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Volumn 53, Issue 40, 2014, Pages 6348-6356

Fractal kinetic behavior of plasmin on the surface of fibrin meshwork

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ATOMIC FORCE MICROSCOPY; ENZYMES; FRACTALS; IMAGING TECHNIQUES; INTERFACES (MATERIALS); MATHEMATICAL MODELS;

EID: 84908032479     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500661m     Document Type: Article
Times cited : (12)

References (30)
  • 4
    • 0034022885 scopus 로고    scopus 로고
    • Influence of fibrin network conformation and fibrin fiber diameter on fibrinolysis speed: Dynamic and structural approaches by confocal microscopy
    • Collet, J. P., Park, D., Lesty, C., Soria, J., Soria, C., Montalescot, G., and Weisel, J. W. (2000) Influence of fibrin network conformation and fibrin fiber diameter on fibrinolysis speed: dynamic and structural approaches by confocal microscopy Arterioscler. Thromb. Vasc. Biol. 20, 1354-1361
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 1354-1361
    • Collet, J.P.1    Park, D.2    Lesty, C.3    Soria, J.4    Soria, C.5    Montalescot, G.6    Weisel, J.W.7
  • 5
    • 78751560568 scopus 로고    scopus 로고
    • The interplay between tissue plasminogen activator domains and fibrin structures in the regulation of fibrinolysis: Kinetic and microscopic studies
    • Longstaff, C., Thelwell, C., Williams, S. C., Silva, M. M., Szabó, L., and Kolev, K. (2011) The interplay between tissue plasminogen activator domains and fibrin structures in the regulation of fibrinolysis: kinetic and microscopic studies Blood 117, 661-668
    • (2011) Blood , vol.117 , pp. 661-668
    • Longstaff, C.1    Thelwell, C.2    Williams, S.C.3    Silva, M.M.4    Szabó, L.5    Kolev, K.6
  • 6
    • 79960618940 scopus 로고    scopus 로고
    • Historical perspective and future direction of thrombolysis research: The re-discovery of plasmin
    • Marder, V. J. (2011) Historical perspective and future direction of thrombolysis research: the re-discovery of plasmin J. Thromb. Haemost. 9 (S1) 364-373
    • (2011) J. Thromb. Haemost. , vol.9 , Issue.S1 , pp. 364-373
    • Marder, V.J.1
  • 7
    • 0030997702 scopus 로고    scopus 로고
    • Functional evaluation of the structural features of proteases and their substrate in fibrin surface degradation
    • Kolev, K., Tenekedjiev, K., Komorowicz, E., and Machovich, R. (1997) Functional evaluation of the structural features of proteases and their substrate in fibrin surface degradation J. Biol. Chem. 272, 13666-13675
    • (1997) J. Biol. Chem. , vol.272 , pp. 13666-13675
    • Kolev, K.1    Tenekedjiev, K.2    Komorowicz, E.3    Machovich, R.4
  • 8
    • 0027141112 scopus 로고
    • Inner clot diffusion and permeation during fibrinolysis
    • Diamond, S. L. and Anand, S. (1993) Inner clot diffusion and permeation during fibrinolysis Biophys. J. 65, 2622-2643
    • (1993) Biophys. J. , vol.65 , pp. 2622-2643
    • Diamond, S.L.1    Anand, S.2
  • 9
    • 0029056293 scopus 로고
    • Enzyme-mediated proteolysis of fibrous biopolymers: Dissolution front movement in fibrin or collagen under conditions of diffusive or convective transport
    • Anand, S., Wu, J. H., and Diamond, S. L. (1995) Enzyme-mediated proteolysis of fibrous biopolymers: Dissolution front movement in fibrin or collagen under conditions of diffusive or convective transport Biotechnol. Bioeng. 48, 89-107
    • (1995) Biotechnol. Bioeng. , vol.48 , pp. 89-107
    • Anand, S.1    Wu, J.H.2    Diamond, S.L.3
  • 10
    • 0037083201 scopus 로고    scopus 로고
    • An experimental and theoretical study on the dissolution of mural fibrin clots by tissue-type plasminogen activator
    • Wootton, D. M., Popel, A. S., and Alevriadou, B. R. (2002) An experimental and theoretical study on the dissolution of mural fibrin clots by tissue-type plasminogen activator Biotechnol. Bioeng. 77, 405-419
    • (2002) Biotechnol. Bioeng. , vol.77 , pp. 405-419
    • Wootton, D.M.1    Popel, A.S.2    Alevriadou, B.R.3
  • 11
    • 0017910967 scopus 로고
    • Size and density of fibrin fibers from turbidity
    • Carr, M. E., Jr. and Hermans, J. (1978) Size and density of fibrin fibers from turbidity Macromolecules 11, 46-50
    • (1978) Macromolecules , vol.11 , pp. 46-50
    • Carr, M.E.1    Hermans, J.2
  • 12
    • 0023000367 scopus 로고
    • Concentration of protein in fibrin fibers and fibrinogen polymers determined by refractive index matching
    • Voter, W. A., Lucaveche, C., and Erickson, H. P. (1986) Concentration of protein in fibrin fibers and fibrinogen polymers determined by refractive index matching Biopolymers 25, 2375-2384
    • (1986) Biopolymers , vol.25 , pp. 2375-2384
    • Voter, W.A.1    Lucaveche, C.2    Erickson, H.P.3
  • 13
    • 48249124302 scopus 로고    scopus 로고
    • Crowding effects on diffusion in solutions and cells
    • Dix, J. A. and Verkman, A. S. (2008) Crowding effects on diffusion in solutions and cells Annu. Rev. Biophys. 37, 247-263
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 247-263
    • Dix, J.A.1    Verkman, A.S.2
  • 14
    • 84881527585 scopus 로고    scopus 로고
    • Diffusion in the extracellular space in brain and tumors
    • Verkman, A. S. (2013) Diffusion in the extracellular space in brain and tumors Phys. Biol. 10, 045003
    • (2013) Phys. Biol. , vol.10 , pp. 045003
    • Verkman, A.S.1
  • 16
    • 84897585583 scopus 로고    scopus 로고
    • Modelling fibrinolysis: A 3D stochastic multiscale model
    • Bannish, B. E., Keener, J. P., and Fogelson, A. L. (2014) Modelling fibrinolysis: a 3D stochastic multiscale model Math. Med. Biol. 31, 17-44
    • (2014) Math. Med. Biol. , vol.31 , pp. 17-44
    • Bannish, B.E.1    Keener, J.P.2    Fogelson, A.L.3
  • 17
    • 84890845081 scopus 로고    scopus 로고
    • Enzyme kinetics, past and present
    • Xie, X. S. (2013) Enzyme kinetics, past and present Science 342, 1457-1459
    • (2013) Science , vol.342 , pp. 1457-1459
    • Xie, X.S.1
  • 18
    • 33744544180 scopus 로고
    • Fractal reaction kinetics
    • Kopelman, R. (1988) Fractal reaction kinetics Science 241, 1620-1626
    • (1988) Science , vol.241 , pp. 1620-1626
    • Kopelman, R.1
  • 19
    • 84883051895 scopus 로고    scopus 로고
    • The origins of enzyme kinetics
    • Cornish-Bowden, A. (2013) The origins of enzyme kinetics FEBS Lett. 587, 2725-2730
    • (2013) FEBS Lett. , vol.587 , pp. 2725-2730
    • Cornish-Bowden, A.1
  • 20
    • 4444296429 scopus 로고    scopus 로고
    • Michaelis-Menten kinetics under spatially constrained conditions: Application to mibefradil pharmacokinetics
    • Kosmidis, K., Karalis, V., Argyrakis, P., and Macheras, P. (2004) Michaelis-Menten kinetics under spatially constrained conditions: application to mibefradil pharmacokinetics Biophys. J. 87, 1498-1506
    • (2004) Biophys. J. , vol.87 , pp. 1498-1506
    • Kosmidis, K.1    Karalis, V.2    Argyrakis, P.3    Macheras, P.4
  • 21
    • 0028360109 scopus 로고
    • Regulation of fibrinolytic activity of neutrophil leukocyte elastase, plasmin, and miniplasmin by plasma protease inhibitors
    • Kolev, K., Léránt, I., Tenekejiev, K., and Machovich, R. (1994) Regulation of fibrinolytic activity of neutrophil leukocyte elastase, plasmin, and miniplasmin by plasma protease inhibitors J. Biol. Chem. 269, 17030-17034
    • (1994) J. Biol. Chem. , vol.269 , pp. 17030-17034
    • Kolev, K.1    Léránt, I.2    Tenekejiev, K.3    Machovich, R.4
  • 23
    • 0027211110 scopus 로고
    • An international collaborative study to investigate standardisation of hirudin potency
    • Longstaff, C., Wong, M. Y., and Gaffney, P. J. (1993) An international collaborative study to investigate standardisation of hirudin potency Thromb. Haemost. 69, 430-435
    • (1993) Thromb. Haemost. , vol.69 , pp. 430-435
    • Longstaff, C.1    Wong, M.Y.2    Gaffney, P.J.3
  • 24
    • 29344462779 scopus 로고    scopus 로고
    • New application of air-drying techniques for studying Ephemeroptera and Plecoptera eggs by scanning electron microscopy
    • Ubero-Pascal, N., Fortuño, J. M., and de Los Angeles, P. M. (2005) New application of air-drying techniques for studying Ephemeroptera and Plecoptera eggs by scanning electron microscopy Microsc. Res. Technol. 68, 264-271
    • (2005) Microsc. Res. Technol. , vol.68 , pp. 264-271
    • Ubero-Pascal, N.1    Fortuño, J.M.2    De Los Angeles, P.M.3
  • 25
    • 48749103309 scopus 로고    scopus 로고
    • Immunological identification of fibrinogen in dual-component protein films by AFM imaging
    • Soman, P., Rice, Z., and Siedlecki, C. A. (2008) Immunological identification of fibrinogen in dual-component protein films by AFM imaging Micron 39, 832-842
    • (2008) Micron , vol.39 , pp. 832-842
    • Soman, P.1    Rice, Z.2    Siedlecki, C.A.3
  • 26
    • 13444262175 scopus 로고    scopus 로고
    • Adhesion mode atomic force microscopy study of dual component protein films
    • Agnihotri, A. and Siedlecki, C. A. (2005) Adhesion mode atomic force microscopy study of dual component protein films Ultramicroscopy 102, 257-268
    • (2005) Ultramicroscopy , vol.102 , pp. 257-268
    • Agnihotri, A.1    Siedlecki, C.A.2
  • 27
    • 84883054120 scopus 로고    scopus 로고
    • A generic rate law for surface-active enzymes
    • Kartal, O. and Ebenhöh, O. (2013) A generic rate law for surface-active enzymes FEBS Lett. 587, 2882-2890
    • (2013) FEBS Lett. , vol.587 , pp. 2882-2890
    • Kartal, O.1    Ebenhöh, O.2
  • 28
    • 0032718245 scopus 로고    scopus 로고
    • Structural studies of fibrinolysis by electron and light microscopy
    • Weisel, J. W., Veklich, Y., Collet, J. P., and Francis, C. W. (1999) Structural studies of fibrinolysis by electron and light microscopy Thromb. Haemost. 82, 277-282
    • (1999) Thromb. Haemost. , vol.82 , pp. 277-282
    • Weisel, J.W.1    Veklich, Y.2    Collet, J.P.3    Francis, C.W.4
  • 30
    • 0037340432 scopus 로고    scopus 로고
    • Molecular mechanisms of initiation of fibrinolysis by fibrin
    • Medved, L. and Nieuwenhuizen, W. (2003) Molecular mechanisms of initiation of fibrinolysis by fibrin Thromb. Haemost. 89, 409-419
    • (2003) Thromb. Haemost. , vol.89 , pp. 409-419
    • Medved, L.1    Nieuwenhuizen, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.