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Volumn 116, Issue 3, 2005, Pages 265-271

Inhibition of thrombin activatable fibrinolysis inhibitor by cysteine derivatives

Author keywords

Fibrinolysis; TAFI; Thrombosis

Indexed keywords

CYSTEINE DERIVATIVE; GLYCYLCYSTEINE; GLYCYLGLYCYLCYSTEINE; GUANIDINYLCYSTEINE; THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR; UNCLASSIFIED DRUG;

EID: 20144381372     PISSN: 00493848     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.thromres.2004.12.023     Document Type: Article
Times cited : (11)

References (27)
  • 1
    • 0029044322 scopus 로고
    • Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor
    • L. Bajzar, R. Manuel, and M.E. Nesheim Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor J. Biol. Chem. 270 24 1995 14477 14484
    • (1995) J. Biol. Chem. , vol.270 , Issue.24 , pp. 14477-14484
    • Bajzar, L.1    Manuel, R.2    Nesheim, M.E.3
  • 2
    • 0032579276 scopus 로고    scopus 로고
    • Both cellular and soluble forms of thrombomodulin inhibit fibrinolysis by potentiating the activation of thrombin-activable fibrinolysis inhibitor
    • L. Bajzar, M. Nesheim, J. Morser, and P.B. Tracy Both cellular and soluble forms of thrombomodulin inhibit fibrinolysis by potentiating the activation of thrombin-activable fibrinolysis inhibitor J. Biol. Chem. 273 5 1998 2792 2798
    • (1998) J. Biol. Chem. , vol.273 , Issue.5 , pp. 2792-2798
    • Bajzar, L.1    Nesheim, M.2    Morser, J.3    Tracy, P.B.4
  • 3
    • 0032538557 scopus 로고    scopus 로고
    • A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activable fibrinolysis inhibitor
    • W. Wang, M.B. Boffa, L. Bajzar, J.B. Walker, and M.E. Nesheim A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activable fibrinolysis inhibitor J. Biol. Chem. 273 42 1998 27176 27181
    • (1998) J. Biol. Chem. , vol.273 , Issue.42 , pp. 27176-27181
    • Wang, W.1    Boffa, M.B.2    Bajzar, L.3    Walker, J.B.4    Nesheim, M.E.5
  • 4
    • 10544253848 scopus 로고    scopus 로고
    • Coagulation-dependent inhibition of fibrinolysis: Role of carboxypeptidase-U and the premature lysis of clots from hemophilic plasma
    • G.J. Broze, and D. Higuchi Coagulation-dependent inhibition of fibrinolysis: role of carboxypeptidase-U and the premature lysis of clots from hemophilic plasma Blood 88 10 1996 3815 3823
    • (1996) Blood , vol.88 , Issue.10 , pp. 3815-3823
    • Broze, G.J.1    Higuchi, D.2
  • 5
    • 0033825322 scopus 로고    scopus 로고
    • Consequences of inhibition of plasma carboxypeptidase B on in vivo thrombolysis, thrombosis and hemostasis
    • C.J. Refino, L. De Guzman, D. Schmitt, R. Smyth, S. Jeet, and M.T. Lipari Consequences of inhibition of plasma carboxypeptidase B on in vivo thrombolysis, thrombosis and hemostasis Fibrinolysis Proteolysis 14 5 2000 305 314
    • (2000) Fibrinolysis Proteolysis , vol.14 , Issue.5 , pp. 305-314
    • Refino, C.J.1    De Guzman, L.2    Schmitt, D.3    Smyth, R.4    Jeet, S.5    Lipari, M.T.6
  • 6
    • 0034192129 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis
    • N.H. van Tilburg, F.R. Rosendaal, and R.M. Bertina Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis Blood 95 9 2000 2855 2859
    • (2000) Blood , vol.95 , Issue.9 , pp. 2855-2859
    • Van Tilburg, N.H.1    Rosendaal, F.R.2    Bertina, R.M.3
  • 7
    • 0038299177 scopus 로고    scopus 로고
    • Association between thrombin-activatable fibrinolysis inhibitor (TAFI) and clinical outcome in patients with unstable angina pectoris
    • G.J. Brouwers, F.W. Leebeek, M.W. Tanck, J. Wouter Jukema, C. Kluft, and M.P. de Maat Association between thrombin-activatable fibrinolysis inhibitor (TAFI) and clinical outcome in patients with unstable angina pectoris Thromb. Haemost. 90 2003 92 100
    • (2003) Thromb. Haemost. , vol.90 , pp. 92-100
    • Brouwers, G.J.1    Leebeek, F.W.2    Tanck, M.W.3    Wouter Jukema, J.4    Kluft, C.5    De Maat, M.P.6
  • 8
    • 0037383184 scopus 로고    scopus 로고
    • Thrombin-activable fibrinolysis inhibitor levels in the acute phase of ischemic stroke
    • J. Montaner, M. Ribo, J. Monasterio, C.A. Molina, and J. Alvarez-Sabin Thrombin-activable fibrinolysis inhibitor levels in the acute phase of ischemic stroke Stroke 34 4 2003 1038 1040
    • (2003) Stroke , vol.34 , Issue.4 , pp. 1038-1040
    • Montaner, J.1    Ribo, M.2    Monasterio, J.3    Molina, C.A.4    Alvarez-Sabin, J.5
  • 9
    • 0036172375 scopus 로고    scopus 로고
    • Insulin resistance is associated with increased circulating level of thrombin-activatable fibrinolysis inhibitor in Type 2 diabetic patients
    • Y. Hori, E.C. Gabazza, Y. Yano, A. Katsuki, K. Suzuki, and Y. Adachi Insulin resistance is associated with increased circulating level of thrombin-activatable fibrinolysis inhibitor in Type 2 diabetic patients J. Clin. Endocrinol. Metab. 87 2 2002 660 665
    • (2002) J. Clin. Endocrinol. Metab. , vol.87 , Issue.2 , pp. 660-665
    • Hori, Y.1    Gabazza, E.C.2    Yano, Y.3    Katsuki, A.4    Suzuki, K.5    Adachi, Y.6
  • 10
    • 0025748556 scopus 로고
    • Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma
    • D. Eaton, B. Malloy, S. Tsai, W. Henzel, and D. Drayna Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma J. Biol. Chem. 266 32 1991 21833 21838
    • (1991) J. Biol. Chem. , vol.266 , Issue.32 , pp. 21833-21838
    • Eaton, D.1    Malloy, B.2    Tsai, S.3    Henzel, W.4    Drayna, D.5
  • 11
    • 0036384505 scopus 로고    scopus 로고
    • Human procarboxypeptidase B: Three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (TAFI)
    • P.J. Barbosa Pereira, S. Segura-Martin, B. Oliva, C. Ferrer-Orta, F.X. Aviles, and M. Coll Human procarboxypeptidase B: three-dimensional structure and implications for thrombin-activatable fibrinolysis inhibitor (TAFI) J. Mol. Biol. 321 2002 537 547
    • (2002) J. Mol. Biol. , vol.321 , pp. 537-547
    • Barbosa Pereira, P.J.1    Segura-Martin, S.2    Oliva, B.3    Ferrer-Orta, C.4    Aviles, F.X.5    Coll, M.6
  • 12
    • 0037436061 scopus 로고    scopus 로고
    • Carboxypeptidase B inhibitors reduce tissue factor-induced renal microthrombi in rats
    • Y. Muto, K. Suzuki, E. Sato, and H. Ishii Carboxypeptidase B inhibitors reduce tissue factor-induced renal microthrombi in rats Eur. J. Pharmacol. 461 2-3 2003 181 189
    • (2003) Eur. J. Pharmacol. , vol.461 , Issue.2-3 , pp. 181-189
    • Muto, Y.1    Suzuki, K.2    Sato, E.3    Ishii, H.4
  • 13
    • 10744221306 scopus 로고    scopus 로고
    • Design and synthesis of potent, orally active, inhibitors of carboxypeptidase U (TAFIa)
    • M.O. Polla, L. Tottie, C. Norden, M. Linschoten, D. Musil, and Trumpp-Kallmeyer Design and synthesis of potent, orally active, inhibitors of carboxypeptidase U (TAFIa) Bioorg. Med. Chem. 12 5 2004 1151 1175
    • (2004) Bioorg. Med. Chem. , vol.12 , Issue.5 , pp. 1151-1175
    • Polla, M.O.1    Tottie, L.2    Norden, C.3    Linschoten, M.4    Musil, D.5    Trumpp-Kallmeyer6
  • 14
    • 10744228937 scopus 로고    scopus 로고
    • Synthesis and evaluation of imidazole acetic acid inhibitors of activated thrombin-activatable fibrinolysis inhibitor as novel antithrombotics
    • J.C. Barrow, P.G. Nantermet, S.R. Stauffer, P.L. Ngo, M.A. Steinbeiser, and S.S. Mao Synthesis and evaluation of imidazole acetic acid inhibitors of activated thrombin-activatable fibrinolysis inhibitor as novel antithrombotics J. Med. Chem. 46 2003 5294 5297
    • (2003) J. Med. Chem. , vol.46 , pp. 5294-5297
    • Barrow, J.C.1    Nantermet, P.G.2    Stauffer, S.R.3    Ngo, P.L.4    Steinbeiser, M.A.5    Mao, S.S.6
  • 15
    • 0017825437 scopus 로고
    • Human plasma carboxypeptidase N. Isolation and characterization
    • T.H. Plummer Jr., and M.Y. Hurwitz Human plasma carboxypeptidase N. Isolation and characterization J. Biol. Chem. 253 11 1978 3907 3912
    • (1978) J. Biol. Chem. , vol.253 , Issue.11 , pp. 3907-3912
    • Plummer Jr., T.H.1    Hurwitz, M.Y.2
  • 16
    • 0029060126 scopus 로고
    • Human carboxypeptidase N: Lysine carboxypeptidase
    • R. Skidgel Human carboxypeptidase N: lysine carboxypeptidase Methods Enzymol. 248 1995 653 663
    • (1995) Methods Enzymol. , vol.248 , pp. 653-663
    • Skidgel, R.1
  • 17
    • 0037447246 scopus 로고    scopus 로고
    • Engineering the proteolytic specificity of activated protein C improves its pharmacological properties
    • D.T. Berg, B. Gerlitz, J. Shang, T. Smith, P. Santa, and M.A. Richardson Engineering the proteolytic specificity of activated protein C improves its pharmacological properties Proc. Natl. Acad. Sci. 100 8 2003 4423 4428
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , Issue.8 , pp. 4423-4428
    • Berg, D.T.1    Gerlitz, B.2    Shang, J.3    Smith, T.4    Santa, P.5    Richardson, M.A.6
  • 18
    • 0015327378 scopus 로고
    • A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors
    • P. Henderson A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors Biochem. J. 127 1972 321 333
    • (1972) Biochem. J. , vol.127 , pp. 321-333
    • Henderson, P.1
  • 19
    • 0019159842 scopus 로고
    • An improved spectrophotometric assay for human plasma carboxypeptidase N1
    • T.H. Plummer Jr., and M.T. Kimmel An improved spectrophotometric assay for human plasma carboxypeptidase N1 Anal. Biochem. 108 1980 348 353
    • (1980) Anal. Biochem. , vol.108 , pp. 348-353
    • Plummer Jr., T.H.1    Kimmel, M.T.2
  • 20
    • 0020460249 scopus 로고
    • A unique activity assay for carboxypeptidase a in human serum
    • L.M. Peterson, B. Holmquist, and J.L. Bethune A unique activity assay for carboxypeptidase A in human serum Anal. Biochem. 125 1982 420 426
    • (1982) Anal. Biochem. , vol.125 , pp. 420-426
    • Peterson, L.M.1    Holmquist, B.2    Bethune, J.L.3
  • 22
    • 0034702768 scopus 로고    scopus 로고
    • Crystal structure of carboxypeptidase a complexed with d-cysteine at 1.75 A-inhibitor-induced conformational changes
    • D.M.F. van Aalten, C.R. Chong, and L. Joshua-Tor Crystal structure of carboxypeptidase A complexed with d-cysteine at 1.75 A-inhibitor-induced conformational changes Biochemistry 39 2000 10082 10089
    • (2000) Biochemistry , vol.39 , pp. 10082-10089
    • Van Aalten, D.M.F.1    Chong, C.R.2    Joshua-Tor, L.3
  • 23
    • 20144366990 scopus 로고    scopus 로고
    • Accelrys Inc., San C.A. Diego, 92121.
    • QUANTA. p. version 98.1111, Accelrys Inc., San C.A. Diego, 92121.
    • QUANTA. P. Version 98.1111
  • 24
    • 20144376002 scopus 로고    scopus 로고
    • CHARMM, v., Accelrys Inc., San C.A. Diego, 92121.
    • CHARMM, v., Accelrys Inc., San C.A. Diego, 92121.
  • 27
    • 20144383021 scopus 로고    scopus 로고
    • Design of peptide-based inhibitors of thrombin activated fibrinolysis inhibitor (TAFI)
    • New York, N.Y., United States 2003 (September 7-11) MEDI-086
    • D.W.D. Beight, Y.H. Do, D. Gifford-Moore, R.W. Harper, V.J. Klimkowski, and D. Lu Design of peptide-based inhibitors of thrombin activated fibrinolysis inhibitor (TAFI) 226th ACS National Meeting, New York, N.Y., United States 2003 (September 7-11) MEDI-086
    • (2003) 226th ACS National Meeting , pp. 086
    • Beight, D.W.D.1    Do, Y.H.2    Gifford-Moore, D.3    Harper, R.W.4    Klimkowski, V.J.5    Lu, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.