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Volumn 80, Issue 4, 1998, Pages 531-541

Structure-function relationships in serpins: Current concepts and controversies

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; LIGAND; PROTEINASE; SERINE PROTEINASE INHIBITOR;

EID: 0031755765     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (87)

References (161)
  • 1
    • 0019313931 scopus 로고
    • A surprising new protein superfamily containing ovaibumin
    • Hunt LT, Dayhoff MO. A surprising new protein superfamily containing ovaibumin. Biochem Biophys Res Commun 1980; 95: 864-71.
    • (1980) Biochem Biophys Res Commun , vol.95 , pp. 864-871
    • Hunt, L.T.1    Dayhoff, M.O.2
  • 2
    • 0021985069 scopus 로고
    • 1-antitrypsin and the serpins: Variation and counter-variation
    • 1-antitrypsin and the serpins: variation and counter-variation. Trends Biochem Sci 1985; 10: 20-4.
    • (1985) Trends Biochem Sci , vol.10 , pp. 20-24
    • Carrell, R.W.1    Travis, J.2
  • 3
    • 0021711639 scopus 로고
    • Ovaibumin is an elastase substrate
    • Wright HT. Ovaibumin is an elastase substrate. J Biol Chem 1984; 259; 14335-6.
    • (1984) J Biol Chem , vol.259 , pp. 14335-14336
    • Wright, H.T.1
  • 5
    • 0027446940 scopus 로고
    • Pigment epithelium-derived factor: Neurotrophic activity and identification as a member of the serine protease inhibitor gene family
    • Steele FR, Chader GJ, Johnson LV, Tombran-Tink J. Pigment epithelium-derived factor: neurotrophic activity and identification as a member of the serine protease inhibitor gene family. Proc Natl Acad Sci USA 1993; 90: 1526-30.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1526-1530
    • Steele, F.R.1    Chader, G.J.2    Johnson, L.V.3    Tombran-Tink, J.4
  • 6
    • 0026728952 scopus 로고
    • Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme
    • Ray CA, Black RA, Kronheim SR, Greenstreet TA, Sleath PR, Salvesen GS, Pickup DJ. Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme. Cell 1992; 69: 597-604.
    • (1992) Cell , vol.69 , pp. 597-604
    • Ray, C.A.1    Black, R.A.2    Kronheim, S.R.3    Greenstreet, T.A.4    Sleath, P.R.5    Salvesen, G.S.6    Pickup, D.J.7
  • 7
    • 0028814981 scopus 로고
    • Squamous cell carcinoma antigen is a potent inhibitor of cysteine proteinase cathepsin L
    • Takeda A, Yamamoto T, Nakamura Y, Takahashi T, Hibino T. Squamous cell carcinoma antigen is a potent inhibitor of cysteine proteinase cathepsin L. FEBS Lett 1995; 359: 78-80.
    • (1995) FEBS Lett , vol.359 , pp. 78-80
    • Takeda, A.1    Yamamoto, T.2    Nakamura, Y.3    Takahashi, T.4    Hibino, T.5
  • 8
    • 0028206262 scopus 로고
    • The serpin superfamily of proteinase inhibitors: Structure, function, and regulation
    • Potempa J, Korzus E, Travis J. The serpin superfamily of proteinase inhibitors: structure, function, and regulation. J Biol Chem 1994; 269: 15957-60.
    • (1994) J Biol Chem , vol.269 , pp. 15957-15960
    • Potempa, J.1    Korzus, E.2    Travis, J.3
  • 9
    • 0027925921 scopus 로고
    • Evolutionary relationships among the serpins
    • Marshall CJ. Evolutionary relationships among the serpins. Philos Trans R Soc Lond B Biol Sci 1993; 342: 101-19.
    • (1993) Philos Trans R Soc Lond B Biol Sci , vol.342 , pp. 101-119
    • Marshall, C.J.1
  • 10
    • 0024423930 scopus 로고
    • 1,-antitrypsin for structure and function of serpins
    • 1,-antitrypsin for structure and function of serpins. Biochemistry 1989; 28: 8951-66.
    • (1989) Biochemistry , vol.28 , pp. 8951-8966
    • Huber, R.1    Carrell, R.W.2
  • 11
    • 0026571516 scopus 로고
    • The latent tendencies of PAI-1
    • Sprang SR. The latent tendencies of PAI-1. Trends Biochem Sci 1992; 17: 49-50.
    • (1992) Trends Biochem Sci , vol.17 , pp. 49-50
    • Sprang, S.R.1
  • 13
  • 15
    • 0019311601 scopus 로고
    • A disulfide bond in antithrombin is required for heparin-accelerated thrombin inactivation
    • Longas MO, Ferguson WS, Finlay TH. A disulfide bond in antithrombin is required for heparin-accelerated thrombin inactivation. J Biol Chem 1980; 255: 3436-41.
    • (1980) J Biol Chem , vol.255 , pp. 3436-3441
    • Longas, M.O.1    Ferguson, W.S.2    Finlay, T.H.3
  • 16
    • 0021747157 scopus 로고
    • Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
    • Loebermann H, Tokuoka R, Deisenhofer J, Huber R. Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J Mol Biol 1984; 177: 531-56.
    • (1984) J Mol Biol , vol.177 , pp. 531-556
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, R.4
  • 18
    • 0026454541 scopus 로고
    • Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 Å resolution
    • Baumann U, Bode W, Huber R, Travis J, Potempa J. Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 Å resolution. J Mol Biol 1992; 226: 1207-18.
    • (1992) J Mol Biol , vol.226 , pp. 1207-1218
    • Baumann, U.1    Bode, W.2    Huber, R.3    Travis, J.4    Potempa, J.5
  • 19
  • 22
    • 0024430428 scopus 로고
    • Ovalbumin and angiotensinogen lack S-R confonnational change
    • Stein PE, Tewkesbury DA, Carrell RW. Ovalbumin and angiotensinogen lack S-R confonnational change. Biochem J 1989; 262: 103-7.
    • (1989) Biochem J , vol.262 , pp. 103-107
    • Stein, P.E.1    Tewkesbury, D.A.2    Carrell, R.W.3
  • 23
    • 0025936528 scopus 로고
    • Mobile reactive centre of serpins and the control of thrombosis
    • Carrell RW, Evans DL, Stein P. Mobile reactive centre of serpins and the control of thrombosis. Nature 1991; 353: 576-8.
    • (1991) Nature , vol.353 , pp. 576-578
    • Carrell, R.W.1    Evans, D.L.2    Stein, P.3
  • 24
    • 0029157233 scopus 로고
    • Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1
    • Aertgeerts K, Debondt HL, De Ranter CJ, Declerck PJ. Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1. Nature Struct Biol 1995; 2: 891-7.
    • (1995) Nature Struct Biol , vol.2 , pp. 891-897
    • Aertgeerts, K.1    Debondt, H.L.2    De Ranter, C.J.3    Declerck, P.J.4
  • 25
    • 0028359849 scopus 로고
    • Proteolytically cleaved mutant antithrombin-Hamilton has high stability to denaturation characteristic of wild type inhibitor serpins
    • Wright HT, Blajchman MA. Proteolytically cleaved mutant antithrombin-Hamilton has high stability to denaturation characteristic of wild type inhibitor serpins. FEBS Lett. 1994; 348: 14-6.
    • (1994) FEBS Lett. , vol.348 , pp. 14-16
    • Wright, H.T.1    Blajchman, M.A.2
  • 26
    • 0028937232 scopus 로고
    • Conformational studies on plasminogen activator inhibitor (PAI-1) in active, latent, substrate, and cleaved forms
    • Sancho E, Declerck PJ, Price NC, Kelly SM, Booth NA. Conformational studies on plasminogen activator inhibitor (PAI-1) in active, latent, substrate, and cleaved forms. Biochemistry 1995; 34: 1064-9.
    • (1995) Biochemistry , vol.34 , pp. 1064-1069
    • Sancho, E.1    Declerck, P.J.2    Price, N.C.3    Kelly, S.M.4    Booth, N.A.5
  • 27
    • 0029943026 scopus 로고    scopus 로고
    • Substrate behaviour of plasminogen activator inhibitor-1 is not associated with a lack of insertion of the reactive site loop
    • Gils A, Knockaert I, Declerck PJ. Substrate behaviour of plasminogen activator inhibitor-1 is not associated with a lack of insertion of the reactive site loop. Biochemistry 1996; 35: 7474-81.
    • (1996) Biochemistry , vol.35 , pp. 7474-7481
    • Gils, A.1    Knockaert, I.2    Declerck, P.J.3
  • 28
    • 0028407364 scopus 로고
    • Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop
    • Wei A, Rubin H, Cooperman BS, Christianson DW. Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop. Nature Struct Biol 1994; 1: 251-8.
    • (1994) Nature Struct Biol , vol.1 , pp. 251-258
    • Wei, A.1    Rubin, H.2    Cooperman, B.S.3    Christianson, D.W.4
  • 29
    • 0029614803 scopus 로고
    • Crystal structures of an uncleaved alpha 1-antitrypsin reveals the conformation of its inhibitory reactive loop
    • Song HK, Lee KN, Kwon KS, Yu MH, Suh SW. Crystal structures of an uncleaved alpha 1-antitrypsin reveals the conformation of its inhibitory reactive loop. FEBS Lett 1995; 377:150-4.
    • (1995) FEBS Lett , vol.377 , pp. 150-154
    • Song, H.K.1    Lee, K.N.2    Kwon, K.S.3    Yu, M.H.4    Suh, S.W.5
  • 31
    • 0028773279 scopus 로고
    • Biological implications of a 3 ̊ structure of dimeric antithrombin
    • Carrell RW, Stein PE, Fermi G, Wardell MR. Biological implications of a 3 ̊ structure of dimeric antithrombin. Structure 1994; 2: 257-70.
    • (1994) Structure , vol.2 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4
  • 33
    • 0025742788 scopus 로고
    • Serpin tertiary structure transformation
    • Stein PE, Chothia C. Serpin tertiary structure transformation. J Mol Biol , 1991; 221: 615-21.
    • (1991) J Mol Biol , vol.221 , pp. 615-621
    • Stein, P.E.1    Chothia, C.2
  • 35
    • 0029587003 scopus 로고
    • Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin family. Contribution of a covalent interaction to the binding energy of serpin-proteinase complexes
    • Olson ST, Bock PE, Kvassman J, Shore JD, Lawrence DA, Ginsburg D, Bjork I. Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin family. Contribution of a covalent interaction to the binding energy of serpin-proteinase complexes. J Biol Chem 1995; 270: 30007-17.
    • (1995) J Biol Chem , vol.270 , pp. 30007-30017
    • Olson, S.T.1    Bock, P.E.2    Kvassman, J.3    Shore, J.D.4    Lawrence, D.A.5    Ginsburg, D.6    Bjork, I.7
  • 36
    • 0023881380 scopus 로고
    • Single amino acid substitutions in the reactive site of antithrombin leading to thrombosis. Congenital substitution of arginine 393 to cysteine in antithrombin Northwick Park and to histidine in antithrombin Glasgow
    • Erdjument H, Lane DA, Panico M, Di Marzo V, Morris HR. Single amino acid substitutions in the reactive site of antithrombin leading to thrombosis. Congenital substitution of arginine 393 to cysteine in antithrombin Northwick Park and to histidine in antithrombin Glasgow. J Biol Chem 1988; 263: 5589-93.
    • (1988) J Biol Chem , vol.263 , pp. 5589-5593
    • Erdjument, H.1    Lane, D.A.2    Panico, M.3    Di Marzo, V.4    Morris, H.R.5
  • 37
    • 0024402722 scopus 로고
    • A novel amino acid substitution in the reactive site of a congenital variant antithrombin. Antithrombin Pescara. ARG393 to pro, caused by a CGT to CCT mutation
    • Lane DA, Erdjument H, Thompson E, Panico M, Di Marzo V, Morris HR, Leone G, De Stefano V, Thein SL. A novel amino acid substitution in the reactive site of a congenital variant antithrombin. Antithrombin Pescara. ARG393 to pro, caused by a CGT to CCT mutation. J Biol Chem 1989; 264: 10200-4.
    • (1989) J Biol Chem , vol.264 , pp. 10200-10204
    • Lane, D.A.1    Erdjument, H.2    Thompson, E.3    Panico, M.4    Di Marzo, V.5    Morris, H.R.6    Leone, G.7    De Stefano, V.8    Thein, S.L.9
  • 38
    • 0023885870 scopus 로고
    • Antithrombin Glasgow, 393 Arg to His: A P1 reactive site variant with increased heparin affinity but no thrombin inhibitory activity
    • Owen MC, Beresford CH, Carrell RW. Antithrombin Glasgow, 393 Arg to His: a P1 reactive site variant with increased heparin affinity but no thrombin inhibitory activity. FEBS Lett 1988; 231: 317-20.
    • (1988) FEBS Lett , vol.231 , pp. 317-320
    • Owen, M.C.1    Beresford, C.H.2    Carrell, R.W.3
  • 41
    • 0020510606 scopus 로고
    • Mutation of antitrypsin to antithrombin. Alpha 1-antitrypsin Pittsburgh (358 Met to Arg), a fatal bleeding disorder
    • Owen MC, Brennan SO, Lewis JH, Carrell RW. Mutation of antitrypsin to antithrombin. Alpha 1-antitrypsin Pittsburgh (358 Met to Arg), a fatal bleeding disorder. N Engl J Med 1983; 309: 694-8.
    • (1983) N Engl J Med , vol.309 , pp. 694-698
    • Owen, M.C.1    Brennan, S.O.2    Lewis, J.H.3    Carrell, R.W.4
  • 42
    • 0022551012 scopus 로고
    • Alpha- 1-antitrypsin-Pittsburgh. A potent inhibitor of human plasma factor XIa, kallikrein, and factor XIIf
    • Scott CF, Carrell RW, Glaser CB, Kueppers F, Lewis JH, Colman RW. Alpha-1-antitrypsin-Pittsburgh. A potent inhibitor of human plasma factor XIa, kallikrein, and factor XIIf. J Clin Invest 1986; 77: 631-4.
    • (1986) J Clin Invest , vol.77 , pp. 631-634
    • Scott, C.F.1    Carrell, R.W.2    Glaser, C.B.3    Kueppers, F.4    Lewis, J.H.5    Colman, R.W.6
  • 43
    • 0028670877 scopus 로고
    • Alpha 1, antitrypsin Pittsburgh (Met358→Arg) inhibits the contact pathway of intrinsic coagulation and alters the release of human neutrophil elastase during simulated extracorporeal circulation
    • Wachtfogel YT, Bischoff R, Bauer R, Hack CE, Nuijens JH, Kucich U, Niewiarowski S, Edmunds LH Jr, Colman RW. Alpha 1, antitrypsin Pittsburgh (Met358→Arg) inhibits the contact pathway of intrinsic coagulation and alters the release of human neutrophil elastase during simulated extracorporeal circulation. Thromb Haemost 1994; 72: 843-7.
    • (1994) Thromb Haemost , vol.72 , pp. 843-847
    • Wachtfogel, Y.T.1    Bischoff, R.2    Bauer, R.3    Hack, C.E.4    Nuijens, J.H.5    Kucich, U.6    Niewiarowski, S.7    Edmunds Jr., L.H.8    Colman, R.W.9
  • 44
    • 0022782636 scopus 로고
    • Kinetic studies on the interaction of alpha 1-proteinase inhibitor (Pittsburgh) with trypsin-like serine proteinases
    • Travis J, Matheson NR, George PM, Carrell RW. Kinetic studies on the interaction of alpha 1-proteinase inhibitor (Pittsburgh) with trypsin-like serine proteinases. Biol Chem Hoppe Seyler 1986; 367: 853-9.
    • (1986) Biol Chem Hoppe Seyler , vol.367 , pp. 853-859
    • Travis, J.1    Matheson, N.R.2    George, P.M.3    Carrell, R.W.4
  • 45
    • 0025195240 scopus 로고
    • Substitution of arginine for Leu444 in the reactive site of heparin cofactor II enhances the rate of thrombin inhibition
    • Derechin VM, Blinder MA, Tollefsen DM Substitution of arginine for Leu444 in the reactive site of heparin cofactor II enhances the rate of thrombin inhibition. J Biol Chem 1990; 265: 5623-8.
    • (1990) J Biol Chem , vol.265 , pp. 5623-5628
    • Derechin, V.M.1    Blinder, M.A.2    Tollefsen, D.M.3
  • 47
    • 0027371851 scopus 로고
    • Reaction of human chymase with reactive site variants of alpha 1-antichymotrypsin. Modulation of inhibitor versus substrate properties
    • Schechter NM, Jordan LM, James AM, Cooperman BS, Wang ZM, Rubin H. Reaction of human chymase with reactive site variants of alpha 1-antichymotrypsin. Modulation of inhibitor versus substrate properties. J Biol Chem 1993; 268: 23626-33.
    • (1993) J Biol Chem , vol.268 , pp. 23626-23633
    • Schechter, N.M.1    Jordan, L.M.2    James, A.M.3    Cooperman, B.S.4    Wang, Z.M.5    Rubin, H.6
  • 48
    • 0028180971 scopus 로고
    • Conversion of alpha 1-antichymotrypsin into a human neutrophil elastase inhibitor: Demonstration of variants with different association rate constants, stoichiometries of inhibition, and complex stabilities
    • Rubin H, Plotnick M, Wang ZM, Liu X, Zhong Q, Schechter NM, Cooperman BS. Conversion of alpha 1-antichymotrypsin into a human neutrophil elastase inhibitor: demonstration of variants with different association rate constants, stoichiometries of inhibition, and complex stabilities. Biochemistry 1994; 33: 7627-33.
    • (1994) Biochemistry , vol.33 , pp. 7627-7633
    • Rubin, H.1    Plotnick, M.2    Wang, Z.M.3    Liu, X.4    Zhong, Q.5    Schechter, N.M.6    Cooperman, B.S.7
  • 49
    • 0023821029 scopus 로고
    • Dysfunctional C1-inhibitor (At), isolated from a type II hereditary-angio-oedema plasma, contains a P1 'reactive centre' (Arg444→His) mutation
    • Aulak KS, Pemberton PA, Rosen FS, Carrell RW, Lachmann PJ, Harrison RA. Dysfunctional C1-inhibitor (At), isolated from a type II hereditary-angio-oedema plasma, contains a P1 'reactive centre' (Arg444→His) mutation. Biochem J 1988; 253: 615-8.
    • (1988) Biochem J , vol.253 , pp. 615-618
    • Aulak, K.S.1    Pemberton, P.A.2    Rosen, F.S.3    Carrell, R.W.4    Lachmann, P.J.5    Harrison, R.A.6
  • 51
    • 0028310845 scopus 로고
    • Mutagenesis of recombinant protein C inhibitor reactive site residues alters target proteinase specificity
    • Phillips JE. Cooper ST, Potter EE, Church FC. Mutagenesis of recombinant protein C inhibitor reactive site residues alters target proteinase specificity. J Biol Chem 1994; 269: 16696-700.
    • (1994) J Biol Chem , vol.269 , pp. 16696-16700
    • Phillips, J.E.1    Cooper, S.T.2    Potter, E.E.3    Church, F.C.4
  • 53
    • 0028918245 scopus 로고
    • Identification of tissue-type plasminogen activator-specific plasminogen activator inhibitor-1 mutants. Evidence that second sites of interaction contribute to target specificity
    • Sherman PM, Lawrence DA, Verhamme IM, Paielli D, Shore JD, Ginsburg D. Identification of tissue-type plasminogen activator-specific plasminogen activator inhibitor-1 mutants. Evidence that second sites of interaction contribute to target specificity. J Biol Chem 1995; 270: 9301-6.
    • (1995) J Biol Chem , vol.270 , pp. 9301-9306
    • Sherman, P.M.1    Lawrence, D.A.2    Verhamme, I.M.3    Paielli, D.4    Shore, J.D.5    Ginsburg, D.6
  • 54
    • 0025917199 scopus 로고
    • Combinatorial mutagenesis of the reactive site region in plasminogen activator inhibitor I
    • York JD, Li P, Gardell SJ. Combinatorial mutagenesis of the reactive site region in plasminogen activator inhibitor I. J Biol Chem 1991; 266: 8495-500.
    • (1991) J Biol Chem , vol.266 , pp. 8495-8500
    • York, J.D.1    Li, P.2    Gardell, S.J.3
  • 55
    • 0030973123 scopus 로고    scopus 로고
    • Proteinase specificity and functional diversity in point mutants of plasminogen activator inhibitor 1
    • Gils A, Declerck PJ. Proteinase specificity and functional diversity in point mutants of plasminogen activator inhibitor 1. J Biol Chem 1997; 272: 12662-6.
    • (1997) J Biol Chem , vol.272 , pp. 12662-12666
    • Gils, A.1    Declerck, P.J.2
  • 56
    • 0017077571 scopus 로고
    • Acceleration of the reaction between thrombin and antithrombin III by non-stoichiometric amounts of heparin
    • Björk I, Nordemnan B. Acceleration of the reaction between thrombin and antithrombin III by non-stoichiometric amounts of heparin. Eur J Biochem 1976; 68: 507-11.
    • (1976) Eur J Biochem , vol.68 , pp. 507-511
    • Björk, I.1    Nordemnan, B.2
  • 57
    • 0021363605 scopus 로고
    • Involvement of heparin chain length in the heparin-catalyzed inhibition of thrombin by antithrombin III
    • Hoylaerts M, Owen WG, Collen D. Involvement of heparin chain length in the heparin-catalyzed inhibition of thrombin by antithrombin III. J Biol Chem 1984; 259: 5670-7.
    • (1984) J Biol Chem , vol.259 , pp. 5670-5677
    • Hoylaerts, M.1    Owen, W.G.2    Collen, D.3
  • 58
    • 0026690347 scopus 로고
    • Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement
    • Olson ST, Bjork I, Sheffer R, Craig PA, Shore JD, Choay J. Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement. J Biol Chem 1992; 267: 12528-38.
    • (1992) J Biol Chem , vol.267 , pp. 12528-12538
    • Olson, S.T.1    Bjork, I.2    Sheffer, R.3    Craig, P.A.4    Shore, J.D.5    Choay, J.6
  • 59
    • 0024515421 scopus 로고
    • Transient kinetics of heparin-catalyzed protease inactivation by antithrombin III. Characterization of assembly, product formation, and heparin dissociation steps in the factor Xa reaction
    • Craig PA, Olson ST, Shore JD. Transient kinetics of heparin-catalyzed protease inactivation by antithrombin III. Characterization of assembly, product formation, and heparin dissociation steps in the factor Xa reaction. J Biol Chem. 1989; 264: 5452-61.
    • (1989) J Biol Chem , vol.264 , pp. 5452-5461
    • Craig, P.A.1    Olson, S.T.2    Shore, J.D.3
  • 60
    • 0025347305 scopus 로고
    • Alteration of serpin specificity by a protein cotactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties
    • Ehrlich HJ, Gehbink RK, Keijer J, Linders M, Preissner KT, Pannekoek H. Alteration of serpin specificity by a protein cotactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties. J Biol Chem 1990; 265: 13029-35.
    • (1990) J Biol Chem , vol.265 , pp. 13029-13035
    • Ehrlich, H.J.1    Gehbink, R.K.2    Keijer, J.3    Linders, M.4    Preissner, K.T.5    Pannekoek, H.6
  • 61
    • 0025990175 scopus 로고
    • On the target specificity of plasminogen activator inhibitor-1: The role of heparin, vitroneclin, and the reactive site
    • Keijer J, Linders M, Wegman JJ, Ehrlich HJ, Mertens K, Pannekoek H. On the target specificity of plasminogen activator inhibitor-1: the role of heparin, vitroneclin, and the reactive site. Blood 1991; 78: 1254-61.
    • (1991) Blood , vol.78 , pp. 1254-1261
    • Keijer, J.1    Linders, M.2    Wegman, J.J.3    Ehrlich, H.J.4    Mertens, K.5    Pannekoek, H.6
  • 62
    • 0028829502 scopus 로고
    • Time-resolved polarized fluorescence speclroscopy studies of plasminogen activator inhibitor type 1: Conformational changes of the reactive center upon interactions with target proteases, vitronectin and heparin
    • Fa M, Karolin J, Aleshkov S, Strandberg L, Johansson LB, Ny T. Time-resolved polarized fluorescence speclroscopy studies of plasminogen activator inhibitor type 1: conformational changes of the reactive center upon interactions with target proteases, vitronectin and heparin. Biochemistry 1995; 34: 13833-40.
    • (1995) Biochemistry , vol.34 , pp. 13833-13840
    • Fa, M.1    Karolin, J.2    Aleshkov, S.3    Strandberg, L.4    Johansson, L.B.5    Ny, T.6
  • 63
    • 0020617887 scopus 로고
    • Activation of heparin cotactor II by dermatan sulfate
    • Tollefsen DM, Pestka CA, Monafo WJ. Activation of heparin cotactor II by dermatan sulfate. J Biol Chem 1983; 258: 6713-6.
    • (1983) J Biol Chem , vol.258 , pp. 6713-6716
    • Tollefsen, D.M.1    Pestka, C.A.2    Monafo, W.J.3
  • 64
    • 0024357408 scopus 로고
    • Antithrombin activity of a peptide corresponding to residues 54-75 of heparin cofactor II
    • Hortin GL, Tollefsen DM, Benutto BM. Antithrombin activity of a peptide corresponding to residues 54-75 of heparin cofactor II. J Biol Chem 1989; 264: 13979-82.
    • (1989) J Biol Chem , vol.264 , pp. 13979-13982
    • Hortin, G.L.1    Tollefsen, D.M.2    Benutto, B.M.3
  • 65
    • 0025835147 scopus 로고
    • The reaction of thrombin with platelet-derived nexin requires a secondary recognition site in addition to the catalytic site
    • Chang AC, Detwiler TC. The reaction of thrombin with platelet-derived nexin requires a secondary recognition site in addition to the catalytic site. Biochem Biophys Res Commun 1991; 177: 1198-204.
    • (1991) Biochem Biophys Res Commun , vol.177 , pp. 1198-1204
    • Chang, A.C.1    Detwiler, T.C.2
  • 66
    • 0018101441 scopus 로고
    • On the kinetics of the reaction between human antiplasmin and plasmin
    • Wiman B, Collen D. On the kinetics of the reaction between human antiplasmin and plasmin. Eur J Biochem 1978; 84: 573-8.
    • (1978) Eur J Biochem , vol.84 , pp. 573-578
    • Wiman, B.1    Collen, D.2
  • 67
    • 0023923568 scopus 로고
    • Kinetics of the inhibition of plasminogen activators by the plasminogen-activator inhibitor. Evidence for 'second-site' interaction
    • Chmielewska J, Ranby M, Wiman B. Kinetics of the inhibition of plasminogen activators by the plasminogen-activator inhibitor. Evidence for 'second-site' interaction. Biochem J 1988; 251: 327-32.
    • (1988) Biochem J , vol.251 , pp. 327-332
    • Chmielewska, J.1    Ranby, M.2    Wiman, B.3
  • 68
    • 0023932693 scopus 로고
    • Kinetic analysis of the interaction between plasminogen activator inhibitor 1 and both urokinase and tissue type plasminogen activator
    • Hekman CM, Loskutoff DJ. Kinetic analysis of the interaction between plasminogen activator inhibitor 1 and both urokinase and tissue type plasminogen activator. Arch Biochem Biophys 1988; 262: 199-210.
    • (1988) Arch Biochem Biophys , vol.262 , pp. 199-210
    • Hekman, C.M.1    Loskutoff, D.J.2
  • 69
    • 0025227854 scopus 로고
    • Structure-function studies of the SERPIN plasminogen activator inhibitor type 1. Analysis of chimeric strained loop mutants
    • Lawrence DA, Strandberg L, Ericson J, Ny T. Structure-function studies of the SERPIN plasminogen activator inhibitor type 1. Analysis of chimeric strained loop mutants. J Biol Chem 1990; 265: 20293-301.
    • (1990) J Biol Chem , vol.265 , pp. 20293-20301
    • Lawrence, D.A.1    Strandberg, L.2    Ericson, J.3    Ny, T.4
  • 72
    • 0029875848 scopus 로고    scopus 로고
    • Sequence requirements in the reactive-center loop of plasminogen-activator inhibitor-1 for recognition of plasminogen activators
    • Tucker HM, Gerard RD. Sequence requirements in the reactive-center loop of plasminogen-activator inhibitor-1 for recognition of plasminogen activators. Eur J Biochem 1996; 237: 180-7.
    • (1996) Eur J Biochem , vol.237 , pp. 180-187
    • Tucker, H.M.1    Gerard, R.D.2
  • 73
    • 0031010046 scopus 로고    scopus 로고
    • Intrinsic specificity of the reactive site loop of alpha1-antitrypsin, alpha 1-antichymotrypsin, antithrombin III, and protease nexin I
    • Djie MZ, Stone SR, Le Bonniec BF. Intrinsic specificity of the reactive site loop of alpha1-antitrypsin, alpha 1-antichymotrypsin, antithrombin III, and protease nexin I. J Biol Chem 1997; 272: 16268-73.
    • (1997) J Biol Chem , vol.272 , pp. 16268-16273
    • Djie, M.Z.1    Stone, S.R.2    Le Bonniec, B.F.3
  • 74
    • 0029058971 scopus 로고
    • The tumor supressor maspin does not undergo the stressed to relaxed transition or inhibit trypsin-like serine proteases. Evidence that maspin is not a protease inhibitory serpin
    • Pemberton PA, Wong DT, Gibson HL, Kiefer MC, Fitzpatrick PA, Sager R, Barr PJ. The tumor supressor maspin does not undergo the stressed to relaxed transition or inhibit trypsin-like serine proteases. Evidence that maspin is not a protease inhibitory serpin. J Biol Chem 1995; 270: 15832-7.
    • (1995) J Biol Chem , vol.270 , pp. 15832-15837
    • Pemberton, P.A.1    Wong, D.T.2    Gibson, H.L.3    Kiefer, M.C.4    Fitzpatrick, P.A.5    Sager, R.6    Barr, P.J.7
  • 75
    • 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
  • 76
    • 0027633477 scopus 로고
    • The role of conformational change in serpin structure and function
    • Gettins P, Patston PA, Schapira M. The role of conformational change in serpin structure and function. Bioessays 1993; 15: 461-7.
    • (1993) Bioessays , vol.15 , pp. 461-467
    • Gettins, P.1    Patston, P.A.2    Schapira, M.3
  • 77
    • 0028168253 scopus 로고
    • Alpha 1-proteinase inhibitor variant T345R. Influence of P14 residue on substrate and inhibitory pathways
    • Hood DB, Huntington JA, Gettins PGW. Alpha 1-proteinase inhibitor variant T345R. Influence of P14 residue on substrate and inhibitory pathways. Biochemistry 1994; 33: 8538-47.
    • (1994) Biochemistry , vol.33 , pp. 8538-8547
    • Hood, D.B.1    Huntington, J.A.2    Gettins, P.G.W.3
  • 78
    • 0027945176 scopus 로고
    • Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition
    • Lawrence DA, Olson ST, Palaniappan S, Ginsburg D. Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition. J Biol Chem 1994; 269: 27657-62.
    • (1994) J Biol Chem , vol.269 , pp. 27657-27662
    • Lawrence, D.A.1    Olson, S.T.2    Palaniappan, S.3    Ginsburg, D.4
  • 80
    • 0028984723 scopus 로고
    • Trypsin complexed with alpha 1-proteinase inhibitor has an increased structural flexibility
    • Kaslik G, Patthy A, Balint M, Graf L. Trypsin complexed with alpha 1-proteinase inhibitor has an increased structural flexibility. FEBS Lett 1995; 370: 179-83.
    • (1995) FEBS Lett , vol.370 , pp. 179-183
    • Kaslik, G.1    Patthy, A.2    Balint, M.3    Graf, L.4
  • 82
    • 0028912190 scopus 로고
    • A fluorescent probe study of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism
    • Shore JD, Day DE, Francis-Chmura AM, Verhamme I, Kvassman J, Lawrence DA, Ginsburg D. A fluorescent probe study of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism. J Biol Chem 1995; 270: 5395-8.
    • (1995) J Biol Chem , vol.270 , pp. 5395-5398
    • Shore, J.D.1    Day, D.E.2    Francis-Chmura, A.M.3    Verhamme, I.4    Kvassman, J.5    Lawrence, D.A.6    Ginsburg, D.7
  • 83
    • 0029591826 scopus 로고
    • The inhibition mechanism of serpins. Evidence that the mobile reactive center loop is cleaved in the native protease-inhibitor complex
    • Wilczynska M, Fa M, Ohlsson PI, Ny T. The inhibition mechanism of serpins. Evidence that the mobile reactive center loop is cleaved in the native protease-inhibitor complex. J Biol Chem 1995; 270: 29652-5.
    • (1995) J Biol Chem , vol.270 , pp. 29652-29655
    • Wilczynska, M.1    Fa, M.2    Ohlsson, P.I.3    Ny, T.4
  • 84
    • 0018611572 scopus 로고
    • Release of a two-chain form of antithrombin from the antithrombin-thrombin complex
    • Fish WW, Bjork I. Release of a two-chain form of antithrombin from the antithrombin-thrombin complex. Eur J Biochem 1979; 101: 31-8.
    • (1979) Eur J Biochem , vol.101 , pp. 31-38
    • Fish, W.W.1    Bjork, I.2
  • 85
    • 0022389299 scopus 로고
    • Heparin and ionic strength-dependent conversion of antithrombin III from an inhibitor to a substrate of alpha-thrombin
    • Olson ST. Heparin and ionic strength-dependent conversion of antithrombin III from an inhibitor to a substrate of alpha-thrombin. J Biol Chem 1985; 260: 10153-60.
    • (1985) J Biol Chem , vol.260 , pp. 10153-10160
    • Olson, S.T.1
  • 86
    • 0025788321 scopus 로고
    • Mechanism of serpin action: Evidence that C1-inhibitor functions as a suicide substrate
    • Patston PA, Gettins P, Beechem J, Shapira M. Mechanism of serpin action: evidence that C1-inhibitor functions as a suicide substrate. Biochemistry 1991; 30: 8876-82.
    • (1991) Biochemistry , vol.30 , pp. 8876-8882
    • Patston, P.A.1    Gettins, P.2    Beechem, J.3    Shapira, M.4
  • 88
    • 0026664170 scopus 로고
    • Identification of a conformationally distinct form of plasminogen activator inhibitor-1. acting as a non-inhibitory substrate for tissue-type plasminogen activator
    • Declerck PJ, De Mol M, Vaughan DE, Collen D. Identification of a conformationally distinct form of plasminogen activator inhibitor-1. acting as a non-inhibitory substrate for tissue-type plasminogen activator. J Biol Chem 1992; 267: 11693-6.
    • (1992) J Biol Chem , vol.267 , pp. 11693-11696
    • Declerck, P.J.1    De Mol, M.2    Vaughan, D.E.3    Collen, D.4
  • 89
    • 0026471040 scopus 로고
    • A substrate-like form of plasminogen activator inhibitor type 1. Conversions between different forms by sodium dodecyl sulphate
    • Urano T, Strandberg L, Johansson LB, Ny T. A substrate-like form of plasminogen activator inhibitor type 1. Conversions between different forms by sodium dodecyl sulphate. Eur J Biochem 1992; 209: 985-92.
    • (1992) Eur J Biochem , vol.209 , pp. 985-992
    • Urano, T.1    Strandberg, L.2    Johansson, L.B.3    Ny, T.4
  • 90
    • 0027290655 scopus 로고
    • Interconversions between active, inert and substrate forms of denatured/refolded type-1 plasminogen activator inhibitor
    • Munch M, Heegaard CW, Andreasen PA. Interconversions between active, inert and substrate forms of denatured/refolded type-1 plasminogen activator inhibitor. Biochim Biophys Acta 1993; 1202: 29-37.
    • (1993) Biochim Biophys Acta , vol.1202 , pp. 29-37
    • Munch, M.1    Heegaard, C.W.2    Andreasen, P.A.3
  • 91
    • 0029828508 scopus 로고    scopus 로고
    • Conformational changes of the reactive-centre loop and ß-strand 5A accompany temperature-dependent inhibitor-substrate transition of plasminogen-activator inhibitor 1
    • Kjöller L, Martensen PM, Sottrup-Jensen L, Justesen J, Rodenburg KW, Andreasen PA. Conformational changes of the reactive-centre loop and ß-strand 5A accompany temperature-dependent inhibitor-substrate transition of plasminogen-activator inhibitor 1. Eur J Biochem 1996; 241: 38-46.
    • (1996) Eur J Biochem , vol.241 , pp. 38-46
    • Kjöller, L.1    Martensen, P.M.2    Sottrup-Jensen, L.3    Justesen, J.4    Rodenburg, K.W.5    Andreasen, P.A.6
  • 92
    • 0031850760 scopus 로고    scopus 로고
    • Modulation of plasminogen activator inhibitor 1 by Triton X-100. Identification of two consecutive conformational transitions
    • Gils A, Declerck PJ. Modulation of plasminogen activator inhibitor 1 by Triton X-100. Identification of two consecutive conformational transitions. Thromb Haemost 1998; 80: 286-91.
    • (1998) Thromb Haemost , vol.80 , pp. 286-291
    • Gils, A.1    Declerck, P.J.2
  • 94
    • 0026529071 scopus 로고
    • Conversion of antithrombin from an inhibitor of thrombin to a substrate with reduced heparin affinity and enhanced conformational stability by binding of a tetradecapeptide corresponding to the P1 to P14 region of the putative reactive bond loop of the inhibitor
    • Björk I, Ylinenjärvi K, Olson ST, Bock PE. Conversion of antithrombin from an inhibitor of thrombin to a substrate with reduced heparin affinity and enhanced conformational stability by binding of a tetradecapeptide corresponding to the P1 to P14 region of the putative reactive bond loop of the inhibitor. J Biol Chem 1992; 267: 1976-82.
    • (1992) J Biol Chem , vol.267 , pp. 1976-1982
    • Björk, I.1    Ylinenjärvi, K.2    Olson, S.T.3    Bock, P.E.4
  • 95
    • 0028832866 scopus 로고
    • The acid stabilization of plasminogen activator inhibitor-1 depends on the protonation of a single group that affects loop insertion into β-sheet A
    • Kvassman JO, Lawrence DA, Shore JD. The acid stabilization of plasminogen activator inhibitor-1 depends on the protonation of a single group that affects loop insertion into β-sheet A. J Biol Chem 1995; 270: 27942-7.
    • (1995) J Biol Chem , vol.270 , pp. 27942-27947
    • Kvassman, J.O.1    Lawrence, D.A.2    Shore, J.D.3
  • 97
    • 0024337511 scopus 로고
    • A monoclonal antibody that triggers deacylation of an intermediate thrombin-antithrombin III complex
    • Asakura S, Matsuda M, Yoshida N, Shigeharu T, Kihara H. A monoclonal antibody that triggers deacylation of an intermediate thrombin-antithrombin III complex. J Biol Chem 1989; 264: 13736-9.
    • (1989) J Biol Chem , vol.264 , pp. 13736-13739
    • Asakura, S.1    Matsuda, M.2    Yoshida, N.3    Shigeharu, T.4    Kihara, H.5
  • 98
    • 0025248027 scopus 로고
    • Hydrophobic residues 382-386 of antithrombin III, Ala-Ala-Ala-Ser-Thr, serve as the epitope for an antibody which facilitates hydrolysis of the inhibitor by thrombin
    • Asakura S, Hirata H, Okazaki H, Hashimoto Gotoh T, Matsuda M. Hydrophobic residues 382-386 of antithrombin III, Ala-Ala-Ala-Ser-Thr, serve as the epitope for an antibody which facilitates hydrolysis of the inhibitor by thrombin. J Biol Chem 1990; 265: 5135-8.
    • (1990) J Biol Chem , vol.265 , pp. 5135-5138
    • Asakura, S.1    Hirata, H.2    Okazaki, H.3    Hashimoto Gotoh, T.4    Matsuda, M.5
  • 99
    • 0031936528 scopus 로고    scopus 로고
    • Identification of a functional epitope in plasminogen activator inhibitor-1. not localized in the reactive center loop
    • Debrock S, Declerck PJ. Identification of a functional epitope in plasminogen activator inhibitor-1. not localized in the reactive center loop. Thromb Haemost 1998; 79: 597-601.
    • (1998) Thromb Haemost , vol.79 , pp. 597-601
    • Debrock, S.1    Declerck, P.J.2
  • 100
    • 0027977885 scopus 로고
    • A database of recombinant wild-type and mutant serpins
    • Patston PA, Gettins PGW. A database of recombinant wild-type and mutant serpins. Thromb Haemost 1994; 72: 166-79.
    • (1994) Thromb Haemost , vol.72 , pp. 166-179
    • Patston, P.A.1    Gettins, P.G.W.2
  • 101
    • 0029589824 scopus 로고
    • What do dysfunctional serpins tell us about molecular mobility and disease?
    • Stein PE, Carrell RW. What do dysfunctional serpins tell us about molecular mobility and disease? Nature Struct Biol 1995; 2: 96-113.
    • (1995) Nature Struct Biol , vol.2 , pp. 96-113
    • Stein, P.E.1    Carrell, R.W.2
  • 103
    • 0025866580 scopus 로고
    • Substrate properties of C1 inhibitor Ma (alanine 434-glutamic acid). Genetic and structural evidence suggesting that the P12-region contains critical determinants of serine protease inhibitor/substrate status
    • Skriver K, Wikoff WR, Patston PA, Tausk F, Schapira M, Kaplan AP, Bock SC. Substrate properties of C1 inhibitor Ma (alanine 434-glutamic acid). Genetic and structural evidence suggesting that the P12-region contains critical determinants of serine protease inhibitor/substrate status. J Biol Chem 1991; 266: 9216-21.
    • (1991) J Biol Chem , vol.266 , pp. 9216-9221
    • Skriver, K.1    Wikoff, W.R.2    Patston, P.A.3    Tausk, F.4    Schapira, M.5    Kaplan, A.P.6    Bock, S.C.7
  • 104
    • 0023716783 scopus 로고
    • Antithrombin-III-Hamilton: A gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity
    • Devraj-Kizuk R, Chui DH, Prochownik EV, Carter CJ, Ofosu FA, Blajchman MA. Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity. Blood 1988; 72: 1518-23.
    • (1988) Blood , vol.72 , pp. 1518-1523
    • Devraj-Kizuk, R.1    Chui, D.H.2    Prochownik, E.V.3    Carter, C.J.4    Ofosu, F.A.5    Blajchman, M.A.6
  • 105
    • 0024418272 scopus 로고
    • Antithrombin Cambridge, 384 Ala to Pro: A new variant identified using the polymerase chain reaction
    • Perry DJ, Harper PL, Fairham S, Daly M, Carrell RW. Antithrombin Cambridge, 384 Ala to Pro: a new variant identified using the polymerase chain reaction. FEBS Lett 1989; 254: 174-6.
    • (1989) FEBS Lett , vol.254 , pp. 174-176
    • Perry, D.J.1    Harper, P.L.2    Fairham, S.3    Daly, M.4    Carrell, R.W.5
  • 107
    • 0029317438 scopus 로고
    • Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition
    • Tucker HM, Mottonen J, Goldsmith EJ, Gerard RD. Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition. Nature Struct Biol 1995; 2: 442-5.
    • (1995) Nature Struct Biol , vol.2 , pp. 442-445
    • Tucker, H.M.1    Mottonen, J.2    Goldsmith, E.J.3    Gerard, R.D.4
  • 108
    • 0028064911 scopus 로고
    • Conversion of plasminogen activator inhibitor-1 from inhibitor to substrate by point mutations in the reactive-site loop
    • Audenaert AM, Knockaert I, Collen D, Declerck PJ. Conversion of plasminogen activator inhibitor-1 from inhibitor to substrate by point mutations in the reactive-site loop. J Biol Chem 1994; 269: 19559-64.
    • (1994) J Biol Chem , vol.269 , pp. 19559-19564
    • Audenaert, A.M.1    Knockaert, I.2    Collen, D.3    Declerck, P.J.4
  • 109
    • 0031474233 scopus 로고    scopus 로고
    • Construction and characterization of plasminogen activator inhibitor 1 mutants in which the active site loop is deleted
    • Gils A, Knockaert I, Declerck PJ. Construction and characterization of plasminogen activator inhibitor 1 mutants in which the active site loop is deleted. Fibrinolysis & Proteolysis 1997; 11: 265-71.
    • (1997) Fibrinolysis & Proteolysis , vol.11 , pp. 265-271
    • Gils, A.1    Knockaert, I.2    Declerck, P.J.3
  • 110
    • 0027136633 scopus 로고
    • Plasminogen activator inhibitor 2 (PAI-2) is a spontaneously polymerizing serpin: Biochemical characterization of the recombinant intracellular and extracellular forms
    • Mikus P, Urano T, Liljestrom P, Ny T. Plasminogen activator inhibitor 2 (PAI-2) is a spontaneously polymerizing serpin: Biochemical characterization of the recombinant intracellular and extracellular forms. Eur J Biochem 1993; 218: 1071-82.
    • (1993) Eur J Biochem , vol.218 , pp. 1071-1082
    • Mikus, P.1    Urano, T.2    Liljestrom, P.3    Ny, T.4
  • 111
    • 0028804702 scopus 로고
    • Crucial residues in the carboxy-terminal end of C1 inhibitor revealed by pathogenic mutants impaired in secretion or function
    • Verpy E, Couture-Tosi E, Eldering E, Lopez-Trascasa M, Spath P, Meo T, Tosi M Crucial residues in the carboxy-terminal end of C1 inhibitor revealed by pathogenic mutants impaired in secretion or function. J Clin Invest 1995; 95: 350-9.
    • (1995) J Clin Invest , vol.95 , pp. 350-359
    • Verpy, E.1    Couture-Tosi, E.2    Eldering, E.3    Lopez-Trascasa, M.4    Spath, P.5    Meo, T.6    Tosi, M.7
  • 112
    • 0028855465 scopus 로고
    • COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization
    • Eldering E, Verpy E, Roem D, Meo T, Tosi M. COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization. J Biol Chem 1995; 270: 2579-87.
    • (1995) J Biol Chem , vol.270 , pp. 2579-2587
    • Eldering, E.1    Verpy, E.2    Roem, D.3    Meo, T.4    Tosi, M.5
  • 113
    • 0027923966 scopus 로고
    • A hinge region mutation in C1-inhibitor (Ala436→Thr) results in nonsubstrate-like behavior and in polymerization of the molecule
    • Aulak KS, Eldering E, Hack CE, Lubbers YP, Harrison RA, Mast A, Cicardi M, Davis AE. A hinge region mutation in C1-inhibitor (Ala436→Thr) results in nonsubstrate-like behavior and in polymerization of the molecule. J Biol Chem 1993; 268: 18088-94.
    • (1993) J Biol Chem , vol.268 , pp. 18088-18094
    • Aulak, K.S.1    Eldering, E.2    Hack, C.E.3    Lubbers, Y.P.4    Harrison, R.A.5    Mast, A.6    Cicardi, M.7    Davis, A.E.8
  • 114
    • 0017163949 scopus 로고
    • Amino acid substitution Glu leads to Lys alpha 1-antitrypsin PiZ
    • Jeppsson JO. Amino acid substitution Glu leads to Lys alpha 1-antitrypsin PiZ. FEBS Lett. 1976; 65: 195-7.
    • (1976) FEBS Lett , vol.65 , pp. 195-197
    • Jeppsson, J.O.1
  • 115
    • 0027999955 scopus 로고
    • Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn→Asp)
    • Bruce D, Perry DJ, Borg JY, Carrell RW, Wardell MR. Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn→Asp). J Clin Invest 1994; 94: 2265-74.
    • (1994) J Clin Invest , vol.94 , pp. 2265-2274
    • Bruce, D.1    Perry, D.J.2    Borg, J.Y.3    Carrell, R.W.4    Wardell, M.R.5
  • 116
    • 0026755363 scopus 로고
    • The mechanism of Z alpha 1-antitrypsin accumulation in the liver
    • Lomas DA, Evans DL, Finch JT, Carrell RW. The mechanism of Z alpha 1-antitrypsin accumulation in the liver. Nature 1992; 357: 605-7.
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3    Carrell, R.W.4
  • 117
    • 0027169598 scopus 로고
    • The molecular basis of alpha 1-antichymotrypsin deficiency in a heterozygote with liver and lung disease
    • Faber JP, Poller W, Olek K, Baumann U, Carlson J, Lindmark B, Eriksson S. The molecular basis of alpha 1-antichymotrypsin deficiency in a heterozygote with liver and lung disease. J Hepatol 1993; 18: 313-21.
    • (1993) J Hepatol , vol.18 , pp. 313-321
    • Faber, J.P.1    Poller, W.2    Olek, K.3    Baumann, U.4    Carlson, J.5    Lindmark, B.6    Eriksson, S.7
  • 118
    • 0027473016 scopus 로고
    • Effect of the Z mutation on the physical and inhibitory properties of alpha 1-antitrypsin
    • Lomas DA, Evans DL, Stone SR, Chang WS, Carrell RW. Effect of the Z mutation on the physical and inhibitory properties of alpha 1-antitrypsin. Biochemistry 1993; 32: 500-8.
    • (1993) Biochemistry , vol.32 , pp. 500-508
    • Lomas, D.A.1    Evans, D.L.2    Stone, S.R.3    Chang, W.S.4    Carrell, R.W.5
  • 120
  • 121
    • 0026532063 scopus 로고
    • Conformation of the reactive site loop of J alpha 1-proteinase inhibitor probed by limited proteolysis
    • Mast AE, Enghild JJ, Salvesen G. Conformation of the reactive site loop of J alpha 1-proteinase inhibitor probed by limited proteolysis. Biochemistry 1992; 31: 2720-8.
    • (1992) Biochemistry , vol.31 , pp. 2720-2728
    • Mast, A.E.1    Enghild, J.J.2    Salvesen, G.3
  • 122
    • 0031588685 scopus 로고    scopus 로고
    • The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site
    • Skinner R, Abrahams JP, Whisstock JC, Lesk AM, Carrell RW, Wardell MR. The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site. J Mol Biol 1997; 266: 601-9.
    • (1997) J Mol Biol , vol.266 , pp. 601-609
    • Skinner, R.1    Abrahams, J.P.2    Whisstock, J.C.3    Lesk, A.M.4    Carrell, R.W.5    Wardell, M.R.6
  • 125
    • 0027945627 scopus 로고
    • Conformationai changes in serpins and the mechanism of alpha 1-antitrypsin deficiency
    • Carrell RW, Whisstock J, Lomas DA. Conformationai changes in serpins and the mechanism of alpha 1-antitrypsin deficiency. Am J Respir Crit Care Med 1994a; 150: 171-75.
    • (1994) Am J Respir Crit Care Med , vol.150 , pp. 171-175
    • Carrell, R.W.1    Whisstock, J.2    Lomas, D.A.3
  • 126
    • 0027965876 scopus 로고
    • Purification and characterization of active and stable recombinant plasminogen activator inhibitor (PAI-1) accumulated at high level in Escherichia coli
    • Sancho E, Tonge DW, Hockney RC, Booth NA. Purification and characterization of active and stable recombinant plasminogen activator inhibitor (PAI-1) accumulated at high level in Escherichia coli. Eur J Biochem 1994; 224: 125-34.
    • (1994) Eur J Biochem , vol.224 , pp. 125-134
    • Sancho, E.1    Tonge, D.W.2    Hockney, R.C.3    Booth, N.A.4
  • 127
    • 0028281746 scopus 로고
    • Engineering plasminogen activator inhibitor 1 mutants with increased functional stability
    • Lawrence DA, Olson ST, Palaniappan S, Ginsburg D. Engineering plasminogen activator inhibitor 1 mutants with increased functional stability. Biochemistry 1994; 33: 3643-8.
    • (1994) Biochemistry , vol.33 , pp. 3643-3648
    • Lawrence, D.A.1    Olson, S.T.2    Palaniappan, S.3    Ginsburg, D.4
  • 128
    • 0029022692 scopus 로고
    • Molecular evolution of plasminogen activator inhibitor-1: Functional stability
    • Berkenpas MB, Lawrence DA, Ginsburg D. Molecular evolution of plasminogen activator inhibitor-1: functional stability. EMBO J 1995; 14: 2969-77.
    • (1995) EMBO J , vol.14 , pp. 2969-2977
    • Berkenpas, M.B.1    Lawrence, D.A.2    Ginsburg, D.3
  • 129
    • 0031590321 scopus 로고    scopus 로고
    • Identification of positively charged residues contributing to the stability of plasminogen activator inhibitor 1
    • Gils A, Lu J, Aertgeerts K, Knockaert I, Declerck PJ. Identification of positively charged residues contributing to the stability of plasminogen activator inhibitor 1. Febs Lett 1997; 415: 192-5.
    • (1997) Febs Lett , vol.415 , pp. 192-195
    • Gils, A.1    Lu, J.2    Aertgeerts, K.3    Knockaert, I.4    Declerck, P.J.5
  • 130
    • 0026755995 scopus 로고
    • Elucidation of structural requirements on plasminogen activator inhibitor 1 for binding to heparin
    • Ehrlich HJ, Gebbink RK, Keijer J, Pannekoek H. Elucidation of structural requirements on plasminogen activator inhibitor 1 for binding to heparin. J Biol Chem 1992; 267; 11606-11.
    • (1992) J Biol Chem , vol.267 , pp. 11606-11611
    • Ehrlich, H.J.1    Gebbink, R.K.2    Keijer, J.3    Pannekoek, H.4
  • 131
    • 0030853308 scopus 로고    scopus 로고
    • Identification of the antithrombin III heparin binding site
    • Ersdal-Badju E, Lu A, Zuo Y, Picard V, Bock SC. Identification of the antithrombin III heparin binding site. J Biol Chem 1997; 272: 19393-400.
    • (1997) J Biol Chem , vol.272 , pp. 19393-19400
    • Ersdal-Badju, E.1    Lu, A.2    Zuo, Y.3    Picard, V.4    Bock, S.C.5
  • 133
    • 0027960551 scopus 로고
    • Role of the H helix in heparin binding to protein C inhibitor
    • Shirk RA, Elisen MG, Meijers JC, Church FC. Role of the H helix in heparin binding to protein C inhibitor. J Biol Chem 1994; 269: 28690-5.
    • (1994) J Biol Chem , vol.269 , pp. 28690-28695
    • Shirk, R.A.1    Elisen, M.G.2    Meijers, J.C.3    Church, F.C.4
  • 134
    • 0023685082 scopus 로고
    • Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma. Identification as a muitimeric form of S protein (vitronectin)
    • Declerck PJ, De Mol M, Alessi MC, Baudner S, Paques EP, Preissner KT, Muller-Berghaus G, Collen D. Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma. Identification as a muitimeric form of S protein (vitronectin). J Biol Chem 1988; 263: 15454-61.
    • (1988) J Biol Chem , vol.263 , pp. 15454-15461
    • Declerck, P.J.1    De Mol, M.2    Alessi, M.C.3    Baudner, S.4    Paques, E.P.5    Preissner, K.T.6    Muller-Berghaus, G.7    Collen, D.8
  • 135
    • 0024427263 scopus 로고
    • Stability of plasminogen activator inhibitor 1 (PAI-1)
    • Lindahl TL, Sigurdardottir O, Wiman B. Stability of plasminogen activator inhibitor 1 (PAI-1). Thromb Haemost 1989; 62: 748-51.
    • (1989) Thromb Haemost , vol.62 , pp. 748-751
    • Lindahl, T.L.1    Sigurdardottir, O.2    Wiman, B.3
  • 136
    • 0024561807 scopus 로고
    • Binding of type 1 plasminogen activator inhibitor to the extracellular matrix of cultured bovine endothelial cells
    • Mimuro J, Loskutoff DJ. Binding of type 1 plasminogen activator inhibitor to the extracellular matrix of cultured bovine endothelial cells. J Biol Chem 1989; 264: 5058-63.
    • (1989) J Biol Chem , vol.264 , pp. 5058-5063
    • Mimuro, J.1    Loskutoff, D.J.2
  • 137
    • 0027963421 scopus 로고
    • Determination of the vitronectin binding site on plasminogen activator inhibitor-1 (PAI-1)
    • van Meijer M. Klein Gebbink R, Preissner KT, Pannekoek H. Determination of the vitronectin binding site on plasminogen activator inhibitor-1 (PAI-1). FEBS Lett 1994; 352: 342-6.
    • (1994) FEBS Lett , vol.352 , pp. 342-346
    • Van Meijer, M.1    Klein Gebbink, R.2    Preissner, K.T.3    Pannekoek, H.4
  • 138
    • 0028339118 scopus 로고
    • Localization of vitronectin binding domain in plasminogen activator inhibitor-1
    • Lawrence DA, Berkenpas MB, Palaniappan S, Ginsburg D. Localization of vitronectin binding domain in plasminogen activator inhibitor-1. J Biol Chem 1994; 269: 15223-8.
    • (1994) J Biol Chem , vol.269 , pp. 15223-15228
    • Lawrence, D.A.1    Berkenpas, M.B.2    Palaniappan, S.3    Ginsburg, D.4
  • 139
    • 0029026675 scopus 로고
    • Localization of a vitronectin binding region on plasminogen activator inhibitor-1
    • Padmanabhan J, Sane DC. Localization of a vitronectin binding region on plasminogen activator inhibitor-1. Thromb Haemost 1995; 73: 829-34.
    • (1995) Thromb Haemost , vol.73 , pp. 829-834
    • Padmanabhan, J.1    Sane, D.C.2
  • 140
    • 0030942190 scopus 로고    scopus 로고
    • The composition of complexes between plasminogen activator inhibitor 1, vitronectin and either thrombin or tissue-type plasminogen activator
    • van Meijer M, Stoop A, Smilde A, Preissner KT, van Zonneveld AJ, Pannekoek H. The composition of complexes between plasminogen activator inhibitor 1, vitronectin and either thrombin or tissue-type plasminogen activator. Thromb Haemost 1997; 77: 516-21.
    • (1997) Thromb Haemost , vol.77 , pp. 516-521
    • Van Meijer, M.1    Stoop, A.2    Smilde, A.3    Preissner, K.T.4    Van Zonneveld, A.J.5    Pannekoek, H.6
  • 141
    • 0026565851 scopus 로고
    • Homology model of thyroxine binding globulin and elucidation of the thyroid binding site
    • Jarvis JA, Munro SLA, Craik DJ. Homology model of thyroxine binding globulin and elucidation of the thyroid binding site. Prot Eng 1992; 5: 61-7.
    • (1992) Prot Eng , vol.5 , pp. 61-67
    • Jarvis, J.A.1    Munro, S.L.A.2    Craik, D.J.3
  • 142
    • 0028942415 scopus 로고
    • Hormone binding site of corticosteroid binding globulin
    • Edgar P, Stein PE. Hormone binding site of corticosteroid binding globulin. Nature Struct Biol 1995; 2: 196-7.
    • (1995) Nature Struct Biol , vol.2 , pp. 196-197
    • Edgar, P.1    Stein, P.E.2
  • 143
    • 0028980988 scopus 로고
    • 1antichymotrypsin important for DNA binding. An unusual combination of DNA-binding elements
    • 1antichymotrypsin important for DNA binding. An unusual combination of DNA-binding elements. J Biol Chem 1995; 270: 14548-55.
    • (1995) J Biol Chem , vol.270 , pp. 14548-14555
    • Naidoo, N.1    Cooperman, B.S.2    Wang, Z.M.3    Liu, X.Z.4    Rubin, H.5
  • 144
    • 0019174107 scopus 로고
    • Isolation and characterization of a human plasma protein with affinity for the lysine binding sites in plasminogen. Role in the regulation of fibrinolysis and identification as histidine-rich glycoprotein
    • Lijnen HR, Hoylaerts M, Collen D. Isolation and characterization of a human plasma protein with affinity for the lysine binding sites in plasminogen. Role in the regulation of fibrinolysis and identification as histidine-rich glycoprotein. J Biol Chem 1980; 255: 10214-22.
    • (1980) J Biol Chem , vol.255 , pp. 10214-10222
    • Lijnen, H.R.1    Hoylaerts, M.2    Collen, D.3
  • 145
    • 0018774402 scopus 로고
    • On the specific interaction between the lysine-binding sites in plasmin and complementary sites in alpha2-antiplasmin and in fibrinogen
    • Wiman B, Lijnen HR, Collen D. On the specific interaction between the lysine-binding sites in plasmin and complementary sites in alpha2-antiplasmin and in fibrinogen. Biochim Biophys Acta 1979; 579: 142-54.
    • (1979) Biochim Biophys Acta , vol.579 , pp. 142-154
    • Wiman, B.1    Lijnen, H.R.2    Collen, D.3
  • 147
    • 0025130625 scopus 로고
    • Endocytosis and degradation of alpha 1-antitrypsin-protease complexes is mediated by the serpin-enzyme complex (SEC) receptor
    • Perlmutter DH, Joslin G, Nelson P, Schasteen C, Adams SP, Fallon RJ. Endocytosis and degradation of alpha 1-antitrypsin-protease complexes is mediated by the serpin-enzyme complex (SEC) receptor. J Biol Chem 1990; 265: 16713-6.
    • (1990) J Biol Chem , vol.265 , pp. 16713-16716
    • Perlmutter, D.H.1    Joslin, G.2    Nelson, P.3    Schasteen, C.4    Adams, S.P.5    Fallon, R.J.6
  • 148
    • 0028181155 scopus 로고
    • The alpha 2-macroglobulin receptor and epithelial glycoprotein-330: Two giant receptors mediating endocytosis of multiple ligands
    • Moestrup SK. The alpha 2-macroglobulin receptor and epithelial glycoprotein-330: two giant receptors mediating endocytosis of multiple ligands. Biochim Biophys Acta 1994; 1197: 197-213.
    • (1994) Biochim Biophys Acta , vol.1197 , pp. 197-213
    • Moestrup, S.K.1
  • 149
    • 0030886795 scopus 로고    scopus 로고
    • Specificity of serine proteinase/serpin complex binding to very-low-density lipoprotein receptor and alpha2-macroglobulin receptor/low-density-lipoprotein-receptor-related protein
    • Kasza A, Petersen HH, Heegaard CW, Oka K, Christensen A, Dubin A, Chan L, Andreasen PA. Specificity of serine proteinase/serpin complex binding to very-low-density lipoprotein receptor and alpha2-macroglobulin receptor/low-density-lipoprotein-receptor-related protein. Eur J Biochem 1997; 248: 270-81.
    • (1997) Eur J Biochem , vol.248 , pp. 270-281
    • Kasza, A.1    Petersen, H.H.2    Heegaard, C.W.3    Oka, K.4    Christensen, A.5    Dubin, A.6    Chan, L.7    Andreasen, P.A.8
  • 150
    • 0028603601 scopus 로고
    • Coagulation factors and their inhibitors
    • Stubbs MT, Bode W. Coagulation factors and their inhibitors. Curr Opin Struct Biol 1994; 4: 823-32.
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 823-832
    • Stubbs, M.T.1    Bode, W.2
  • 151
    • 0031962017 scopus 로고    scopus 로고
    • Binding of urokinase-type plasminogen activator plasminogen activator inhibitor-1 complex to the endocytosis receptors alpha(2)-macroglobulin receptor low-density lipoprotein receptor-related protein and very-low-density lipoprotein receptor involves basic residues in the inhibitor
    • Rodenburg KW, Kjöller L, Petersen HH, Andreasen PA. Binding of urokinase-type plasminogen activator plasminogen activator inhibitor-1 complex to the endocytosis receptors alpha(2)-macroglobulin receptor low-density lipoprotein receptor-related protein and very-low-density lipoprotein receptor involves basic residues in the inhibitor. Biochem J 1998; 329: 55-63.
    • (1998) Biochem J , vol.329 , pp. 55-63
    • Rodenburg, K.W.1    Kjöller, L.2    Petersen, H.H.3    Andreasen, P.A.4
  • 152
    • 0029050316 scopus 로고
    • Structural basis for serpin inhibitor activity
    • Wright HT, Scarsdale JN, Structural basis for serpin inhibitor activity. Proteins 1995; 22: 210-25.
    • (1995) Proteins , vol.22 , pp. 210-225
    • Wright, H.T.1    Scarsdale, J.N.2
  • 153
    • 0030983024 scopus 로고    scopus 로고
    • Rational design of complex formation between plasminogen activator inhibitor-1 and its target proteinases
    • Aertgeerts K, De Ranter CJ, Booth NA, Declerck PJ. Rational design of complex formation between plasminogen activator inhibitor-1 and its target proteinases. J Struct Biol. 1997; 118: 236-42.
    • (1997) J Struct Biol , vol.118 , pp. 236-242
    • Aertgeerts, K.1    De Ranter, C.J.2    Booth, N.A.3    Declerck, P.J.4
  • 154
    • 0031036673 scopus 로고    scopus 로고
    • Major proteinase movement upon stable serpin-proteinase complex formation
    • Stratikos E, Gettins PGW. Major proteinase movement upon stable serpin-proteinase complex formation. Proc Natl Acad Sci USA 1997; 94: 453-8.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 453-458
    • Stratikos, E.1    Gettins, P.G.W.2
  • 156
    • 0029992894 scopus 로고    scopus 로고
    • Distortion of the active site of chymotrypsin complexed with a serpin
    • Plotnick MI, Mayne L, Schlechter NM, Rubin H. Distortion of the active site of chymotrypsin complexed with a serpin. Biochemistry 1996; 35: 7586-90.
    • (1996) Biochemistry , vol.35 , pp. 7586-7590
    • Plotnick, M.I.1    Mayne, L.2    Schlechter, N.M.3    Rubin, H.4
  • 157
    • 0030888853 scopus 로고    scopus 로고
    • The serpin-proteinase complex revealed
    • Lawrence DA. The serpin-proteinase complex revealed. Nat Struct Biol 1997; 4: 339-41.
    • (1997) Nat Struct Biol , vol.4 , pp. 339-341
    • Lawrence, D.A.1
  • 159
    • 0032522374 scopus 로고    scopus 로고
    • Functional effects of single amino acid substitutions in the region of phe(113) to asp(138) in the plasminogen activator inhibitor 1 molecule
    • Sui GC, Wiman B. Functional effects of single amino acid substitutions in the region of phe(113) to asp(138) in the plasminogen activator inhibitor 1 molecule. Biochemical Journal 1998; 331 Part 2: 409-15.
    • (1998) Biochemical Journal , vol.331 , Issue.2 PART , pp. 409-415
    • Sui, G.C.1    Wiman, B.2
  • 160
    • 0032524769 scopus 로고    scopus 로고
    • Interfering with the inhibitory mechanism of serpins: Crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide
    • Xue Y, Björquist P, Inghardt T, Linschoten M, Musil D, Sjölin L, Deinum J. Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide. Structure 1998; 6: 627-36.
    • (1998) Structure , vol.6 , pp. 627-636
    • Xue, Y.1    Björquist, P.2    Inghardt, T.3    Linschoten, M.4    Musil, D.5    Sjölin, L.6    Deinum, J.7


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