 로고
    • Metallocarboxypeptidases: Emerging drug targets in biomedicine
    • DOI 10.2174/138161207779313614
    • Arolas, J. L., Vendrell, J., Aviles, F. X., and Fricker, L. D. (2007) Metallocarboxypeptidases: emerging drug targets in biomedicine. Curr. Pharm. Des. 13, 347-364 (Pubitemid 46085283)
    • (2007) Current Pharmaceutical Design , vol.13 , Issue.3 , pp. 347-364
    • Arolas, J.L.1    Vendrell, J.2    Aviles, F.X.3    Fricker, L.D.4
  • 3
    • 0019879637 scopus 로고
    • Amino acid sequence of a carboxypeptidase inhibitor from tomato fruit
    • Hass, G. M., and Hermodson, M. A. (1981) Amino acid sequence of a carboxypeptidase inhibitor from tomato fruit. Biochemistry 20, 2256-2260
    • (1981) Biochemistry , vol.20 , pp. 2256-2260
    • Hass, G.M.1    Hermodson, M.A.2
  • 4
    • 0032573588 scopus 로고    scopus 로고
    • Characterization of the wound-induced metallocarboxypeptidase inhibitor from potato: cDNA sequence, induction of gene expression, subcellular immunolocalization and potential roles of the C-terminal propeptide
    • DOI 10.1016/S0014-5793(98)01447-1, PII S0014579398014471
    • Villanueva, J., Canals, F., Prat, S., Ludevid, D., Querol, E., and Avilés, F. X. (1998) Characterization of the wound-induced metallocarboxypeptidase inhibitor from potato. cDNA sequence, induction of gene expression, subcellular immunolocalization and potential roles of the C-terminal propeptide. FEBS Lett. 440, 175-182 (Pubitemid 28558760)
    • (1998) FEBS Letters , vol.440 , Issue.1-2 , pp. 175-182
    • Villanueva, J.1    Canals, F.2    Prat, S.3    Ludevid, D.4    Querol, E.5    Aviles, F.X.6
  • 5
    • 0019052776 scopus 로고
    • Structure of the potato inhibitor complex of carboxypeptidase A at 2.5 Å
    • Rees, D. C., and Lipscomb, W. N. (1980) Structure of the potato inhibitor complex of carboxypeptidase A at 2.5 Å. Proc. Natl. Acad. Sci. 77, 4633-4637
    • (1980) Proc. Natl. Acad. Sci. , vol.77 , pp. 4633-4637
    • Rees, D.C.1    Lipscomb, W.N.2
  • 6
    • 0024651408 scopus 로고
    • Carboxypeptidase inhibitors from Ascaris suum. The primary structure
    • Homandberg, G. A., Litwiller, R. D., and Peanasky, R. J. (1989) Carboxypeptidase inhibitors from Ascaris suum. The primary structure. Arch. Biochem. Biophys. 270, 153-161
    • (1989) Arch. Biochem. Biophys. , vol.270 , pp. 153-161
    • Homandberg, G.A.1    Litwiller, R.D.2    Peanasky, R.J.3
  • 8
    • 0032484025 scopus 로고    scopus 로고
    • A carboxypeptidase inhibitor from the medical leech Hirudo medicinalis: Isolation, sequence analysis, cDNA cloning, recombinant expression, and characterization
    • DOI 10.1074/jbc.273.49.32927
    • Reverter, D., Vendrell, J., Canals, F., Horstmann, J., Avilés, F. X., Fritz, H., and Sommerhoff, C. P. (1998) A carboxypeptidase inhibitor from the medical leech Hirudo medicinalis. Isolation, sequence analysis, cDNA cloning, recombinant expression, and characterization. J. Biol. Chem. 273, 32927-32933 (Pubitemid 28557685)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.49 , pp. 32927-32933
    • Reverter, D.1    Vendrell, J.2    Canals, F.3    Horstmann, J.4    Aviles, F.X.5    Fritz, H.6    Sommerhoff, C.P.7
  • 9
    • 13544272567 scopus 로고    scopus 로고
    • A carboxypeptidase inhibitor from the tick Rhipicephalus bursa: Isolation, cDNA cloning, recombinant expression, and characterization
    • DOI 10.1074/jbc.M411086200
    • Arolas, J. L., Lorenzo, J., Rovira, A., Castellà, J., Aviles, F. X., and Sommerhoff, C. P. (2005) A carboxypeptidase inhibitor from the tick Rhipicephalus bursa. Isolation, cDNA cloning, recombinant expression, and characterization. J. Biol. Chem. 280, 3441-3448 (Pubitemid 40223808)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.5 , pp. 3441-3448
    • Arolas, J.L.1    Lorenzo, J.2    Rovira, A.3    Castella, J.4    Aviles, F.X.5    Sommerhoff, C.P.6
  • 10
    • 34748904625 scopus 로고    scopus 로고
    • Characterization of a carboxypeptidase inhibitor from the tick Haemaphysalis longicornis
    • DOI 10.1016/j.jinsphys.2007.06.008, PII S002219100700131X
    • Gong, H., Zhou, J., Liao, M., Hatta, T., Harnnoi, T., Umemiya, R., Inoue, N., Xuan, X., and Fujisaki, K. (2007) Characterization of a carboxypeptidase inhibitor from the tick Haemaphysalis longicornis. J. Insect Physiol. 53,1079-1087 (Pubitemid 47488385)
    • (2007) Journal of Insect Physiology , vol.53 , Issue.10 , pp. 1079-1087
    • Gong, H.1    Zhou, J.2    Liao, M.3    Hatta, T.4    Harnnoi, T.5    Umemiya, R.6    Inoue, N.7    Xuan, X.8    Fujisaki, K.9
  • 12
    • 0034436795 scopus 로고    scopus 로고
    • Cloning, tissue expression pattern and genomic organization of latexin, a human homologue of rat carboxypeptidase A inhibitor
    • DOI 10.1023/A:1010971219806
    • Liu, Q., Yu, L., Gao, J., Fu, Q., Zhang, J., Zhang, P., Chen, J., Zhao, S. (2000) Cloning, tissue expression pattern, and genomic organization of latexin, a human homologue of rat carboxypeptidase A inhibitor. Mol. Biol. Rep. 27, 241-246 (Pubitemid 32608414)
    • (2000) Molecular Biology Reports , vol.27 , Issue.4 , pp. 241-246
    • Liu, Q.1    Yu, L.2    Gao, J.3    Fu, Q.4    Zhang, J.5    Zhang, P.6    Chen, J.7    Zhao, S.8
  • 13
    • 20444446808 scopus 로고    scopus 로고
    • The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode
    • DOI 10.1016/j.jmb.2005.05.015, PII S0022283605005462
    • Arolas, J. L., Popowicz, G. M., Lorenzo, J., Sommerhoff, C. P., Huber, R., Aviles, F. X., and Holak, T. A. (2005) The three-dimensional structures of tick carboxypeptidase inhibitor in complex with A/B carboxypeptidases reveal a novel double-headed binding mode. J. Mol. Biol. 350, 489-498 (Pubitemid 40828909)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.3 , pp. 489-498
    • Arolas, J.L.1    Popowicz, G.M.2    Lorenzo, J.3    Sommerhoff, C.P.4    Huber, R.5    Aviles, F.X.6    Holak, T.A.7
  • 15
    • 0026548881 scopus 로고
    • Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation
    • Guasch, A., Coll, M., Avilés, F. X., and Huber, R. (1992) Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation. J. Mol. Biol. 224, 141-157
    • (1992) J. Mol. Biol. , vol.224 , pp. 141-157
    • Guasch, A.1    Coll, M.2    Avilés, F.X.3    Huber, R.4
  • 16
    • 0033538529 scopus 로고    scopus 로고
    • Mapping the pro-region of carboxypeptidase B by protein engineering. Cloning, overexpression, and mutagenesis of the porcine proenzyme
    • Ventura, S., Villegas, V., Sterner, J., Larson, J., Vendrell, J., Hershberger, C. L., and Avilés, F. X. (1999) Mapping the pro-region of carboxypeptidase B by protein engineering. Cloning, overexpression, and mutagenesis of the porcine proenzyme. J. Biol. Chem. 274, 19925-19933
    • (1999) J. Biol. Chem. , vol.274 , pp. 19925-19933
    • Ventura, S.1    Villegas, V.2    Sterner, J.3    Larson, J.4    Vendrell, J.5    Hershberger, C.L.6    Avilés, F.X.7
  • 17
    • 0027968784 scopus 로고
    • Proteinase inhibitor from Stichodactyla helianthus. Purification, characterization, and immobilization
    • Delfín, J., González, Y., Díaz, J., and Chávez, M. (1994) Proteinase inhibitor from Stichodactyla helianthus. Purification, characterization, and immobilization. Arch. Med. Res. 25, 199-204
    • (1994) Arch. Med. Res. , vol.25 , pp. 199-204
    • Delfín, J.1    González, Y.2    Díaz, J.3    Chávez, M.4
  • 18
    • 0040020321 scopus 로고    scopus 로고
    • Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin type-1 domain
    • Lenarcic, B., Ritonja, A., Strukelj, B., Turk, B., and Turk, V. (1997) Equistatin, a new inhibitor of cysteine proteinases from Actinia equina, is structurally related to thyroglobulin-type-1 domain. J. Biol. Chem. 272, 13899-13903 (Pubitemid 27224832)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.21 , pp. 13899-13903
    • Lenarcic, B.1    Ritonja, A.2    Strukelj, B.3    Turk, B.4    Turk, V.5
  • 20
    • 0018825666 scopus 로고
    • Isolation of proteinase inhibitory, toxic and hemolytic polypeptides from a sea anemone. Stoichactis sp.
    • Mebs, D., and Gebauer, E. (1980) Isolation of proteinase inhibitory, toxic, and hemolytic polypeptides from a sea anemone. Stoichactis sp. Toxicon 18, 97-106 (Pubitemid 10100701)
    • (1980) Toxicon , vol.18 , Issue.1 , pp. 97-106
    • Mebs, D.1    Gebauer, E.2
  • 22
    • 0015263278 scopus 로고
    • Polyvalent isoinhibitors for trypsin, chymotrypsin, plasmin, and kallikreins of sea anemones (Anemonia sulcata), isolation, inhibitory behavior, and amino acid composition
    • Fritz, H., Brey, B., and Béress, L. (1972) Polyvalent isoinhibitors for trypsin, chymotrypsin, plasmin, and kallikreins of sea anemones (Anemonia sulcata), isolation, inhibitory behavior, and amino acid composition. Hoppe-Seyler's Z. Physiol. Chem. 353, 19-30
    • (1972) Hoppe-Seyler's Z. Physiol. Chem. , vol.353 , pp. 19-30
    • Fritz, H.1    Brey, B.2    Béress, L.3
  • 23
    • 0023285482 scopus 로고
    • A new inhibitor of elastase from the sea anemone (Anemonia sulcata)
    • Kolkenbrock, H., and Tschesche, H. (1987) A new inhibitor of elastase from the sea anemone (Anemonia sulcata). Biol. Chem. Hoppe-Seyler 368, 93-99
    • (1987) Biol. Chem. Hoppe-Seyler , vol.368 , pp. 93-99
    • Kolkenbrock, H.1    Tschesche, H.2
  • 24
    • 0023433076 scopus 로고
    • The covalent structure of the elastase inhibitor from Anemonia sulcata. A "nonclassical"Kazal-type protein
    • Tschesche, H., Kolkenbrock, H., and Bode, W. (1987) The covalent structure of the elastase inhibitor from Anemonia sulcata. A "nonclassical"Kazal-type protein. Biol. Chem. Hoppe-Seyler 368, 1297-1304
    • (1987) Biol. Chem. Hoppe-Seyler , vol.368 , pp. 1297-1304
    • Tschesche, H.1    Kolkenbrock, H.2    Bode, W.3
  • 25
    • 85044705249 scopus 로고    scopus 로고
    • Low molecular cytolysins and trypsin inhibitors from sea anemone Radianthus macrodactylus. Isolation and partial characterization
    • Zykova, T. A., Monastyrnaia, M. M., Apalikova, O. V., Shvets, T. V., and Kozlovskaia, E. P. (1998) Low molecular cytolysins and trypsin inhibitors from sea anemone Radianthus macrodactylus. Isolation and partial characterization. Bioorg. Khim. 24, 509-516
    • (1998) Bioorg. Khim. , vol.24 , pp. 509-516
    • Zykova, T.A.1    Monastyrnaia, M.M.2    Apalikova, O.V.3    Shvets, T.V.4    Kozlovskaia, E.P.5
  • 26
    • 0000038862 scopus 로고
    • Amino acid sequence of trypsin inhibitor IV from the sea anemone Radianthus macrodactylus
    • Zykova, T. A., Vinokurov, L. M., Markova, L. F., Kozlovskaya, E. P., and Elyakov, G. B. (1985) Amino acid sequence of trypsin inhibitor IV from the sea anemone Radianthus macrodactylus. Bioorg. Khim. 11, 293-301
    • (1985) Bioorg. Khim. , vol.11 , pp. 293-301
    • Zykova, T.A.1    Vinokurov, L.M.2    Markova, L.F.3    Kozlovskaya, E.P.4    Elyakov, G.B.5
  • 28
    • 1442359904 scopus 로고    scopus 로고
    • Purification and preliminary characterization of a plasma kallikrein inhibitor isolated from sea hares Aplysia dactylomela Rang, 1828
    • DOI 10.1016/j.toxicon.2003.11.016, PII S0041010103003428
    • Gonzalez, Y., Araujo, M. S., Oliva, M. L., Sampaio, C. A., and Chávez, M. A. (2004) Purification and preliminary characterization of a plasma kallikrein inhibitor isolated from sea hares Aplysia dactylomela Rang. 1828. Toxicon 23, 219-223 (Pubitemid 38281238)
    • (2004) Toxicon , vol.43 , Issue.2 , pp. 219-223
    • Gonzalez, Y.1    Araujo, M.S.2    Oliva, M.L.V.3    Sampaio, C.A.M.4    Chavez, M.A.5
  • 30
    • 0035085233 scopus 로고    scopus 로고
    • Structure, localization and potential role of a novel molluscan trypsin inhibitor in Lymnaea
    • DOI 10.1046/j.1432-1327.2001.01972.x
    • Nagle, G. T., de Jong-Brink, M., Painter, S. D., and Li, K. W. (2001) Structure, localization, and potential role of a novel molluscan trypsin inhibitor in Lymnaea. Eur. J. Biochem. 268, 1213-1221 (Pubitemid 32231873)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.5 , pp. 1213-1221
    • Nagle, G.T.1    De Jong-Brink, M.2    Painter, S.D.3    Li, K.W.4
  • 31
    • 35848964031 scopus 로고    scopus 로고
    • Characterization and comparative three-dimensional modeling of CmPI-II, a novel "nonclassical"Kazal-type inhibitor from the marine snail Cenchritis muricatus (Mollusca)
    • González, Y., Pons, T., Gil, J., Besada, V., Alonso-del-Rivero, M., Tanaka, A. S., Araujo, M. S., and Chávez, M. A. (2007) Characterization and comparative three-dimensional modeling of CmPI-II, a novel "nonclassical"Kazal-type inhibitor from the marine snail Cenchritis muricatus (Mollusca). Biol. Chem. 388, 1183-1194
    • (2007) Biol. Chem. , vol.388 , pp. 1183-1194
    • González, Y.1    Pons, T.2    Gil, J.3    Besada, V.4    Alonso-del-Rivero, M.5    Tanaka, A.S.6    Araujo, M.S.7    Chávez, M.A.8
  • 32
    • 0017122851 scopus 로고
    • Further characterization of trypsin inhibitors in the polychaet Sabellastarte indica (Savigny), II
    • Mitteilung, Z. (1976) Further characterization of trypsin inhibitors in the polychaet Sabellastarte indica (Savigny), II. J. Clin. Chem. Clin. Biochem. 14, 245-251
    • (1976) J. Clin. Chem. Clin. Biochem. , vol.14 , pp. 245-251
    • Mitteilung, Z.1
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0030218802 scopus 로고    scopus 로고
    • Arazoformyl peptide surrogates as spectrophotometric kinetic assay substrates for carboxypeptidase A
    • DOI 10.1006/abio.1996.0318
    • Mock, W. L., Liu, Y., and Stanford, D. J. (1996) Arazoformyl peptide surrogates as spectrophotometric kinetic assay substrates for carboxypeptidase A. Anal. Biochem. 239, 218-222 (Pubitemid 26268805)
    • (1996) Analytical Biochemistry , vol.239 , Issue.2 , pp. 218-222
    • Mock, W.L.1    Liu, Y.2    Stanford, D.J.3
  • 38
    • 0033579982 scopus 로고    scopus 로고
    • Catalytic activity of carboxypeptidase B and of carboxypeptidase Y with anisylazoformyl substrates
    • DOI 10.1016/S0960-894X(98)00715-X, PII S0960894X9800715X
    • Mock, W. L., and Xu, D. (1999) Catalytic activity of carboxypeptidase B and of carboxypeptidase Y with anisylazoformyl substrates. Bioorg. Med. Chem. Lett. 9, 187-192 (Pubitemid 29059525)
    • (1999) Bioorganic and Medicinal Chemistry Letters , vol.9 , Issue.2 , pp. 187-192
    • Mock, W.L.1    Donghong, X.2
  • 39
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates of trypsin
    • Erlanger, B. F., Kokowsky, N., and Cohen, E. (1961) The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 95, 271-278
    • (1961) Arch. Biochem. Biophys. , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, E.3
  • 41
    • 0018747530 scopus 로고
    • Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the (α1)-protease inhibitor reactive site
    • Nakajima, K., Powers, J. C., Ashe, B. M., and Zimmerman, M. (1979) Mapping the extended substrate-binding site of cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the α1-protease inhibitor reactive site. J. Biol. Chem. 254, 4027-4032 (Pubitemid 9178816)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.10 , pp. 4027-4032
    • Nakajima, K.1    Powers, J.C.2    Ashe, B.M.3    Zimmermann, M.4
  • 42
    • 0014942114 scopus 로고
    • Mapping the active site of papain with the aid of peptide substrates and inhibitors
    • Berger, A., and Schechter, I. (1970) Mapping the active site of papain with the aid of peptide substrates and inhibitors. Philos. Trans. R. Soc. Lond. Biol. 257, 249-264
    • (1970) Philos. Trans. R. Soc. Lond. Biol. , vol.257 , pp. 249-264
    • Berger, A.1    Schechter, I.2
  • 43
    • 0019322201 scopus 로고
    • Kinetic studies on the action of Mucor pusillus, Mucor miehei acid proteases. and chymosins A and B on a synthetic chromophoric hexapeptide
    • Martin, P., Raymond, M. N., Bricas, E., and Dumas, B. R. (1980) Kinetic studies on the action of Mucor pusillus, Mucor miehei acid proteases. and chymosins A and B on a synthetic chromophoric hexapeptide. Biochim. Biophys. Acta 612, 410-420
    • (1980) Biochim. Biophys. Acta , vol.612 , pp. 410-420
    • Martin, P.1    Raymond, M.N.2    Bricas, E.3    Dumas, B.R.4
  • 44
    • 33644864110 scopus 로고
    • p-Nitrophenyl-p′-guanidinobenzoate HCl. A new active site titrant for trypsin
    • Chase, T., Jr., and Shaw, E. (1967) p-Nitrophenyl-p′- guanidinobenzoate HCl. A new active site titrant for trypsin. Biochem. Biophys. Res. Commun. 29, 508-514
    • (1967) Biochem. Biophys. Res. Commun. , vol.29 , pp. 508-514
    • Chase Jr., T.1    Shaw, E.2
  • 45
    • 0029003409 scopus 로고
    • Theoretical and practical aspects of proteinase inhibition kinetics
    • Bieth, J. G. (1995) Theoretical and practical aspects of proteinase inhibition kinetics. Methods Enzymol. 248, 59-84
    • (1995) Methods Enzymol. , vol.248 , pp. 59-84
    • Bieth, J.G.1
  • 46
    • 0018699952 scopus 로고
    • The kinetics of reversible tight-binding inhibition
    • Williams, J. W., and Morrison, J. F. (1979) The kinetics of reversible tight-binding inhibition. Methods Enzymol. 63, 437-467
    • (1979) Methods Enzymol. , vol.63 , pp. 437-467
    • Williams, J.W.1    Morrison, J.F.2
  • 47
    • 0000717689 scopus 로고
    • Bergmeyer, H. U., ed 2nd Ed., Academic Press, Inc., New York
    • Bergmeyer, H. U., Gawehn, K., and Grassl, M. (1974) in Methods of Enzymatic Analysis (Bergmeyer, H. U., ed) Vol. 1, 2nd Ed., pp. 436-437, Academic Press, Inc., New York
    • (1974) Methods of Enzymatic Analysis , vol.1 , pp. 436-437
    • Bergmeyer, H.U.1    Gawehn, K.2    Grassl, M.3
  • 48
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • DOI 10.1093/nar/25.17.3389
    • Altschul, S. F., Madden, T. L., Schäffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J. (1997) Gapped BLAST and PSI-BLAST. A new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402 (Pubitemid 27359211)
    • (1997) Nucleic Acids Research , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 50
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • DOI 10.1093/nar/25.24.4876
    • Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., and Higgins, D. G. (1997) The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882 (Pubitemid 28022245)
    • (1997) Nucleic Acids Research , vol.25 , Issue.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 51
    • 0025259313 scopus 로고
    • Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes
    • Karlin, S., and Altschul, S. F (1990) Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes. Proc. Nat. Acad. Sci. U.S.A. 87, 2264-2268
    • (1990) Proc. Nat. Acad. Sci. U.S.A. , vol.87 , pp. 2264-2268
    • Karlin, S.1    Altschul, S.F.2
  • 53
    • 35448942782 scopus 로고    scopus 로고
    • Evaluation of three-dimensional Jury on CASP7 models
    • Kaján, L., and Rychlewski, L. (2007) Evaluation of three-dimensional Jury on CASP7 models. BMC Bioinformatics 8, 304
    • (2007) BMC Bioinformatics , vol.8 , pp. 304
    • Kaján, L.1    Rychlewski, L.2
  • 54
  • 56
    • 0034703067 scopus 로고    scopus 로고
    • A broad spectrum Kunitz type serine protease inhibitor secreted by the hookworm Ancylostoma ceylanicum
    • DOI 10.1074/jbc.M002715200
    • Milstone, A. M., Harrison, L. M., Bungiro, R. D., Kuzmic, P., and Cappello, M. (2000) A broad spectrum Kunitz-type serine protease inhibitor secreted by the hookworm Ancylostoma ceylanicum. J. Biol. Chem. 275, 29391-29399 (Pubitemid 32043812)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.38 , pp. 29391-29399
    • Milstone, A.M.1    Harrison, L.M.2    Bungiro, R.D.3    Kuzmic, P.4    Cappello, M.5
  • 57
    • 0041662114 scopus 로고    scopus 로고
    • Rhipicephalus sanguineus trypsin inhibitors present in the tick larvae: Isolation, characterization, and partial primary structure determination
    • DOI 10.1016/S0003-9861(03)00344-8
    • Sant'Anna Azzolini, S., Sasaki, S. D., Torquato, R. J., Andreotti, R., Andreotti, E., and Tanaka, A. S. (2003) Rhipicephalus sanguineus trypsin inhibitors present in the tick larvae. Isolation, characterization, and partial primary structure determination. Arch. Biochem. Biophys. 417, 176-182 (Pubitemid 36993793)
    • (2003) Archives of Biochemistry and Biophysics , vol.417 , Issue.2 , pp. 176-182
    • Azzolini, S.S.'A.1    Sasaki, S.D.2    Soares, T.R.J.3    Andreotti, R.4    Andreotti, E.5    Tanaka, A.S.6
  • 58
    • 0032735453 scopus 로고    scopus 로고
    • A double-headed serine proteinase inhibitor, human plasma kallikrein and elastase inhibitor, from Boophilus microplus larvae
    • Tanaka, A. S., Andreotti, R., Gomes, A., Torquato, R. J., Sampaio, M. U., and Sampaio, C. A. (1999) A double-headed serine proteinase inhibitor, human plasma kallikrein and elastase inhibitor, from Boophilus microplus larvae. Immunopharmacology 45, 171-177
    • (1999) Immunopharmacology , vol.45 , pp. 171-177
    • Tanaka, A.S.1    Andreotti, R.2    Gomes, A.3    Torquato, R.J.4    Sampaio, M.U.5    Sampaio, C.A.6
  • 59
    • 0020678186 scopus 로고
    • Biochemistry and applications of aprotinin, the kallikrein inhibitor from bovine organs
    • Fritz, H., and Wunderer, G. (1983) Biochemistry and applications of aprotinin, the kallikrein inhibitor from bovine organs. Arzneimittelforschung 33, 479-494 (Pubitemid 13161964)
    • (1983) Arzneimittel-Forschung/Drug Research , vol.33 , Issue.4 , pp. 479-494
    • Fritz, H.1    Wunderer, G.2
  • 60
    • 0033556259 scopus 로고    scopus 로고
    • Primary structure and possible functions of a trypsin inhibitor of Bombyx mori
    • DOI 10.1046/j.1432-1327.1999.00030.x
    • Kurioka, A., Yamazaki, M., and Hirano, H. (1999) Primary structure and possible functions of a trypsin inhibitor of Bombyx mori. Eur. J. Biochem. 259, 120-126 (Pubitemid 29030826)
    • (1999) European Journal of Biochemistry , vol.259 , Issue.1-2 , pp. 120-126
    • Kurioka, A.1    Yamazaki, M.2    Hirano, H.3
  • 61
    • 0032513008 scopus 로고    scopus 로고
    • The crystal structure of bikunin from the inter-α-inhibitor complex: A serine protease inhibitor with two Kunitz domains
    • DOI 10.1006/jmbi.1997.1582
    • Xu, Y., Carr, P. D., Guss, J. M., and Ollis, D. L (1998) The crystal structure of bikunin from the inter-α-inhibitor complex.Aserine protease inhibitor with two Kunitz domains. J. Mol. Biol. 276, 955-966 (Pubitemid 28130267)
    • (1998) Journal of Molecular Biology , vol.276 , Issue.5 , pp. 955-966
    • Xu, Y.1    Carr, P.D.2    Guss, J.M.3    Ollis, D.L.4
  • 62
    • 0021045341 scopus 로고
    • 1-7]. Characterization of the bovine inhibitor as double-headed trypsin-elastase inhibitor
    • Hochstrasser, K., Albrecht, G., Schönberger, O. L., and Wachter, E. (1983) Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-α-trypsin inhibitor, VII. Characterization of the bovine inhibitor as double-headed trypsin-elastase inhibitor. Hoppe-Seyler's Z. Physiol. Chem. 364, 1689-1696 (Pubitemid 14198436)
    • (1983) Hoppe-Seyler's Zeitschrift fur Physiologische Chemie , vol.364 , Issue.12 , pp. 1689-1696
    • Hochstrasser, K.1    Albrecht, G.J.2    Schonberger, O.L.3    Wachter, E.4
  • 63
    • 0030959314 scopus 로고    scopus 로고
    • Identification and cloning of human placental bikunin, a novel serine protease inhibitor containing two Kunitz domains
    • DOI 10.1074/jbc.272.18.12202
    • Marlor, C. W., Delaria, K. A., Davis, G., Muller, D. K., Greve, J. M., and Tamburini, P. P. (1997) Identification and cloning of human placental bikunin, a novel serine protease inhibitor containing two Kunitz domains. J. Biol. Chem. 272, 12202-12208 (Pubitemid 27202805)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.18 , pp. 12202-12208
    • Marlor, C.W.1    Delaria, K.A.2    Davis, G.3    Muller, D.K.4    Greve, J.M.5    Tamburini, P.P.6
  • 64
    • 2342419730 scopus 로고    scopus 로고
    • Structure-Function Analysis of the Reactive Site in the First Kunitz-type Domain of Human Tissue Factor Pathway Inhibitor-2
    • DOI 10.1074/jbc.M400802200
    • Chand, H. S., Schmidt, A. E., Bajaj, S. P., and Kisiel, W. (2004) Structure-function analysis of the reactive site in the first Kunitz-type domain of human tissue factor pathway inhibitor-2. J. Biol. Chem. 279, 17500-17507 (Pubitemid 38560513)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 17500-17507
    • Chand, H.S.1    Schmidt, A.E.2    Bajaj, S.P.3    Kisiel, W.4
  • 65
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • DOI 10.1016/S0168-6445(99)00029-7, PII S0168644599000297
    • Cereghino, J. L., and Cregg, J. M. (2000) Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 24, 45-66 (Pubitemid 30047114)
    • (2000) FEMS Microbiology Reviews , vol.24 , Issue.1 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 66
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode, W., and Huber, R. (1992) Natural protein proteinase inhibitors and their interaction with proteinases. Eur J. Biochem. 204, 433-451
    • (1992) Eur J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 68
    • 0034602930 scopus 로고    scopus 로고
    • High resolution structure of bovine pancreatic trypsin inhibitor with altered binding loop sequence
    • Czapinska, H., Otlewski, J., Krzywda, S., Sheldrick, G. M., and Jaskólski, M. (2000) High resolution structure of bovine pancreatic trypsin inhibitor with altered binding loop sequence. J. Mol. Biol. 295, 1237-1249
    • (2000) J. Mol. Biol. , vol.295 , pp. 1237-1249
    • Czapinska, H.1    Otlewski, J.2    Krzywda, S.3    Sheldrick, G.M.4    Jaskólski, M.5
  • 69
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski, M., Jr., and Kato, I. (1980) Protein inhibitors of proteinases. Annu. Rev. Biochem. 49, 593-626
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski Jr., M.1    Kato, I.2
  • 70
    • 0034604364 scopus 로고    scopus 로고
    • Substitutions at the P(1) position in BPTI strongly affect the association energy with serine proteinases
    • Grzesiak, A., Helland, R., Smalås, A. O., Krowarsch, D., Dadlez, M., and Otlewski, J. (2000) Substitutions at the P(1) position in BPTI strongly affect the association energy with serine proteinases. J. Mol. Biol. 301, 205-217
    • (2000) J. Mol. Biol. , vol.301 , pp. 205-217
    • Grzesiak, A.1    Helland, R.2    Smalås, A.O.3    Krowarsch, D.4    Dadlez, M.5    Otlewski, J.6
  • 72
    • 0033612211 scopus 로고    scopus 로고
    • 1 variants of bovine pancreatic trypsin inhibitor to four serine proteases
    • DOI 10.1006/jmbi.1999.2757
    • Krowarsch, D., Dadlez, M., Buczek, O., Krokoszynska, I., Smalas, A. O., and Otlewski, J. (1999) Interscaffolding additivity: binding of P1 variants of bovine pancreatic trypsin inhibitor to four serine proteases. J. Mol. Biol. 289, 175-186 (Pubitemid 29278373)
    • (1999) Journal of Molecular Biology , vol.289 , Issue.1 , pp. 175-186
    • Krowarsch, D.1    Dadlez, M.2    Buczek, O.3    Krokoszynska, I.4    Smalas, A.O.5    Otlewski, J.6
  • 73
    • 13844296946 scopus 로고    scopus 로고
    • Conformational lability in serine protease active sites: Structures of hepatocyte growth factor activator (HGFA) alone and with the inhibitory domain from HGFA inhibitor-1B
    • DOI 10.1016/j.jmb.2004.12.048
    • Shia, S., Stamos, J., Kirchhofer, D., Fan, B., Wu, J., Corpuz, R. T., Santell, L., Lazarus, R. A., and Eigenbrot, C. (2005) Conformational lability in serine protease active sites. Structures of hepatocyte growth factor activator (HGFA) alone and with the inhibitory domain from HGFA inhibitor-1B. J. Mol. Biol. 346, 1335-1349 (Pubitemid 40248833)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.5 , pp. 1335-1349
    • Shia, S.1    Stamos, J.2    Kirchhofer, D.3    Fan, B.4    Wu, J.5    Corpuz, R.T.6    Santell, L.7    Lazarus, R.A.8    Eigenbrot, C.9
  • 74
    • 0033485402 scopus 로고    scopus 로고
    • Selection of human elastase inhibitors from a conformationally constrained combinatorial peptide library
    • McBride, J. D., Freeman, H. N., and Leatherbarrow, R. J. (1999) Selection of human elastase inhibitors from a conformationally constrained combinatorial peptide library. Eur. J. Biochem. 266, 403-412
    • (1999) Eur. J. Biochem. , vol.266 , pp. 403-412
    • McBride, J.D.1    Freeman, H.N.2    Leatherbarrow, R.J.3
  • 75
    • 0034682835 scopus 로고    scopus 로고
    • A novel double-headed proteinaceous inhibitor for metalloproteinase and serine proteinase
    • Hiraga, K., Suzuki, T., and Oda, K. (2000) A novel double-headed proteinaceous inhibitor for metalloproteinase and serine proteinase. J. Biol. Chem. 275, 25173-25179
    • (2000) J. Biol. Chem. , vol.275 , pp. 25173-25179
    • Hiraga, K.1    Suzuki, T.2    Oda, K.3
  • 77
    • 0025970932 scopus 로고
    • The three-dimensional structure of the bifunctional proteinase K/α-amylase inhibitor from wheat (PK13) at 2.5 Å resolution
    • Zemke, K. J., Müller-Fahrnow, A., Jany, K. D., Pal, G. P., and Saenger, W. (1991) The three-dimensional structure of the bifunctional proteinase K/α-amylase inhibitor from wheat (PK13) at 2.5 Å resolution. FEBS Lett. 279, 240-242
    • (1991) FEBS Lett. , vol.279 , pp. 240-242
    • Zemke, K.J.1    Müller-Fahrnow, A.2    Jany, K.D.3    Pal, G.P.4    Saenger, W.5
  • 78
    • 0032524130 scopus 로고    scopus 로고
    • Barley α-amylase bound to its endogenous protein inhibitor BASI: Crystal structure of the complex at 1.9 Å resolution
    • Vallée, F., Kadziola, A., Bourne, Y., Juy, M., Rodenburg, K. W., Svensson, B., and Haser, R. (1998) Barley α-amylase bound to its endogenous protein inhibitor BASI. Crystal structure of the complex at 1.9 Å resolution. Structure 6, 649-659 (Pubitemid 28258117)
    • (1998) Structure , vol.6 , Issue.5 , pp. 649-659
    • Vallee, F.1    Kadziola, A.2    Bourne, Y.3    Juy, M.4    Rodenburg, K.W.5    Svensson, B.6    Haser, R.7
  • 79
    • 2942711678 scopus 로고    scopus 로고
    • Secondary binding site of the potato carboxypeptidase inhibitor. Contribution to its structure, folding, and biological properties
    • DOI 10.1021/bi049596j
    • Arolas, J. L., Lorenzo, J., Rovira, A., Vendrell, J., Aviles, F. X., and Ventura, S. (2004) Secondary binding site of the potato carboxypeptidase inhibitor. Contribution to its structure, folding, and biological properties. Biochemistry 43, 7973-7982 (Pubitemid 38787707)
    • (2004) Biochemistry , vol.43 , Issue.24 , pp. 7973-7982
    • Arolas, J.L.1    Lorenzo, J.2    Rovira, A.3    Vendrell, J.4    Aviles, F.X.5    Ventura, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.