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References

  • 1
    Kolev K, Longstaff C, Machovich R. Fibrinolysis at the fluid-solid interface of thrombi. Curr Med Chem Cardiovasc Hematol Agents 2005; 3: 34155.
  • 2
    Weisel JW, Litvinov RI. The biochemical and physical process of fibrinolysis and effects of clot structure and stability on the lysis rate. Cardiovasc Hematol Agents Med Chem 2008; 6: 16180.
  • 3
    Collet JP, Montalescot G, Lesty C, Weisel JW. A structural and dynamic investigation of the facilitating effect of glycoprotein IIb/IIIa inhibitors in dissolving platelet-rich clots. Circ Res 2002; 90: 42834.
  • 4
    Collet JP, Allali Y, Lesty C, Tanguy ML, Silvain J, Ankri A, Blanchet B, Dumaine R, Gianetti J, Payot L, Weisel JW, Montalescot G. Altered fibrin architecture is associated with hypofibrinolysis and premature coronary atherothrombosis. Arterioscler Thromb Vasc Biol 2006; 26: 256773.
  • 5
    Undas A, Zalewski J, Krochin M, Siudak Z, Sadowski M, Pregowski J, Dudek D, Janion M, Witkowski A, Zmudka K. Altered plasma fibrin clot properties are associated with in-stent thrombosis. Arterioscler Thromb Vasc Biol 2010; 30: 27682.
  • 6
    Brown AE, Litvinov RI, Discher DE, Purohit PK, Weisel JW. Multiscale mechanics of fibrin polymer: gel stretching with protein unfolding and loss of water. Science 2009; 325: 7414.
  • 7
    Eskin SG, McIntire LV. Rheology of thrombosis. In: Colman RW, Marder VJ, Clowes AW, George JN, Goldhaber SZ, eds. Hemostasis and Thrombosis: Basic Principles and Clinical Practice, 5th edn. Philadelphia: Lippincott Williams & Wilkins, 2006: 73750.
  • 8
    Lundblad RL, Kingdon HS, Mann KG. Thrombin. Meth Enzymol 1976; 45: 15676.
  • 9
    Thelwell C, Longstaff C. The regulation by fibrinogen and fibrin of tissue plasminogen activator kinetics and inhibition by plasminogen activator inhibitor 1. J Thromb Haemost 2007; 5: 80411.
  • 10
    Longstaff C, Thelwell C, Williams S, Silva MMCG, Szabó L, Kolev K. The interplay between tissue plasminogen activator domains and fibrin structures in the regulation of fibrinolysis: kinetic and microscopic studies. Blood 2011; 117: 6618.
  • 11
    Deutsch DG, Mertz ET. Plasminogen: purification from human plasma by affinity chromatography. Science 1970; 170: 10956.
  • 12
    Kolev K, Léránt I, Tenekejiev K, Machovich R. Regulation of fibrinolytic activity of neutrophil leukocyte elastase, plasmin, and miniplasmin by plasma protease inhibitors. J Biol Chem 1994; 269: 170304.
  • 13
    Tanka-Salamon A, Tenekedjiev K, Machovich R, Kolev K. Suppressed catalytic efficiency of plasmin in the presence of long-chain fatty acids. Identification of kinetic parameters from continuous enzymatic assay with Monte Carlo simulation. FEBS J 2008; 275: 127482.
  • 14
    Komorowicz E, Kolev K, Machovich R. Fibrinolysis with des-kringle derivatives of plasmin and its modulation by plasma protease inhibitors. Biochemistry 1998; 37: 91128.
  • 15
    Gonzales RC, Woods RE, Eddins SL. Digital Image Processing with Matlab, 2nd edn. Gatesmark Publishing, http://www.gatesmark.com 2009: 53596.
  • 16
    Nikolova ND, Toneva DS, Tenekedjieva AMK. Statistical procedures for finding distribution fits over datasets with applications in biochemistry. Bioautomation 2009; 13: 2744.
  • 17
    Lee KW, Xu XY. Modelling of flow and wall behaviour in a mildly stenosed tube. Med Eng Phys 2002; 24: 57586.
  • 18
    Whittaker P, Przyklenk K. Fibrin architecture in clots: a quantitative polarized light microscopy analysis. Blood Cells Mol Dis 2009; 42: 516.
  • 19
    Kolev K, Tenekedjiev K, Komorowicz E, Machovich R. Functional evaluation of the structural features of proteases and their substrate in fibrin surface degradation. J Biol Chem 1997; 272: 1366675.
  • 20
    Collet JP, Park D, Lesty C, Soria J, Soria C, Montalescot G, Weisel JW. Influence of fibrin network conformation and fibrin fiber diameter on fibrinolysis speed: dynamic and structural approaches by confocal microscopy. Arterioscler Thromb Vasc Biol 2000; 20: 135461.
  • 21
    Collet JP, Lesty C, Montalescot G, Weisel JW. Dynamic changes of fibrin architecture during fibrin formation and intrinsic fibrinolysis of fibrin-rich clots. J Biol Chem 2003; 278: 213315.
  • 22
    Collet JP, Moen JL, Veklich YI, Gorkun OV, Lord ST, Montalescot G, Weisel JW. The alphaC domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis. Blood 2005; 106: 382430.
  • 23
    Kunitada S, FitzGerald GA, Fitzgerald DJ. Inhibition of clot lysis and decreased binding of tissue-type plasminogen activator as a consequence of clot retraction. Blood 1992; 79: 14207.
  • 24
    Sakharov DV, Rijken DC. The effect of flow on lysis of plasma clots in a plasma environment. Thromb Haemost 2000; 83: 46974.
  • 25
    Gersh KC, Edmondson KE, Weisel JW. Flow rate and fibrin fiber alignment. J Thromb Haemost 2010; 8: 28268.
  • 26
    Campbell RA, Aleman M, Gray LD, Falvo MR, Wolberg AS. Flow profoundly influences fibrin network structure: implications for fibrin formation and clot stability in haemostasis. Thromb Haemost 2010; 104: 12814.
  • 27
    McBane RD II, Ford MAP, Karnicki K, Stewart M, Owen WG. Fibrinogen, fibrin and crosslinking in aging arterial thrombi. Thromb Haemost 2000; 84: 837.
  • 28
    Sabovic M, Lijnen HR, Keber D, Collen D. Effect of retraction on the lysis of human clots with fibrin specific and non-fibrin specific plasminogen activators. Thromb Haemost 1989; 62: 10837.
  • 29
    Braaten JV, Jerome WG, Hantgan RR. Uncoupling fibrin from integrin receptors hastens fibrinolysis at the platelet-fibrin interface. Blood 1994; 83: 98293.