메뉴 건너뛰기




Volumn 48, Issue 40, 2009, Pages 9606-9617

Nonproteolytic induction of catalytic activity into the single-chain form of urokinase-type plasminogen activator by dipeptides

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; AMINO TERMINUS; ASPARTATE RESIDUE; CATALYTIC ACTIVITY; CATALYTIC SITES; CONFORMATIONAL CHANGE; DI-PEPTIDES; DIPEPTIDE; DIRECT OBSERVATION; FLUORESCENT PROBES; HYDROPHOBIC POCKETS; ORDERS OF MAGNITUDE; OXYANION HOLE; PROTEASE COMPLEX; PROTEOLYTIC ACTIVATION; PROTEOLYTIC CLEAVAGE; SALT BRIDGES; SERINE PROTEASE; UROKINASE-TYPE PLASMINOGEN ACTIVATOR; UROKINASE-TYPE PLASMINOGEN ACTIVATOR (UPA); ZYMOGEN ACTIVATION;

EID: 70350065910     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900510f     Document Type: Article
Times cited : (10)

References (56)
  • 1
    • 0021273620 scopus 로고
    • Evolution of proteolytic enzymes
    • Neurath, H. (1984) Evolution of proteolytic enzymes. Science 224, 350-357.
    • (1984) Science , vol.224 , pp. 350-357
    • Neurath, H.1
  • 2
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • Hedstrom, L. (2002) Serine protease mechanism and specificity. Chem. Rev. 102, 4501-4524.
    • (2002) Chem. Rev. , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 3
    • 0027496219 scopus 로고
    • Converting tissue plasminogen activator to a zymogen: A regulatory triad of Asp-His-Ser
    • Madison, E. L., Kobe, A., Gething, M. J., Sambrook, J. F., and Goldsmith, E. J. (1993) Converting tissue plasminogen activator to a zymogen: A regulatory triad of Asp-His-Ser. Science 262, 419-421. (Pubitemid 23353383)
    • (1993) Science , vol.262 , Issue.5132 , pp. 419-421
    • Madison, E.L.1    Kobe, A.2    Gething, M.-J.3    Sambrook, J.F.4    Goldsmith, E.J.5
  • 4
    • 0017107996 scopus 로고
    • Induction of the bovine trypsinogen-trypsin transition by peptides sequentially similar to the N-terminus of trypsin
    • Bode, W., and Huber, R. (1976) Induction of the bovine trypsinogen-trypsin transition by peptides sequentially similar to the N-terminus of trypsin. FEBS Lett. 68, 231-236.
    • (1976) FEBS Lett. , vol.68 , pp. 231-236
    • Bode, W.1    Huber, R.2
  • 5
    • 0017893796 scopus 로고
    • The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 Å resolution
    • Bode, W., Schwager, P., and Huber, R. (1978) The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 Å resolution. J. Mol. Biol. 118, 99-112.
    • (1978) J. Mol. Biol. , vol.118 , pp. 99-112
    • Bode, W.1    Schwager, P.2    Huber, R.3
  • 6
    • 0018781771 scopus 로고
    • The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen
    • Bode, W. (1979) The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen. J. Mol. Biol. 127, 357-374.
    • (1979) J. Mol. Biol. , vol.127 , pp. 357-374
    • Bode, W.1
  • 7
    • 0021340579 scopus 로고
    • Catalytic and ligand binding properties of bovine trypsinogen and its complex with the effector dipeptide Ile-Val. A comparative study
    • Antonini, E., Ascenzi, P., Bolognesi, M., Guarneri, M., Menegatti, E., and Amiconi, G. (1984) Catalytic and ligand binding properties of bovine trypsinogen and its complex with the effector dipeptide Ile-Val. A comparative study. Mol. Cell. Biochem. 60, 163-181.
    • (1984) Mol. Cell. Biochem. , vol.60 , pp. 163-181
    • Antonini, E.1    Ascenzi, P.2    Bolognesi, M.3    Guarneri, M.4    Menegatti, E.5    Amiconi, G.6
  • 8
    • 0023660290 scopus 로고
    • Binding of the Ile-Val and Val-Val effector dipeptides to the binary adducts of bovine trypsinogen with Kunitz and Kazal inhibitors as well as the acylating agent p-nitrophenyl p-guanidinobenzoate. A thermodynamic and kinetic study
    • Ascenzi, P., Amiconi, G., Bolognesi, M., Menegatti, E., and Guarneri, M. (1987) Binding of the Ile-Val and Val-Val effector dipeptides to the binary adducts of bovine trypsinogen with Kunitz and Kazal inhibitors as well as the acylating agent p-nitrophenyl p-guanidinobenzoate. A thermodynamic and kinetic study. J. Mol. Biol. 194, 751-754.
    • (1987) J. Mol. Biol. , vol.194 , pp. 751-754
    • Ascenzi, P.1    Amiconi, G.2    Bolognesi, M.3    Menegatti, E.4    Guarneri, M.5
  • 9
    • 0028100718 scopus 로고
    • Denaturation of free and complexed bovine trypsinogen with the calcium ion, dipeptide Ile-Val and basic pancreatic trypsin inhibitor (Kunitz)
    • DOI 10.1111/j.1432-1033.1994.tb19071.x
    • Bulaj, G., and Otlewski, J. (1994) Denaturation of free and complexed bovine trypsinogen with the calcium ion, dipeptide Ile-Val and basic pancreatic trypsin inhibitor (Kunitz). Eur. J. Biochem. 223, 939-946. (Pubitemid 24263178)
    • (1994) European Journal of Biochemistry , vol.223 , Issue.3 , pp. 939-946
    • Bulaj, G.1    Otlewski, J.2
  • 10
    • 0028961339 scopus 로고
    • Ligand-induced changes in the conformational stability of bovine trypsinogen and their implications for the protein function
    • Bulaj, G., and Otlewski, J. (1995) Ligand-induced changes in the conformational stability of bovine trypsinogen and their implications for the protein function. J. Mol. Biol. 247, 701-716.
    • (1995) J. Mol. Biol. , vol.247 , pp. 701-716
    • Bulaj, G.1    Otlewski, J.2
  • 12
    • 0022405119 scopus 로고
    • Activating effect of the Ile-Val dipeptide on the catalytic properties of bovine trypsinogen
    • Menegatti, E., Guarneri, M., Bolognesi, M., Ascenzi, P., and Amiconi, G. (1985) Activating effect of the Ile-Val dipeptide on the catalytic properties of bovine trypsinogen. Biochim. Biophys. Acta 832, 1-6.
    • (1985) Biochim. Biophys. Acta , vol.832 , pp. 1-6
    • Menegatti, E.1    Guarneri, M.2    Bolognesi, M.3    Ascenzi, P.4    Amiconi, G.5
  • 14
    • 0035854772 scopus 로고    scopus 로고
    • Streptokinase triggers conformational activation of plasminogen through specific interactions of the amino-terminal sequence and stabilizes the active zymogen conformation
    • Boxrud, P. D., Verhamme, I. M., Fay, W. P., and Bock, P. E. (2001) Streptokinase triggers conformational activation of plasminogen through specific interactions of the amino-terminal sequence and stabilizes the active zymogen conformation. J. Biol. Chem. 276, 26084-26089.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26084-26089
    • Boxrud, P.D.1    Verhamme, I.M.2    Fay, W.P.3    Bock, P.E.4
  • 15
    • 0033586797 scopus 로고    scopus 로고
    • Deletion of ile1 changes the mechanism of streptokinase: Evidence for the molecular sexuality hypothesis
    • Wang, S., Reed, G. L., and Hedstrom, L. (1999) Deletion of Ile1 changes the mechanism of streptokinase: Evidence for the molecular sexuality hypothesis. Biochemistry 38, 5232-5240. (Pubitemid 129514799)
    • (1999) Biochemistry , vol.38 , Issue.16 , pp. 5232-5240
    • Wang, S.1    Reed, G.L.2    Hedstrom, L.3
  • 16
    • 4344608139 scopus 로고    scopus 로고
    • Coupling of conformational and proteolytic activation in the kinetic mechanism of plasminogen activation by streptokinase
    • Boxrud, P. D., and Bock, P. E. (2004) Coupling of conformational and proteolytic activation in the kinetic mechanism of plasminogen activation by streptokinase. J. Biol. Chem. 279, 36642-36649.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36642-36649
    • Boxrud, P.D.1    Bock, P.E.2
  • 17
    • 0034640546 scopus 로고    scopus 로고
    • Streptokinase binds to human plasmin with high affinity, perturbs the plasmin active site, and induces expression of a substrate recognition exosite for plasminogen
    • Boxrud, P. D., Fay, W. P., and Bock, P. E. (2000) Streptokinase binds to human plasmin with high affinity, perturbs the plasmin active site, and induces expression of a substrate recognition exosite for plasminogen. J. Biol. Chem. 275, 14579-14589.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14579-14589
    • Boxrud, P.D.1    Fay, W.P.2    Bock, P.E.3
  • 18
    • 4344601358 scopus 로고    scopus 로고
    • Resolution of conformational activation in the kinetic mechanism of plasminogen activation by streptokinase
    • Boxrud, P. D., Verhamme, I. M., and Bock, P. E. (2004) Resolution of conformational activation in the kinetic mechanism of plasminogen activation by streptokinase. J. Biol. Chem. 279, 36633-36641.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36633-36641
    • Boxrud, P.D.1    Verhamme, I.M.2    Bock, P.E.3
  • 19
    • 0035854772 scopus 로고    scopus 로고
    • Streptokinase triggers conformational activation of plasminogen through specific interactions of the amino-terminal sequence and stabilizes the active zymogen conformation
    • Boxrud, P. D., Verhamme, I. M., Fay, W. P., and Bock, P. E. (2001) Streptokinase triggers conformational activation of plasminogen through specific interactions of the amino-terminal sequence and stabilizes the active zymogen conformation. J. Biol. Chem. 276, 26084-26089.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26084-26089
    • Boxrud, P.D.1    Verhamme, I.M.2    Fay, W.P.3    Bock, P.E.4
  • 20
    • 0033981473 scopus 로고    scopus 로고
    • The plasminogen activation system in tumor growth, invasion, and metastasis
    • Andreasen, P. A., Egelund, R., and Petersen, H. H. (2000) The plasminogen activation system in tumor growth, invasion, and metastasis. Cell. Mol. Life Sci. 57, 25-40.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 25-40
    • Andreasen, P.A.1    Egelund, R.2    Petersen, H.H.3
  • 21
    • 0020352040 scopus 로고
    • Purification of zymogen to plasminogen activator from human glioblastoma cells by affinity chromatography with monoclonal antibody
    • Nielsen, L. S., Hansen, J. G., Skriver, L., Wilson, E. L., Kaltoft, K., Zeuthen, J., and Dano, K. (1982) Purification of zymogen to plasminogen activator from human glioblastoma cells by affinity chromatography with monoclonal antibody. Biochemistry 21, 6410-6415. (Pubitemid 13141147)
    • (1982) Biochemistry , vol.21 , Issue.25 , pp. 6410-6415
    • Nielsen, L.S.1    Hansen, J.G.2    Skriver, L.3
  • 22
    • 0020318976 scopus 로고
    • Plasminogen activator released as inactive proenzyme from murine cells transformed by sarcoma virus
    • Skriver, L., Nielsen, L. S., Stephens, R., and Dano, K. (1982) Plasminogen activator released as inactive proenzyme from murine cells transformed by sarcoma virus. Eur. J. Biochem. 124, 409-414.
    • (1982) Eur. J. Biochem. , vol.124 , pp. 409-414
    • Skriver, L.1    Nielsen, L.S.2    Stephens, R.3    Dano, K.4
  • 23
    • 0020490792 scopus 로고
    • A proenzyme form of human urokinase
    • Wun, T. C., Ossowski, L., and Reich, E. (1982) A proenzyme form of human urokinase. J. Biol. Chem. 257, 7262-7268.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7262-7268
    • Wun, T.C.1    Ossowski, L.2    Reich, E.3
  • 24
    • 0021826499 scopus 로고
    • Proenzyme to urokinase-type plasminogen activator in the mouse in vivo
    • DOI 10.1016/0014-5793(85)80350-1
    • Kielberg, V., Andreasen, P. A., Grondahl-Hansen, J., Nielsen, L. S., Skriver, L., and Dano, K. (1985) Proenzyme to urokinase-type plasminogen activator in the mouse in vivo. FEBS Lett. 182, 441-445. (Pubitemid 15074330)
    • (1985) FEBS Letters , vol.182 , Issue.2 , pp. 441-445
    • Kielberg, V.1    Andreasen, P.A.2    Grondahl-Hansen, J.3
  • 25
    • 0034711736 scopus 로고    scopus 로고
    • Plasminogen-independent initiation of the pro-urokinase activation cascade in vivo. Activation of prourokinase by glandular kallikrein (mGK-6) in plasminogen-deficient mice
    • List, K., Jensen, O. N., Bugge, T. H., Lund, L. R., Ploug, M., Dano, K., and Behrendt, N. (2000) Plasminogen-independent initiation of the pro-urokinase activation cascade in vivo. Activation of prourokinase by glandular kallikrein (mGK-6) in plasminogen-deficient mice. Biochemistry 39, 508-515.
    • (2000) Biochemistry , vol.39 , pp. 508-515
    • List, K.1    Jensen, O.N.2    Bugge, T.H.3    Lund, L.R.4    Ploug, M.5    Dano, K.6    Behrendt, N.7
  • 26
    • 33750614146 scopus 로고    scopus 로고
    • Initiation of plasminogen activation on the surface of monocytes expressing the type II transmembrane serine protease matriptase
    • DOI 10.1182/blood-2006-02-001073
    • Kilpatrick, L. M., Harris, R. L., Owen, K. A., Bass, R., Ghorayeb, C., Bar-Or, A., and Ellis, V. (2006) Initiation of plasminogen activation on the surface of monocytes expressing the type II transmembrane serine protease matriptase. Blood 108, 2616-2623. (Pubitemid 44776996)
    • (2006) Blood , vol.108 , Issue.8 , pp. 2616-2623
    • Kilpatrick, L.M.1    Harris, R.L.2    Owen, K.A.3    Bass, R.4    Ghorayeb, C.5    Bar-Or, A.6    Ellis, V.7
  • 27
    • 33750156940 scopus 로고    scopus 로고
    • Pro-urokinase-type plasminogen activator is a substrate for hepsin
    • Moran, P., Li, W., Fan, B., Vij, R., Eigenbrot, C., and Kirchhofer, D. (2006) Pro-urokinase-type plasminogen activator is a substrate for hepsin. J. Biol. Chem. 281, 30439-30446.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30439-30446
    • Moran, P.1    Li, W.2    Fan, B.3    Vij, R.4    Eigenbrot, C.5    Kirchhofer, D.6
  • 28
    • 0032542024 scopus 로고    scopus 로고
    • Activating a zymogen without proteolytic processing: Mutation of Lys15 and Asn194 activates trypsinogen
    • DOI 10.1021/bi980951d
    • Pasternak, A., Liu, X., Lin, T. Y., and Hedstrom, L. (1998) Activating a zymogen without proteolytic processing: Mutation of Lys15 and Asn194 activates trypsinogen. Biochemistry 37, 16201-16210. (Pubitemid 28536256)
    • (1998) Biochemistry , vol.37 , Issue.46 , pp. 16201-16210
    • Pasternak, A.1    Liu, X.2    Lin, T.-Y.3    Hedstrom, L.4
  • 29
    • 20444368848 scopus 로고    scopus 로고
    • Construction and Characterization of a Mutant of Single-chain Urokinase-type Plasminogen Activator Ser(175)-His(187)-mscu-PA
    • Xue, Y. M., Zhu, H., Shi, W., Liu, W., Liu, J. N., and Ma, Z. (2000) Construction and Characterization of a Mutant of Single-chain Urokinase-type Plasminogen Activator Ser(175)-His(187)-mscu-PA. Acta Biochim. Biophys. Sin. 32, 26-30.
    • (2000) Acta Biochim. Biophys. Sin. , vol.32 , pp. 26-30
    • Xue, Y.M.1    Zhu, H.2    Shi, W.3    Liu, W.4    Liu, J.N.5    Ma, Z.6
  • 30
    • 0022976041 scopus 로고
    • Plasminogen activator inhibitor from human fibrosarcoma cells binds urokinase-type plasminogen activator, but not its proenzyme
    • Andreasen, P. A., Nielsen, L. S., Kristensen, P., Grondahl-Hansen, J., Skriver, L., and Dano, K. (1986) Plasminogen activator inhibitor from human fibrosarcoma cells binds urokinase-type plasminogen activator, but not its proenzyme. J. Biol. Chem. 261, 7644-7651.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7644-7651
    • Andreasen, P.A.1    Nielsen, L.S.2    Kristensen, P.3    Grondahl-Hansen, J.4    Skriver, L.5    Dano, K.6
  • 31
    • 0037965779 scopus 로고    scopus 로고
    • The pro-urokinase plasminogen-activation system in the presence of serpin-type inhibitors and the urokinase receptor: Rescue of activity through reciprocal pro-enzyme activation
    • DOI 10.1042/BJ20021508
    • Behrendt, N., List, K., Andreasen, P. A., and Dano, K. (2003) The pro-urokinase plasminogen-activation system in the presence of serpin-type inhibitors and the urokinase receptor: Rescue of activity through reciprocal pro-enzyme activation. Biochem. J. 371, 277-287. (Pubitemid 36547610)
    • (2003) Biochemical Journal , vol.371 , Issue.2 , pp. 277-287
    • Behrendt, N.1    List, K.2    Andreasen, P.A.3    Dano, K.4
  • 32
    • 33744933988 scopus 로고    scopus 로고
    • Activity-based protein profiling implicates urokinase activation as a key step in human fibrosarcoma intravasation
    • Madsen, M. A., Deryugina, E. I., Niessen, S., Cravatt, B. F., and Quigley, J. P. (2006) Activity-based protein profiling implicates urokinase activation as a key step in human fibrosarcoma intravasation. J. Biol. Chem. 281, 15997-16005.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15997-16005
    • Madsen, M.A.1    Deryugina, E.I.2    Niessen, S.3    Cravatt, B.F.4    Quigley, J.P.5
  • 33
    • 0034832988 scopus 로고    scopus 로고
    • Localization of epitopes for monoclonal antibodies to urokinase-type plasminogen activator: Relationship between epitope localization and effects of antibodies on molecular interactions of the enzyme
    • Petersen, H. H., Hansen, M., Schousboe, S. L., and Andreasen, P. A. (2001) Localization of epitopes for monoclonal antibodies to urokinase-type plasminogen activator: Relationship between epitope localization and effects of antibodies on molecular interactions of the enzyme. Eur. J. Biochem. 268, 4430-4439.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4430-4439
    • Petersen, H.H.1    Hansen, M.2    Schousboe, S.L.3    Andreasen, P.A.4
  • 36
    • 0142095053 scopus 로고    scopus 로고
    • Mutation of the Highly Conserved Tryptophan in the Serpin Breach Region Alters the Inhibitory Mechanism of Plasminogen Activator Inhibitor-1
    • DOI 10.1021/bi034737n
    • Blouse, G. E., Perron, M. J., Kvassman, J. O., Yunus, S., Thompson, J. H., Betts, R. L., Lutter, L. C., and Shore, J. D. (2003) Mutation of the highly conserved tryptophan in the serpin breach region alters the inhibitory mechanism of plasminogen activator inhibitor-1. Biochemistry 42, 12260-12272. (Pubitemid 37296503)
    • (2003) Biochemistry , vol.42 , Issue.42 , pp. 12260-12272
    • Blouse, G.E.1    Perron, M.J.2    Kvassman, J.-O.3    Yunus, S.4    Thompson, J.H.5    Betts, R.L.6    Lutter, L.C.7    Shore, J.D.8
  • 38
    • 33644669437 scopus 로고    scopus 로고
    • A urokinase-type plasminogen activator-inhibiting cyclic peptide with an unusual P2 residue and an extended protease binding surface demonstrates new modalities for enzyme inhibition
    • Hansen, M., Wind, T., Blouse, G. E., Christensen, A., Petersen, H. H., Kjelgaard, S., Mathiasen, L., Holtet, T. L., and Andreasen, P. A. (2005) A urokinase-type plasminogen activator-inhibiting cyclic peptide with an unusual P2 residue and an extended protease binding surface demonstrates new modalities for enzyme inhibition. J. Biol. Chem. 280, 38424-38437.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38424-38437
    • Hansen, M.1    Wind, T.2    Blouse, G.E.3    Christensen, A.4    Petersen, H.H.5    Kjelgaard, S.6    Mathiasen, L.7    Holtet, T.L.8    Andreasen, P.A.9
  • 39
    • 0014404233 scopus 로고
    • Comparative studies on the inhibition of trypsin, plasmin, and thrombin by derivatives of benzylamine and benzamidine
    • Markwardt, F., Landmann, H., and Walsmann, P. (1968) Comparative studies on the inhibition of trypsin, plasmin, and thrombin by derivatives of benzylamine and benzamidine. Eur. J. Biochem. 6, 502-506.
    • (1968) Eur. J. Biochem. , vol.6 , pp. 502-506
    • Markwardt, F.1    Landmann, H.2    Walsmann, P.3
  • 40
    • 0023646314 scopus 로고
    • Amiloride selectively inhibits the urokinase-type plasminogen activator
    • Vassalli, J. D., and Belin, D. (1987) Amiloride selectively inhibits the urokinase-type plasminogen activator. FEBS Lett. 214, 187-191.
    • (1987) FEBS Lett. , vol.214 , pp. 187-191
    • Vassalli, J.D.1    Belin, D.2
  • 41
    • 34548642972 scopus 로고    scopus 로고
    • Structural basis of specificity of a peptidyl urokinase inhibitor, upain-1
    • Zhao, G., Yuan, C., Wind, T., Huang, Z., Andreasen, P. A., and Huang, M. (2007) Structural basis of specificity of a peptidyl urokinase inhibitor, upain-1. J. Struct. Biol. 160, 1-10.
    • (2007) J. Struct. Biol. , vol.160 , pp. 1-10
    • Zhao, G.1    Yuan, C.2    Wind, T.3    Huang, Z.4    Andreasen, P.A.5    Huang, M.6
  • 42
    • 0030025146 scopus 로고    scopus 로고
    • Analogs of human plasminogen that are labeled with fluorescence probes at the catalytic site of the zymogen. Preparation, characterization, and interaction with streptokinase
    • Bock, P. E., Day, D. E., Verhamme, I. M., Bernardo, M. M., Olson, S. T., and Shore, J. D. (1996) Analogs of human plasminogen that are labeled with fluorescence probes at the catalytic site of the zymogen. Preparation, characterization, and interaction with streptokinase. J. Biol. Chem. 271, 1072-1080.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1072-1080
    • Bock, P.E.1    Day, D.E.2    Verhamme, I.M.3    Bernardo, M.M.4    Olson, S.T.5    Shore, J.D.6
  • 45
    • 33746503823 scopus 로고    scopus 로고
    • Shape-shifting serpins: Advantages of a mobile mechanism
    • Huntington, J. A. (2006) Shape-shifting serpins: Advantages of a mobile mechanism. Trends Biochem. Sci. 31, 427-435.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 427-435
    • Huntington, J.A.1
  • 46
    • 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, J. D., Day, D. E., Francis-Chmura, A. M., Verhamme, I., Kvassman, J., Lawrence, D. A., and Ginsburg, D. (1995) 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. 270, 5395-5398.
    • (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
  • 47
    • 0023784931 scopus 로고
    • One-chain urokinase-type plasminogen activator from human sarcoma cells is a proenzyme with little or no intrinsic activity
    • Petersen, L. C., Lund, L. R., Nielsen, L. S., Dano, K., and Skriver, L. (1988) One-chain urokinase-type plasminogen activator from human sarcoma cells is a proenzyme with little or no intrinsic activity. J. Biol. Chem. 263, 11189-11195.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11189-11195
    • Petersen, L.C.1    Lund, L.R.2    Nielsen, L.S.3    Dano, K.4    Skriver, L.5
  • 48
    • 0022578098 scopus 로고
    • Activation of plasminogen by pro-urokinase. II. Kinetics
    • Collen, D., Zamarron, C., Lijnen, H. R., and Hoylaerts, M. (1986) Activation of plasminogen by pro-urokinase. II. Kinetics. J. Biol. Chem. 261, 1259-1266.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1259-1266
    • Collen, D.1    Zamarron, C.2    Lijnen, H.R.3    Hoylaerts, M.4
  • 49
    • 0029863066 scopus 로고    scopus 로고
    • Hydrophobic interactions control zymogen activation in the trypsin family of serine proteases
    • DOI 10.1021/bi951928k
    • Hedstrom, L., Lin, T. Y., and Fast, W. (1996) Hydrophobic interactions control zymogen activation in the trypsin family of serine proteases. Biochemistry 35, 4515-4523. (Pubitemid 26113512)
    • (1996) Biochemistry , vol.35 , Issue.14 , pp. 4515-4523
    • Hedstrom, L.1    Lin, T.-Y.2    Fast, W.3
  • 50
    • 0035692792 scopus 로고    scopus 로고
    • Serpins and other covalent protease inhibitors
    • Ye, S., and Goldsmith, E. J. (2001) Serpins and other covalent protease inhibitors. Curr. Opin. Struct. Biol. 11, 740-745.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 740-745
    • Ye, S.1    Goldsmith, E.J.2
  • 53
    • 0017639138 scopus 로고
    • Activation of factor IX by the reaction product of tissue factor and factor VII: Additional pathway for initiating blood coagulation
    • Osterud, B., and Rapaport, S. I. (1977) Activation of factor IX by the reaction product of tissue factor and factor VII: Additional pathway for initiating blood coagulation. Proc. Natl. Acad. Sci. U.S.A. 74, 5260-5264.
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 5260-5264
    • Osterud, B.1    Rapaport, S.I.2
  • 55
    • 0034616954 scopus 로고    scopus 로고
    • Protein crystallization by design: Chymotrypsinogen without precipitants
    • Pjura, P. E., Lenhoff, A. M., Leonard, S. A., and Gittis, A. G. (2000) Protein crystallization by design: Chymotrypsinogen without precipitants. J. Mol. Biol. 300, 235-239.
    • (2000) J. Mol. Biol. , vol.300 , pp. 235-239
    • Pjura, P.E.1    Lenhoff, A.M.2    Leonard, S.A.3    Gittis, A.G.4
  • 56
    • 0035976783 scopus 로고    scopus 로고
    • Crystal structure of γ-chymotrypsin in complex with 7-hydroxycoumarin
    • Ghani, U., Ng, K. K., Atta ur, R., Choudhary, M. I., Ullah, N., and James, M. N. (2001) Crystal structure of γ-chymotrypsin in complex with 7-hydroxycoumarin. J. Mol. Biol. 314, 519-525.
    • (2001) J. Mol. Biol. , vol.314 , pp. 519-525
    • Ghani, U.1    Ng, K.K.2    Atta Ur, R.3    Choudhary, M.I.4    Ullah, N.5    James, M.N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.