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Volumn 121, Issue 10, 2013, Pages 1712-1719

Mechanisms of fibrin polymerization and clinical implications

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLSALICYLIC ACID; ARGININE; ASPARAGINE; BLOOD CLOTTING FACTOR 13A; CALCIUM ION; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; FIBRIN; FIBRINOGEN; FIBRINOPEPTIDE; GLUTAMINE; HEPARIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; METFORMIN; NANOMATERIAL; OLIGOMER; PROLINE; SIALIC ACID;

EID: 84876458886     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2012-09-306639     Document Type: Review
Times cited : (367)

References (100)
  • 1
    • 59049099881 scopus 로고    scopus 로고
    • Fibrinogen and factor xiii subcommittee of scientific standardization committee of international society on thrombosis and haemostasis. Recommendations for nomenclature on fibrinogen and fibrin
    • Medved L, Weisel JW. Fibrinogen and Factor XIII Subcommittee of Scientific Standardization Committee of International Society on Thrombosis and Haemostasis. Recommendations for nomenclature on fibrinogen and fibrin. J Thromb Haemost. 2009;7(2):355-359.
    • (2009) J Thromb Haemost. , vol.7 , Issue.2 , pp. 355-359
    • Medved, L.1    Weisel, J.W.2
  • 2
    • 79551624917 scopus 로고    scopus 로고
    • Fibrinopeptides a and b release in the process of surface fibrin formation
    • Riedel T, Suttnar J, Brynda E, et al. Fibrinopeptides A and B release in the process of surface fibrin formation. Blood. 2011;117(5): 1700-1706.
    • (2011) Blood. , vol.117 , Issue.5 , pp. 1700-1706
    • Riedel, T.1    Suttnar, J.2    Brynda, E.3
  • 3
    • 0024315774 scopus 로고
    • Fibrinogen Stony Brook, a heterozygous Aα16Arg -Cys dysfibrinogenemia. Evaluation of diminished platelet aggregation support and of enhanced inhibition of fibrin assembly
    • Galanakis DK, Henschen A, Peerschke EI, et al. Fibrinogen Stony Brook, a heterozygous A alpha 16Arg -Cys dysfibrinogenemia. Evaluation of diminished platelet aggregation support and of enhanced inhibition of fibrin assembly. J Clin Invest. 1989;84(1):295-304. (Pubitemid 19170122)
    • (1989) Journal of Clinical Investigation , vol.84 , Issue.1 , pp. 295-304
    • Galanakis, D.K.1    Henschen, A.2    Peerschke, E.I.B.3    Kehl, M.4
  • 4
    • 0141481996 scopus 로고    scopus 로고
    • Recombinant BβArg14His fibrinogen implies participation of N-terminus of Bβ chain in desA fibrin polymerization
    • DOI 10.1182/blood-2003-01-0204
    • Moen JL, Gorkun OV, Weisel JW, et al. Recombinant BbetaArg14His fibrinogen implies participation of N-terminus of Bbeta chain in desA fibrin polymerization. Blood. 2003;102(7):2466-2471. (Pubitemid 37193584)
    • (2003) Blood , vol.102 , Issue.7 , pp. 2466-2471
    • Moen, J.L.1    Gorkun, O.V.2    Weisel, J.W.3    Lord, S.T.4
  • 5
    • 27644526146 scopus 로고    scopus 로고
    • Polymerization of fibrin: Specificity, strength, and stability of knob-hole interactions studied at the single-molecule level
    • DOI 10.1182/blood-2005-05-2039
    • Litvinov RI, Gorkun OV, Owen SF, et al. Polymerization of fibrin: specificity, strength, and stability of knob-hole interactions studied at the single-molecule level. Blood. 2005;106(9): 2944-2951. (Pubitemid 41565884)
    • (2005) Blood , vol.106 , Issue.9 , pp. 2944-2951
    • Litvinov, R.I.1    Gorkun, O.V.2    Owen, S.F.3    Shuman, H.4    Weisel, J.W.5
  • 6
    • 0032537486 scopus 로고    scopus 로고
    • Crystal structure of fragment double-D from human fibrin with two different bound ligands
    • DOI 10.1021/bi9804129
    • Everse SJ, Spraggon G, Veerapandian L, et al. Crystal structure of fragment double-D from human fibrin with two different bound ligands. Biochemistry. 1998;37(24): 8637-8642. (Pubitemid 28299601)
    • (1998) Biochemistry , vol.37 , Issue.24 , pp. 8637-8642
    • Everse, S.J.1    Spraggon, G.2    Veerapandian, L.3    Riley, M.4    Doolittle, R.F.5
  • 7
    • 0037044194 scopus 로고    scopus 로고
    • 2.8 A Crystal Structures Of Recombinant Fibrinogen Fragment D With And Without Two Peptide Ligands: GHRP Binding To The "b" site disrupts its nearby calcium-binding site
    • Kostelansky MS, Betts L, Gorkun OV, et al. 2.8 A crystal structures of recombinant fibrinogen fragment D with and without two peptide ligands: GHRP binding to the "b" site disrupts its nearby calcium-binding site. Biochemistry. 2002;41(40): 12124-12132.
    • (2002) Biochemistry. , vol.41 , Issue.40 , pp. 12124-12132
    • Kostelansky, M.S.1    Betts, L.2    Gorkun, O.V.3
  • 8
    • 0030725658 scopus 로고    scopus 로고
    • Severely impaired polymerization of recombinant fibrinogen γ-364 Asp - His, the substitution discovered in a heterozygous individual
    • DOI 10.1074/jbc.272.47.29596
    • Okumura N, Gorkun OV, Lord ST. Severely impaired polymerization of recombinant fibrinogen gamma-364 Asp -. His, the substitution discovered in a heterozygous individual. J Biol Chem. 1997;272(47): 29596-29601. (Pubitemid 27508049)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.47 , pp. 29596-29601
    • Okumura, N.1    Gorkun, O.V.2    Lord, S.T.3
  • 10
    • 33846017609 scopus 로고    scopus 로고
    • Polymerization of fibrin: Direct observation and quantification of individual B:b knob-hole interactions
    • DOI 10.1182/blood-2006-07-033910
    • Litvinov RI, Gorkun OV, Galanakis DK, et al. Polymerization of fibrin: Direct observation and quantification of individual B:b knob-hole interactions. Blood. 2007;109(1):130-138. (Pubitemid 46053053)
    • (2007) Blood , vol.109 , Issue.1 , pp. 130-138
    • Litvinov, R.I.1    Gorkun, O.V.2    Galanakis, D.K.3    Yakovlev, S.4    Medved, L.5    Shuman, H.6    Weisel, J.W.7
  • 11
    • 0027511259 scopus 로고
    • Unusual Aα16Arg -Cys dysfibrinogenaemic family: Absence of normal Aα-chains in fibrinogen from two of four heterozygous siblings
    • Galanakis D, Spitzer S, Scharrer I. Unusual A alpha 16Arg -.Cys dysfibrinogenaemic family: absence of normal A alpha-chains in fibrinogen from two of four heterozygous siblings. Blood Coagul Fibrinolysis. 1993;4(1):67-71. (Pubitemid 23064918)
    • (1993) Blood Coagulation and Fibrinolysis , vol.4 , Issue.1 , pp. 67-71
    • Galanakis, D.1    Spitzer, S.2    Scharrer, I.3
  • 13
    • 66149110352 scopus 로고    scopus 로고
    • Fibrinogen variant bbetad432a has normal polymerization but does not bind knob "b"
    • Bowley SR, Lord ST. Fibrinogen variant BbetaD432A has normal polymerization but does not bind knob "B". Blood. 2009;113(18): 4425-4430.
    • (2009) Blood , vol.113 , Issue.18 , pp. 4425-4430
    • Bowley, S.R.1    Lord, S.T.2
  • 14
    • 33644513725 scopus 로고    scopus 로고
    • Binding of synthetic b knobs to fibrinogen changes the character of fibrin and inhibits its ability to activate tissue plasminogen activator and its destruction by plasmin
    • Doolittle RF, Pandi L. Binding of synthetic B knobs to fibrinogen changes the character of fibrin and inhibits its ability to activate tissue plasminogen activator and its destruction by plasmin. Biochemistry. 2006;45(8):2657-2667.
    • (2006) Biochemistry , vol.45 , Issue.8 , pp. 2657-2667
    • Doolittle, R.F.1    Pandi, L.2
  • 16
    • 79951624828 scopus 로고    scopus 로고
    • High-resolution visualization of fibrinogen molecules and fibrin fibers with atomic force microscopy
    • Yermolenko IS, Lishko VK, Ugarova TP, et al. High-resolution visualization of fibrinogen molecules and fibrin fibers with atomic force microscopy. Biomacromolecules. 2011;12(2): 370-379.
    • (2011) Biomacromolecules , vol.12 , Issue.2 , pp. 370-379
    • Yermolenko, I.S.1    Lishko, V.K.2    Ugarova, T.P.3
  • 17
    • 0018222289 scopus 로고
    • Crystals of modified fibrinogen: Size, shape and packing of molecules
    • Weisel JW, Warren SG, Cohen C. Crystals of modified fibrinogen: size, shape and packing of molecules. J Mol Biol. 1978;126(2):159-183. (Pubitemid 9088858)
    • (1978) Journal of Molecular Biology , vol.126 , Issue.2 , pp. 159-183
    • Weisel, J.W.1    Warren, S.G.2    Cohen, C.3
  • 18
    • 80855133530 scopus 로고    scopus 로고
    • Mechanism of fibrin(ogen) forced unfolding
    • Zhmurov A, Brown AE, Litvinov RI, et al. Mechanism of fibrin(ogen) forced unfolding. Structure. 2011;19(11):1615-1624.
    • (2011) Structure , vol.19 , Issue.11 , pp. 1615-1624
    • Zhmurov, A.1    Brown, A.E.2    Litvinov, R.I.3
  • 19
    • 0037093093 scopus 로고    scopus 로고
    • Fibrinogen hillsborough: A novel γGly309Asp dysfibrinogen with impaired clotting
    • DOI 10.1182/blood.V99.10.3597
    • Mullin JL, Brennan SO, Ganly PS, et al. Fibrinogen Hillsborough: a novel gammaGly309Asp dysfibrinogen with impaired clotting. Blood. 2002;99(10):3597- 3601. (Pubitemid 34534528)
    • (2002) Blood , vol.99 , Issue.10 , pp. 3597-3601
    • Mullin, J.L.1    Brennan, S.O.2    Ganly, P.S.3    George, P.M.4
  • 20
    • 33645504287 scopus 로고    scopus 로고
    • Functional characterization of fibrinogen biĉetre ii: A gamma 308 asn -.lys mutation located near the fibrin d:d interaction sites
    • Marchi RC, Carvajal Z, Boyer-Neumann C, et al. Functional characterization of fibrinogen Biĉetre II: a gamma 308 Asn -.Lys mutation located near the fibrin D:D interaction sites. Blood Coagul Fibrinolysis. 2006;17(3):193-201.
    • (2006) Blood Coagul Fibrinolysis , vol.17 , Issue.3 , pp. 193-201
    • Marchi, R.C.1    Carvajal, Z.2    Boyer-Neumann, C.3
  • 21
    • 70149114200 scopus 로고    scopus 로고
    • Impaired protofibril formation in fibrinogen gamma n308k is due to altered D: D and A: A interactions
    • Bowley SR, Okumura N, Lord ST. Impaired protofibril formation in fibrinogen gamma N308K is due to altered D:D and "A:a" interactions. Biochemistry. 2009;48(36):8656-8663.
    • (2009) Biochemistry. , vol.48 , Issue.36 , pp. 8656-8663
    • Bowley, S.R.1    Okumura, N.2    Lord, S.T.3
  • 22
    • 79955967930 scopus 로고    scopus 로고
    • Visualization and identification of the structures formed during early stages of fibrin polymerization
    • Chernysh IN, Nagaswami C, Weisel JW. Visualization and identification of the structures formed during early stages of fibrin polymerization. Blood. 2011;117(17):4609-4614.
    • (2011) Blood. , vol.117 , Issue.17 , pp. 4609-4614
    • Chernysh, I.N.1    Nagaswami, C.2    Weisel, J.W.3
  • 23
    • 0025679015 scopus 로고
    • Electron microscope investigation of the early stages of fibrin assembly: Twisted protofibrils and fibers
    • Medved' L, Ugarova T, Veklich Y, et al. Electron microscope investigation of the early stages of fibrin assembly. Twisted protofibrils and fibers. J Mol Biol. 1990;216(3):503-509. (Pubitemid 120037383)
    • (1990) Journal of Molecular Biology , vol.216 , Issue.3 , pp. 503-509
    • Medved, L.1    Ugarova, T.2    Veklich, Y.3    Lukinova, N.4    Weisel, J.5
  • 24
    • 84861707362 scopus 로고    scopus 로고
    • Evidence that fibrinogen g' directly interferes with protofibril growth: Implications for fibrin structure and clot stiffness
    • Allan P, Uitte de Willige S, Abou-Saleh RH, et al. Evidence that fibrinogen g' directly interferes with protofibril growth: implications for fibrin structure and clot stiffness. J Thromb Haemost. 2012; 10(6):1072-1080.
    • (2012) J Thromb Haemost , vol.10 , Issue.6 , pp. 1072-1080
    • Allan, P.1    Uitte De Willige, S.2    Abou-Saleh, R.H.3
  • 25
    • 0038494830 scopus 로고    scopus 로고
    • Fibrinogen gamma-chain splice variant γ′ alters fibrin formation and structure
    • DOI 10.1182/blood-2002-10-3150
    • Cooper AV, Standeven KF, Ariěns RA. Fibrinogen gamma-chain splice variant gamma' alters fibrin formation and structure. Blood. 2003; 102(2):535-540. (Pubitemid 36841972)
    • (2003) Blood , vol.102 , Issue.2 , pp. 535-540
    • Cooper, A.V.1    Standeven, K.F.2    Ariens, R.A.S.3
  • 26
    • 67649710434 scopus 로고    scopus 로고
    • The presence of gamma' chain impairs fibrin polymerization
    • Gersh KC, Nagaswami C, Weisel JW, et al. The presence of gamma' chain impairs fibrin polymerization. Thromb Res. 2009;124(3): 356-363.
    • (2009) Thromb Res , vol.124 , Issue.3 , pp. 356-363
    • Gersh, K.C.1    Nagaswami, C.2    Weisel, J.W.3
  • 29
    • 0023752048 scopus 로고
    • Deglycosylation of fibrinogen accelerates polymerization and increases lateral aggregation of fibrin fibers
    • Langer BG, Weisel JW, Dinauer PA, et al. Deglycosylation of fibrinogen accelerates polymerization and increases lateral aggregation of fibrin fibers. J Biol Chem. 1988;263(29): 15056-15063.
    • (1988) J Biol Chem , vol.263 , Issue.29 , pp. 15056-15063
    • Langer, B.G.1    Weisel, J.W.2    Dinauer, P.A.3
  • 30
    • 0034664089 scopus 로고    scopus 로고
    • Decreased lateral aggregation of a variant recombinant fibrinogen provides insight into the polymerization mechanism
    • DOI 10.1021/bi000045c
    • Mullin JL, Gorkun OV, Lord ST. Decreased lateral aggregation of a variant recombinant fibrinogen provides insight into the polymerization mechanism. Biochemistry. 2000; 39(32):9843-9849. (Pubitemid 30626832)
    • (2000) Biochemistry , vol.39 , Issue.32 , pp. 9843-9849
    • Mullin, J.L.1    Gorkun, O.V.2    Lord, S.T.3
  • 31
    • 0141785263 scopus 로고    scopus 로고
    • Fibrinogens kosai and ogasa: Bbeta15gly -.cys (ggt -.tgt) substitution associated with impairment of fibrinopeptide b release and lateral aggregation
    • Hirota-Kawadobora M, Terasawa F, Yonekawa O, et al. Fibrinogens Kosai and Ogasa: Bbeta15Gly -.Cys (GGT -.TGT) substitution associated with impairment of fibrinopeptide B release and lateral aggregation. J Thromb Haemost. 2003;1(2):275-283.
    • (2003) J Thromb Haemost. , vol.1 , Issue.2 , pp. 275-283
    • Hirota-Kawadobora, M.1    Terasawa, F.2    Yonekawa, O.3
  • 33
    • 80052707733 scopus 로고    scopus 로고
    • Structure, stability, and interaction of fibrin ac-domain polymers
    • Tsurupa G, Mahid A, Veklich Y, et al. Structure, stability, and interaction of fibrin aC-domain polymers. Biochemistry. 2011;50(37): 8028-8037.
    • (2011) Biochemistry , vol.50 , Issue.37 , pp. 8028-8037
    • Tsurupa, G.1    Mahid, A.2    Veklich, Y.3
  • 34
    • 84859178020 scopus 로고    scopus 로고
    • On the mechanism of ac polymer formation in fibrin
    • Tsurupa G, Pechik I, Litvinov RI, et al. On the mechanism of aC polymer formation in fibrin. Biochemistry. 2012;51(12):2526-2538.
    • (2012) Biochemistry , vol.51 , Issue.12 , pp. 2526-2538
    • Tsurupa, G.1    Pechik, I.2    Litvinov, R.I.3
  • 35
    • 34547753415 scopus 로고    scopus 로고
    • Direct evidence for specific interactions of the fibrinogen αC-domains with the central E region and with each other
    • DOI 10.1021/bi700944j
    • Litvinov RI, Yakovlev S, Tsurupa G, et al. Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other. Biochemistry. 2007; 46(31):9133-9142. (Pubitemid 47237388)
    • (2007) Biochemistry , vol.46 , Issue.31 , pp. 9133-9142
    • Litvinov, R.I.1    Yakovlev, S.2    Tsurupa, G.3    Gorkun, O.V.4    Medved, L.5    Weisel, J.W.6
  • 36
    • 28444478753 scopus 로고    scopus 로고
    • The αC domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis
    • DOI 10.1182/blood-2005-05-2150
    • Collet JP, Moen JL, Veklich YI, et al. The alphaC domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis. Blood. 2005;106(12): 3824-3830. (Pubitemid 41739019)
    • (2005) Blood , vol.106 , Issue.12 , pp. 3824-3830
    • Collet, J.-P.1    Moen, J.L.2    Veklich, Y.I.3    Gorkun, O.V.4    Lord, S.T.5    Montalescot, G.6    Weisel, J.W.7
  • 37
    • 80054991411 scopus 로고    scopus 로고
    • Substitution of the human ac region with the analogous chicken domain generates a fibrinogen with severely impaired lateral aggregation: Fibrin monomers assemble into protofibrils but protofibrils do not assemble into fibers
    • Ping L, Huang L, Cardinali B, et al. Substitution of the human aC region with the analogous chicken domain generates a fibrinogen with severely impaired lateral aggregation: fibrin monomers assemble into protofibrils but protofibrils do not assemble into fibers. Biochemistry. 2011;50(42):9066-9075.
    • (2011) Biochemistry , vol.50 , Issue.42 , pp. 9066-9075
    • Ping, L.1    Huang, L.2    Cardinali, B.3
  • 38
    • 1542297673 scopus 로고    scopus 로고
    • Calcium-Binding Site β2, Adjacent to the 'b' Polymerization Site, Modulates Lateral Aggregation of Protofibrils during Fibrin Polymerization
    • DOI 10.1021/bi0359978
    • Kostelansky MS, Lounes KC, Ping LF, et al. Calcium-binding site beta 2, adjacent to the "b" polymerization site, modulates lateral aggregation of protofibrils during fibrin polymerization. Biochemistry. 2004;43(9): 2475-2483. (Pubitemid 38327843)
    • (2004) Biochemistry , vol.43 , Issue.9 , pp. 2475-2483
    • Kostelansky, M.S.1    Lounes, K.C.2    Ping, L.F.3    Dickerson, S.K.4    Gorkun, O.V.5    Lord, S.T.6
  • 39
    • 34247594833 scopus 로고    scopus 로고
    • Probing the γ2 calcium-binding site: Studies with γD298,301A fibrinogen reveal changes in the γ294-301 loop that alter the integrity of the 'a' polymerization site
    • DOI 10.1021/bi602607a
    • Kostelansky MS, Lounes KC, Ping LF, et al. Probing the gamma2 calcium-binding site: studies with gammaD298,301A fibrinogen reveal changes in the gamma294-301 loop that alter the integrity of the "a" polymerization site. Biochemistry. 2007;46(17):5114-5123. (Pubitemid 46683009)
    • (2007) Biochemistry , vol.46 , Issue.17 , pp. 5114-5123
    • Kostelansky, M.S.1    Lounes, K.C.2    Ping, L.F.3    Dickerson, S.K.4    Gorkun, O.V.5    Lord, S.T.6
  • 40
    • 0024443424 scopus 로고
    • Fibrinogen sialic acid residues are low affinity calcium-binding sites that influence fibrin assembly
    • Dang CV, Shin CK, Bell WR, et al. Fibrinogen sialic acid residues are low affinity calciumbinding sites that influence fibrin assembly. J Biol Chem. 1989;264(25):15104-15108. (Pubitemid 19237344)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.25 , pp. 15104-15108
    • Dang, C.V.1    Shin, C.K.2    Bell, W.R.3    Nagaswami, C.4    Weisel, J.W.5
  • 41
    • 0142063416 scopus 로고    scopus 로고
    • 2+ Concentration
    • DOI 10.1021/bi034411e
    • Profumo A, Turci M, Damonte G, et al. Kinetics of fibrinopeptide release by thrombin as a function of CaCl2 concentration: different susceptibility of FPA and FPB and evidence for a fibrinogen isoform-specific effect at physiological Ca21 concentration. Biochemistry. 2003;42(42):12335-12348. (Pubitemid 37296510)
    • (2003) Biochemistry , vol.42 , Issue.42 , pp. 12335-12348
    • Profumo, A.1    Turci, M.2    Damonte, G.3    Ferri, F.4    Magatti, D.5    Cardinali, B.6    Cuniberti, C.7    Rocco, M.8
  • 42
    • 0037161292 scopus 로고    scopus 로고
    • Analysis of engineered fibrinogen variants suggests that an additional site mediates platelet aggregation and that 'B-b' interactions have a role in protofibril formation
    • DOI 10.1021/bi011988s
    • Lounes KC, Ping L, Gorkun OV, et al. Analysis of engineered fibrinogen variants suggests that an additional site mediates platelet aggregation and that "B-b" interactions have a role in protofibril formation. Biochemistry. 2002;41(16): 5291-5299. (Pubitemid 34411685)
    • (2002) Biochemistry , vol.41 , Issue.16 , pp. 5291-5299
    • Lounes, K.C.1    Ping, L.2    Gorkun, O.V.3    Lord, S.T.4
  • 43
    • 77956567764 scopus 로고    scopus 로고
    • Calcium dependence of fibrin nanomechanics: The g1 calcium mediates the unfolding of fibrinogen induced by force applied to the "a-A" bond
    • Averett LE, Akhremitchev BB, Schoenfisch MH, et al. Calcium dependence of fibrin nanomechanics: the g1 calcium mediates the unfolding of fibrinogen induced by force applied to the "A-a" bond. Langmuir. 2010;26(18): 14716-14722.
    • (2010) Langmuir. , vol.26 , Issue.18 , pp. 14716-14722
    • Averett, L.E.1    Akhremitchev, B.B.2    Schoenfisch, M.H.3
  • 44
    • 84860504905 scopus 로고    scopus 로고
    • Fibrinogen residue gala341 is necessary for calcium binding and 'a-A' interactions
    • Park R, Ping L, Song J, et al. Fibrinogen residue gAla341 is necessary for calcium binding and 'A-a' interactions. Thromb Haemost. 2012; 107(5):875-883.
    • (2012) Thromb Haemost , vol.107 , Issue.5 , pp. 875-883
    • Park, R.1    Ping, L.2    Song, J.3
  • 45
    • 0027247825 scopus 로고
    • Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular junction
    • Mosesson MW, DiOrio JP, Siebenlist KR, et al. Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular junction. Blood. 1993;82(5):1517-1521. (Pubitemid 23263968)
    • (1993) Blood , vol.82 , Issue.5 , pp. 1517-1521
    • Mosesson, M.W.1    DiOrio, J.P.2    Siebenlist, K.R.3    Wall, J.S.4    Hainfeld, J.F.5
  • 48
    • 46749153500 scopus 로고    scopus 로고
    • Dynamic imaging of fibrin network formation correlated with other measures of polymerization
    • Chernysh IN, Weisel JW. Dynamic imaging of fibrin network formation correlated with other measures of polymerization. Blood. 2008; 111(10):4854-4861.
    • (2008) Blood , vol.111 , Issue.10 , pp. 4854-4861
    • Chernysh, I.N.1    Weisel, J.W.2
  • 49
    • 41349099123 scopus 로고    scopus 로고
    • Structure of fibrin gels studied by elastic light scattering techniques: Dependence of fractal dimension, gel crossover length, fiber diameter, and fiber density on monomer concentration
    • Ferri F, Greco M, Arcòvito G, et al. Structure of fibrin gels studied by elastic light scattering techniques: dependence of fractal dimension, gel crossover length, fiber diameter, and fiber density on monomer concentration. Phys Rev E Stat Nonlin Soft Matter Phys. 2002;66(1): 011913.
    • (2002) Phys Rev E Stat Nonlin Soft Matter Phys. , vol.66 , Issue.1 , pp. 011913
    • Ferri, F.1    Greco, M.2    Arcòvito, G.3
  • 51
    • 77956169533 scopus 로고    scopus 로고
    • Gel point and fractal microstructure of incipient blood clots are significant new markers of hemostasis for healthy and anticoagulated blood
    • Evans PA, Hawkins K, Morris RH, et al. Gel point and fractal microstructure of incipient blood clots are significant new markers of hemostasis for healthy and anticoagulated blood. Blood. 2010; 116(17):3341-3346.
    • (2010) Blood. , vol.116 , Issue.17 , pp. 3341-3346
    • Evans, P.A.1    Hawkins, K.2    Morris, R.H.3
  • 52
    • 77958474678 scopus 로고    scopus 로고
    • Nanostructure of the fibrin clot
    • Yeromonahos C, Polack B, Caton F. Nanostructure of the fibrin clot. Biophys J. 2010; 99(7):2018-2027.
    • (2010) Biophys J , vol.99 , Issue.7 , pp. 2018-2027
    • Yeromonahos, C.1    Polack, B.2    Caton, F.3
  • 53
    • 0020645310 scopus 로고
    • Factors influencing fibrin gel structure studied by flow measurement
    • Okada M, Blombǎck B. Factors influencing fibrin gel structure studied by flow measurement. Ann N Y Acad Sci. 1983;408:233-253. (Pubitemid 13072040)
    • (1983) Annals of the New York Academy of Sciences , vol.408 , pp. 233-253
    • Okada, M.1    Blomback, B.2
  • 54
    • 80052477348 scopus 로고    scopus 로고
    • Nanoparticle diffusion measures bulk clot permeability
    • Spero RC, Sircar RK, Schubert R, et al. Nanoparticle diffusion measures bulk clot permeability. Biophys J. 2011;101(4):943-950.
    • (2011) Biophys J , vol.101 , Issue.4 , pp. 943-950
    • Spero, R.C.1    Sircar, R.K.2    Schubert, R.3
  • 55
    • 3242690025 scopus 로고    scopus 로고
    • Cross-linked γ-chains in fibrin fibrils bridge transversely between strands: No
    • DOI 10.1111/j.1538-7933.2003.00621.x
    • Weisel JW. Cross-linked gamma-chains in fibrin fibrils bridge transversely between strands: no. J Thromb Haemost. 2004;2(3):394-399. (Pubitemid 40185648)
    • (2004) Journal of Thrombosis and Haemostasis , vol.2 , Issue.3 , pp. 394-399
    • Weisel, J.W.1
  • 56
    • 3242707117 scopus 로고    scopus 로고
    • Cross-linked γ-chains in fibrin fibrils bridge transversely between strands: Yes
    • DOI 10.1111/j.1538-7933.2004.00613.x
    • Mosesson MW. Cross-linked gamma-chains in fibrin fibrils bridge 'transversely' between strands: yes. J Thromb Haemost. 2004;2(3): 388-393. (Pubitemid 40185647)
    • (2004) Journal of Thrombosis and Haemostasis , vol.2 , Issue.3 , pp. 388-393
    • Mosesson, M.W.1
  • 57
    • 77956474949 scopus 로고    scopus 로고
    • Single fibrin fiber experiments suggest longitudinal rather than transverse cross-linking: Reply to a rebuttal
    • Guthold M, Carlisle C. Single fibrin fiber experiments suggest longitudinal rather than transverse cross-linking: reply to a rebuttal. J Thromb Haemost. 2010;8(9):2090-2091.
    • (2010) J Thromb Haemost , vol.8 , Issue.9 , pp. 2090-2091
    • Guthold, M.1    Carlisle, C.2
  • 58
    • 34547942696 scopus 로고    scopus 로고
    • Functional analysis of fibrin γ-chain cross-linking by activated factor XIII: Determination of a cross-linking pattern that maximizes clot stiffness
    • DOI 10.1182/blood-2007-01-066837
    • Standeven KF, Carter AM, Grant PJ, et al. Functional analysis of fibrin gamma-chain crosslinking by activated factor XIII: determination of a cross-linking pattern that maximizes clot stiffness. Blood. 2007;110(3):902-907. (Pubitemid 47267427)
    • (2007) Blood , vol.110 , Issue.3 , pp. 902-907
    • Standeven, K.F.1    Carter, A.M.2    Grant, P.J.3    Weisel, J.W.4    Chernysh, I.5    Masova, L.6    Lord, S.T.7    Ariens, R.A.S.8
  • 59
    • 0242348804 scopus 로고    scopus 로고
    • Genetic regulation of fibrin structure and function: Complex gene-environment interactions may modulate vascular risk
    • DOI 10.1016/S0140-6736(03)13135-2
    • Lim BC, Ariěns RA, Carter AM, et al. Genetic regulation of fibrin structure and function: complex gene-environment interactions may modulate vascular risk. Lancet. 2003;361(9367): 1424-1431. (Pubitemid 36515043)
    • (2003) Lancet , vol.361 , Issue.9367 , pp. 1424-1431
    • Lim, B.C.B.1    Ariens, R.A.S.2    Carter, A.M.3    Weisel, J.W.4    Grant, P.J.5
  • 60
    • 48249113756 scopus 로고    scopus 로고
    • Alterations of fibrinogen structure in human disease
    • Hoffman M. Alterations of fibrinogen structure in human disease. Cardiovasc Hematol Agents Med Chem. 2008;6(3):206-211.
    • (2008) Cardiovasc Hematol Agents Med Chem , vol.6 , Issue.3 , pp. 206-211
    • Hoffman, M.1
  • 62
    • 0026771894 scopus 로고
    • Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: Clot structure and assembly are kinetically controlled
    • Weisel JW, Nagaswami C. Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: clot structure and assembly are kinetically controlled. Biophys J. 1992;63(1):111-128.
    • (1992) Biophys J , vol.63 , Issue.1 , pp. 111-128
    • Weisel, J.W.1    Nagaswami, C.2
  • 63
    • 80053641885 scopus 로고    scopus 로고
    • Factor xiia regulates the structure of the fibrin clot independently of thrombin generation through direct interaction with fibrin
    • Konings J, Govers-Riemslag JW, Philippou H, et al. Factor XIIa regulates the structure of the fibrin clot independently of thrombin generation through direct interaction with fibrin. Blood. 2011; 118(14):3942-3951.
    • (2011) Blood , vol.118 , Issue.14 , pp. 3942-3951
    • Konings, J.1    Govers-Riemslag, J.W.2    Philippou, H.3
  • 64
    • 80055112784 scopus 로고    scopus 로고
    • Differential contributions of monocyte-and platelet-derived microparticles towards thrombin generation and fibrin formation and stability
    • Aleman MM, Gardiner C, Harrison P, et al. Differential contributions of monocyte-and platelet-derived microparticles towards thrombin generation and fibrin formation and stability. J Thromb Haemost. 2011;9(11):2251-2261.
    • (2011) J Thromb Haemost , vol.9 , Issue.11 , pp. 2251-2261
    • Aleman, M.M.1    Gardiner, C.2    Harrison, P.3
  • 65
    • 0037040831 scopus 로고    scopus 로고
    • A structural and dynamic investigation of the facilitating effect of glycoprotein IIb/IIIa inhibitors in dissolving platelet-rich clots
    • DOI 10.1161/hh0402.105095
    • Collet JP, Montalescot G, Lesty C, et al. A structural and dynamic investigation of the facilitating effect of glycoprotein IIb/IIIa inhibitors in dissolving platelet-rich clots. Circ Res. 2002; 90(4):428-434. (Pubitemid 34633912)
    • (2002) Circulation Research , vol.90 , Issue.4 , pp. 428-434
    • Collet, J.Ph.1    Montalescot, G.2    Lesty, C.3    Weisel, J.W.4
  • 66
    • 57549089843 scopus 로고    scopus 로고
    • Cellular procoagulant activity dictates clot structure and stability as a function of distance from the cell surface
    • Campbell RA, Overmyer KA, Bagnell CR, et al. Cellular procoagulant activity dictates clot structure and stability as a function of distance from the cell surface. Arterioscler Thromb Vasc Biol. 2008;28(12):2247-2254.
    • (2008) Arterioscler Thromb Vasc Biol , vol.28 , Issue.12 , pp. 2247-2254
    • Campbell, R.A.1    Overmyer, K.A.2    Bagnell, C.R.3
  • 67
    • 77952974521 scopus 로고    scopus 로고
    • Polyphosphate modifies the fibrin network and down-regulates fibrinolysis by attenuating binding of tpa and plasminogen to fibrin
    • Mutch NJ, Engel R, Uitte de Willige S, et al. Polyphosphate modifies the fibrin network and down-regulates fibrinolysis by attenuating binding of tPA and plasminogen to fibrin. Blood. 2010;115(19):3980-3988.
    • (2010) Blood , vol.115 , Issue.19 , pp. 3980-3988
    • Mutch, N.J.1    Engel, R.2    Uitte De Willige, S.3
  • 69
    • 84055193881 scopus 로고    scopus 로고
    • Mechanobiology of platelets: Techniques to study the role of fluid flow and platelet retraction forces at the micro-and nano-scale
    • Feghhi S, Sniadecki NJ. Mechanobiology of platelets: techniques to study the role of fluid flow and platelet retraction forces at the micro-and nano-scale. Int J Mol Sci. 2011;12(12): 9009-9030.
    • (2011) Int J Mol Sci , vol.12 , Issue.12 , pp. 9009-9030
    • Feghhi, S.1    Sniadecki, N.J.2
  • 70
    • 20844432399 scopus 로고    scopus 로고
    • Initiation and propagation of coagulation from tissue factor-bearing cell monolayers to plasma: Initiator cells do not regulate spatial growth rate
    • DOI 10.1111/j.1538-7836.2005.01128.x
    • Ovanesov MV, Ananyeva NM, Panteleev MA, et al. Initiation and propagation of coagulation from tissue factor-bearing cell monolayers to plasma: initiator cells do not regulate spatial growth rate. J Thromb Haemost. 2005;3(2): 321-331. (Pubitemid 41623621)
    • (2005) Journal of Thrombosis and Haemostasis , vol.3 , Issue.2 , pp. 321-331
    • Ovanesov, M.V.1    Ananyeva, N.M.2    Panteleev, M.A.3    Ataullakhanov, F.I.4    Saenko, E.L.5
  • 71
    • 74049100937 scopus 로고    scopus 로고
    • Contributions of extravascular and intravascular cells to fibrin network formation, structure, and stability
    • Campbell RA, Overmyer KA, Selzman CH, et al. Contributions of extravascular and intravascular cells to fibrin network formation, structure, and stability. Blood. 2009;114(23):4886-4896.
    • (2009) Blood. , vol.114 , Issue.23 , pp. 4886-4896
    • Campbell, R.A.1    Overmyer, K.A.2    Selzman, C.H.3
  • 72
    • 72949113232 scopus 로고    scopus 로고
    • Fibrin network structure and clot mechanical properties are altered by incorporation of erythrocytes
    • Gersh KC, Nagaswami C, Weisel JW. Fibrin network structure and clot mechanical properties are altered by incorporation of erythrocytes. Thromb Haemost. 2009;102(6):1169-1175.
    • (2009) Thromb Haemost. , vol.102 , Issue.6 , pp. 1169-1175
    • Gersh, K.C.1    Nagaswami, C.2    Weisel, J.W.3
  • 73
    • 77953521329 scopus 로고    scopus 로고
    • Plasma and cellular contributions to fibrin network formation, structure and stability
    • Wolberg AS. Plasma and cellular contributions to fibrin network formation, structure and stability. Haemophilia. 2010;16(suppl): 37-12.
    • (2010) Haemophilia. , vol.16 , Issue.SUPPL. , pp. 37-12
    • Wolberg, A.S.1
  • 74
    • 84865444722 scopus 로고    scopus 로고
    • Determinants of fibrin formation, structure, and function
    • Wolberg AS. Determinants of fibrin formation, structure, and function. Curr Opin Hematol. 2012;19(5):349-356.
    • (2012) Curr Opin Hematol , vol.19 , Issue.5 , pp. 349-356
    • Wolberg, A.S.1
  • 75
    • 77950635369 scopus 로고    scopus 로고
    • Thrombin flux and wall shear rate regulate fibrin fiber deposition state during polymerization under flow
    • Neeves KB, Illing DA, Diamond SL. Thrombin flux and wall shear rate regulate fibrin fiber deposition state during polymerization under flow. Biophys J. 2010;98(7):1344-1352.
    • (2010) Biophys J. , vol.98 , Issue.7 , pp. 1344-1352
    • Neeves, K.B.1    Illing, D.A.2    Diamond, S.L.3
  • 77
    • 78649726921 scopus 로고    scopus 로고
    • Flow profoundly influences fibrin network structure: Implications for fibrin formation and clot stability in haemostasis
    • Campbell RA, Aleman M, Gray LD, et al. Flow profoundly influences fibrin network structure: implications for fibrin formation and clot stability in haemostasis. Thromb Haemost. 2010;104(6): 1281-1284.
    • (2010) Thromb Haemost , vol.104 , Issue.6 , pp. 1281-1284
    • Campbell, R.A.1    Aleman, M.2    Gray, L.D.3
  • 78
    • 57949113145 scopus 로고    scopus 로고
    • Fibrin architecture in clots: A quantitative polarized light microscopy analysis
    • Whittaker P, Przyklenk K. Fibrin architecture in clots: a quantitative polarized light microscopy analysis. Blood Cells Mol Dis. 2009;42(1):51-56.
    • (2009) Blood Cells Mol Dis , vol.42 , Issue.1 , pp. 51-56
    • Whittaker, P.1    Przyklenk, K.2
  • 79
    • 79955648845 scopus 로고    scopus 로고
    • Hindered dissolution of fibrin formed under mechanical stress
    • Varj ́u I, S'otonyi P, Machovich R, et al. Hindered dissolution of fibrin formed under mechanical stress. J Thromb Haemost. 2011;9(5):979-986.
    • (2011) J Thromb Haemost. , vol.9 , Issue.5 , pp. 979-986
    • Varj́u, I.1    S'otonyi, P.2    Machovich, R.3
  • 80
    • 84861529620 scopus 로고    scopus 로고
    • Thrombus growth and embolism on tissue factorbearing collagen surfaces under flow: Role of thrombin with and without fibrin
    • Colace TV, Muthard RW, Diamond SL. Thrombus growth and embolism on tissue factorbearing collagen surfaces under flow: role of thrombin with and without fibrin. Arterioscler Thromb Vasc Biol. 2012;32(6):1466-1476.
    • (2012) Arterioscler Thromb Vasc Biol. , vol.32 , Issue.6 , pp. 1466-1476
    • Colace, T.V.1    Muthard, R.W.2    Diamond, S.L.3
  • 81
    • 66749154095 scopus 로고    scopus 로고
    • Molecular magnetic resonance imaging of deep vein thrombosis using a fibrin-targeted contrast agent: A feasibility study
    • Katoh M, Haage P, Wiethoff AJ, et al. Molecular magnetic resonance imaging of deep vein thrombosis using a fibrin-targeted contrast agent: a feasibility study. Invest Radiol. 2009; 44(3):146-150.
    • (2009) Invest Radiol , vol.44 , Issue.3 , pp. 146-150
    • Katoh, M.1    Haage, P.2    Wiethoff, A.J.3
  • 82
    • 67651093879 scopus 로고    scopus 로고
    • Effects of acetylsalicylic acid on increase of fibrin network porosity and the consequent upregulation of fibrinolysis
    • He S, Bark N, Wang H, et al. Effects of acetylsalicylic acid on increase of fibrin network porosity and the consequent upregulation of fibrinolysis. J Cardiovasc Pharmacol. 2009; 53(1):24-29.
    • (2009) J Cardiovasc Pharmacol , vol.53 , Issue.1 , pp. 24-29
    • He, S.1    Bark, N.2    Wang, H.3
  • 83
    • 84860123901 scopus 로고    scopus 로고
    • Antithrombin-independent effects of heparins on fibrin clot nanostructure
    • Yeromonahos C, Marlu R, Polack B, et al. Antithrombin-independent effects of heparins on fibrin clot nanostructure. Arterioscler Thromb Vasc Biol. 2012;32(5):1320-1324.
    • (2012) Arterioscler Thromb Vasc Biol , vol.32 , Issue.5 , pp. 1320-1324
    • Yeromonahos, C.1    Marlu, R.2    Polack, B.3
  • 84
    • 77956267128 scopus 로고    scopus 로고
    • Atorvastatin has antithrombotic effects in patients with type 1 diabetes and dyslipidemia
    • Tehrani S, Mobarrez F, Antovic A, et al. Atorvastatin has antithrombotic effects in patients with type 1 diabetes and dyslipidemia. Thromb Res. 2010;126(3):e225-e231.
    • (2010) Thromb Res , vol.126 , Issue.3
    • Tehrani, S.1    Mobarrez, F.2    Antovic, A.3
  • 85
    • 84878089110 scopus 로고    scopus 로고
    • Statins, fenofibrate, and quinapril increase clot permeability and enhance fibrinolysis in patients with coronary artery disease
    • Undas A, Celinska-Lǒwenhoff M, Lǒwenhoff T, et al. Statins, fenofibrate, and quinapril increase clot permeability and enhance fibrinolysis in patients with coronary artery disease. J Thromb Haemost. 2006;4(5):1029-1036.
    • (2006) J Thromb Haemost , vol.4 , Issue.5 , pp. 1029-1036
    • Undas, A.1    Celinska-Lǒwenhoff, M.2    Lǒwenhoff, T.3
  • 86
    • 0036091884 scopus 로고    scopus 로고
    • The effect of dimethylbiguanide on thrombin activity, FXIII activation, fibrin polymerization, and fibrin clot formation
    • Standeven KF, Ariěns RA, Whitaker P, et al. The effect of dimethylbiguanide on thrombin activity, FXIII activation, fibrin polymerization, and fibrin clot formation. Diabetes. 2002;51(1):189-197. (Pubitemid 34517997)
    • (2002) Diabetes , vol.51 , Issue.1 , pp. 189-197
    • Standeven, K.F.1    Ariens, R.A.S.2    Whitaker, P.3    Ashcroft, A.E.4    Weisel, J.W.5    Grant, P.J.6
  • 87
    • 80055108960 scopus 로고    scopus 로고
    • Engineering fibrin polymers through engagement of alternative polymerization mechanisms
    • Stabenfeldt SE, Gourley M, Krishnan L, et al. Engineering fibrin polymers through engagement of alternative polymerization mechanisms. Biomaterials. 2012;33(2):535-544.
    • (2012) Biomaterials , vol.33 , Issue.2 , pp. 535-544
    • Stabenfeldt, S.E.1    Gourley, M.2    Krishnan, L.3
  • 88
    • 80755141258 scopus 로고    scopus 로고
    • Peptide-derivatized albumins that inhibit fibrin polymerization
    • Watson JW, Doolittle RF. Peptide-derivatized albumins that inhibit fibrin polymerization. Biochemistry. 2011;50(45):9923-9927.
    • (2011) Biochemistry , vol.50 , Issue.45 , pp. 9923-9927
    • Watson, J.W.1    Doolittle, R.F.2
  • 89
    • 81755161511 scopus 로고    scopus 로고
    • Fibrin clot structure and function: A role in the pathophysiology of arterial and venous thromboembolic diseases
    • Undas A, Ariěns RA. Fibrin clot structure and function: a role in the pathophysiology of arterial and venous thromboembolic diseases. Arterioscler Thromb Vasc Biol. 2011;31(12): e88-e99.
    • (2011) Arterioscler Thromb Vasc Biol. , vol.31 , Issue.12
    • Undas, A.1    Ariěns, R.A.2
  • 90
    • 0036799775 scopus 로고    scopus 로고
    • Realtime in vivo imaging of platelets, tissue factor and fibrin during arterial thrombus formation in the mouse
    • Falati S, Gross P, Merrill-Skoloff G, et al. Realtime in vivo imaging of platelets, tissue factor and fibrin during arterial thrombus formation in the mouse. Nat Med. 2002;8(10):1175-1181.
    • (2002) Nat Med , vol.8 , Issue.10 , pp. 1175-1181
    • Falati, S.1    Gross, P.2    Merrill-Skoloff, G.3
  • 91
    • 84868108253 scopus 로고    scopus 로고
    • Platelet-targeting sensor reveals thrombin gradients within blood clots forming in microfluidic assays and in mouse
    • Welsh JD, Colace TV, Muthard RW, et al. Platelet-targeting sensor reveals thrombin gradients within blood clots forming in microfluidic assays and in mouse. J Thromb Haemost. 2012;10(11):2344-2353.
    • (2012) J Thromb Haemost , vol.10 , Issue.11 , pp. 2344-2353
    • Welsh, J.D.1    Colace, T.V.2    Muthard, R.W.3
  • 92
    • 79952673992 scopus 로고    scopus 로고
    • Composition of coronary thrombus in acute myocardial infarction
    • Silvain J, Collet JP, Nagaswami C, et al. Composition of coronary thrombus in acute myocardial infarction. J Am Coll Cardiol. 2011; 57(12):1359-1367.
    • (2011) J Am Coll Cardiol , vol.57 , Issue.12 , pp. 1359-1367
    • Silvain, J.1    Collet, J.P.2    Nagaswami, C.3
  • 94
    • 34250692159 scopus 로고    scopus 로고
    • Structure of fibrin: Impact on clot stability
    • DOI 10.1111/j.1538-7836.2007.02504.x, State of the Art 2007: XXI Congress of the International Society on Thrombosis and Haemostasis
    • Weisel JW. Structure of fibrin: impact on clot stability. J Thromb Haemost. 2007;5(suppl 1): 116-124. (Pubitemid 46958824)
    • (2007) Journal of Thrombosis and Haemostasis , vol.5 , Issue.SUPPL. 1 , pp. 116-124
    • Weisel, J.W.1
  • 96
    • 81755173567 scopus 로고    scopus 로고
    • Clot architecture is altered in abdominal aortic aneurysms and correlates with aneurysm size
    • Scott DJ, Prasad P, Philippou H, et al. Clot architecture is altered in abdominal aortic aneurysms and correlates with aneurysm size. Arterioscler Thromb Vasc Biol. 2011;31(12): 3004-3010.
    • (2011) Arterioscler Thromb Vasc Biol , vol.31 , Issue.12 , pp. 3004-3010
    • Scott, D.J.1    Prasad, P.2    Philippou, H.3
  • 97
    • 65249140472 scopus 로고    scopus 로고
    • Altered fibrin clot structure/function in patients with cryptogenic ischemic stroke
    • Undas A, Podolec P, Zawilska K, et al. Altered fibrin clot structure/function in patients with cryptogenic ischemic stroke. Stroke. 2009;40(4): 1499-1501.
    • (2009) Stroke , vol.40 , Issue.4 , pp. 1499-1501
    • Undas, A.1    Podolec, P.2    Zawilska, K.3
  • 98
    • 77949263452 scopus 로고    scopus 로고
    • Altered fibrin clot structure/function in patients with idiopathic venous thromboembolism and in their relatives
    • Undas A, Zawilska K, Ciesla-Dul M, et al. Altered fibrin clot structure/function in patients with idiopathic venous thromboembolism and in their relatives. Blood. 2009;114(19):4272-4278.
    • (2009) Blood , vol.114 , Issue.19 , pp. 4272-4278
    • Undas, A.1    Zawilska, K.2    Ciesla-Dul, M.3
  • 99
    • 57749122066 scopus 로고    scopus 로고
    • Fibrinogen beta-chain tyrosine nitration is a prothrombotic risk factor
    • Parastatidis I, Thomson L, Burke A, et al. Fibrinogen beta-chain tyrosine nitration is a prothrombotic risk factor. J Biol Chem. 2008; 283(49):33846-33853.
    • (2008) J Biol Chem , vol.283 , Issue.49 , pp. 33846-33853
    • Parastatidis, I.1    Thomson, L.2    Burke, A.3


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