메뉴 건너뛰기




Volumn 105, Issue 49, 2008, Pages 19438-19443

Ultrathin self-assembled fibrin sheets

Author keywords

Clot; Fiber; Monomolecular sheet; Network; Thrombus

Indexed keywords

FIBRIN; FIBRIN SHEET; FIBRINOGEN; POLYMER; THROMBIN; UNCLASSIFIED DRUG;

EID: 58049192874     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0804865105     Document Type: Article
Times cited : (29)

References (44)
  • 1
    • 0034964371 scopus 로고    scopus 로고
    • Fibrinogen: Evolution of the structure-function concept
    • Blomback B (2001) Fibrinogen: evolution of the structure-function concept. Ann N Y Acad Sci 936:1-10.
    • (2001) Ann N Y Acad Sci , vol.936 , pp. 1-10
    • Blomback, B.1
  • 2
    • 70249091771 scopus 로고
    • The fibrinogen molecule, its size, shape and mode of polymerization
    • Hall CE, Slayter HS (1959) The fibrinogen molecule, its size, shape and mode of polymerization. J Biophys Biochem Cytol 5:11-17.
    • (1959) J Biophys Biochem Cytol , vol.5 , pp. 11-17
    • Hall, C.E.1    Slayter, H.S.2
  • 3
    • 0018725401 scopus 로고
    • Trinodular structure of fibrinogen. Confirmation by both shadowing and negative stain electron microscopy
    • Fowler WE, Erickson HP (1979) Trinodular structure of fibrinogen. Confirmation by both shadowing and negative stain electron microscopy. J Mol Biol 134:241-249.
    • (1979) J Mol Biol , vol.134 , pp. 241-249
    • Fowler, W.E.1    Erickson, H.P.2
  • 4
    • 0019881596 scopus 로고
    • Morphology of bovine fibrinogen monomers and fibrin oligomers
    • Williams RC (1981) Morphology of bovine fibrinogen monomers and fibrin oligomers. J Mol Biol 150:399-408.
    • (1981) J Mol Biol , vol.150 , pp. 399-408
    • Williams, R.C.1
  • 6
    • 0035940439 scopus 로고    scopus 로고
    • Crystal structure of native chicken fibrinogen at 2.7 A resolution
    • Yang Z, Kollman JM, Pandi L, Doolittle RF (2001) Crystal structure of native chicken fibrinogen at 2.7 A resolution. Biochemistry 40:12515-12523.
    • (2001) Biochemistry , vol.40 , pp. 12515-12523
    • Yang, Z.1    Kollman, J.M.2    Pandi, L.3    Doolittle, R.F.4
  • 7
    • 0001464757 scopus 로고
    • Fibrino-peptide'; new aspects of the fibrinogen-fibrin transformation
    • Lorand L (1951) "Fibrino-peptide'; new aspects of the fibrinogen-fibrin transformation. Nature 167:992-993.
    • (1951) Nature , vol.167 , pp. 992-993
    • Lorand, L.1
  • 8
    • 0000946077 scopus 로고
    • Synthetic peptide derivatives that bind to fibrinogen and prevent the polymerization of fibrin monomers
    • Laudano AP, Doolittle RF (1978) Synthetic peptide derivatives that bind to fibrinogen and prevent the polymerization of fibrin monomers. Proc Natl Acad Sci USA 75:3085-3089.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 3085-3089
    • Laudano, A.P.1    Doolittle, R.F.2
  • 9
    • 0030738474 scopus 로고    scopus 로고
    • The primary fibrin polymerization pocket: Three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro
    • Pratt KP, Cote HC, Chung DW, Stenkamp RE, Davie EW (1997) The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro. Proc Natl Acad Sci USA 94:7176-7181.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7176-7181
    • Pratt, K.P.1    Cote, H.C.2    Chung, D.W.3    Stenkamp, R.E.4    Davie, E.W.5
  • 10
    • 0032537486 scopus 로고    scopus 로고
    • Crystal structure of fragment double-D from human fibrin with two different bound ligands
    • Everse SJ, Spraggon G, Veerapandian L, Riley M, Doolittle RF (1998) Crystal structure of fragment double-D from human fibrin with two different bound ligands. Biochemistry 37:8637-8642.
    • (1998) Biochemistry , vol.37 , pp. 8637-8642
    • Everse, S.J.1    Spraggon, G.2    Veerapandian, L.3    Riley, M.4    Doolittle, R.F.5
  • 11
    • 27644526146 scopus 로고    scopus 로고
    • Polymerization of fibrin: Specificity, strength, and stability of knob-hole interactions studied at the single-molecule level
    • Litvinov RI, Gorkun OV, Owen, SF Suman H, Weisel JW (2005) Polymerization of fibrin: specificity, strength, and stability of knob-hole interactions studied at the single-molecule level. Blood 106:2944-2951.
    • (2005) Blood , vol.106 , pp. 2944-2951
    • Litvinov, R.I.1    Gorkun, O.V.2    Owen, S.F.3    Suman, H.4    Weisel, J.W.5
  • 12
    • 28344448202 scopus 로고    scopus 로고
    • Fibrinogen and fibrin structure and functions
    • Mosesson WW (2005) Fibrinogen and fibrin structure and functions. J Thromb Haemost 3:1894-1904
    • (2005) J Thromb Haemost , vol.3 , pp. 1894-1904
    • Mosesson, W.W.1
  • 13
    • 34247105815 scopus 로고    scopus 로고
    • Fibrinogen and fibrin: Scaffold proteins in hemostasis
    • Lord ST (2007) Fibrinogen and fibrin: scaffold proteins in hemostasis. Curr Opin Hematol. 14:236-241.
    • (2007) Curr Opin Hematol , vol.14 , pp. 236-241
    • Lord, S.T.1
  • 14
    • 34250692159 scopus 로고    scopus 로고
    • Structure of fibrin: Impact on clot stability
    • Weisel JW (2007) Structure of fibrin: impact on clot stability. J Thromb Haemost 5 1:116-124.
    • (2007) J Thromb Haemost , vol.5 , Issue.1 , pp. 116-124
    • Weisel, J.W.1
  • 15
    • 40849126406 scopus 로고    scopus 로고
    • Thrombin generation, fibrin clot formation and hemostasis
    • Wolberg AS, Campbell RA (2008) Thrombin generation, fibrin clot formation and hemostasis. Transfus Apher Sci 38:15-23.
    • (2008) Transfus Apher Sci , vol.38 , pp. 15-23
    • Wolberg, A.S.1    Campbell, R.A.2
  • 16
    • 10044247492 scopus 로고    scopus 로고
    • Visualization and mechanical manipulations of individual fibrin fibers suggest that fiber cross section has fractal dimension 1.3
    • Guthold M, et al. (2004) Visualization and mechanical manipulations of individual fibrin fibers suggest that fiber cross section has fractal dimension 1.3. Biophys J 87:4226-4236.
    • (2004) Biophys J , vol.87 , pp. 4226-4236
    • Guthold, M.1
  • 17
    • 33746872559 scopus 로고    scopus 로고
    • Fibrin fibers have extraordinary extensibility and elasticity
    • Liu W, et al. (2006) Fibrin fibers have extraordinary extensibility and elasticity. Science 313:634.
    • (2006) Science , vol.313 , pp. 634
    • Liu, W.1
  • 18
    • 0017280291 scopus 로고
    • A neutron small-angle scattering study of bovine fibrinogen
    • Marguerie G, Stuhrmann HB (1976) A neutron small-angle scattering study of bovine fibrinogen. J Mol Biol 102:143-156.
    • (1976) J Mol Biol , vol.102 , pp. 143-156
    • Marguerie, G.1    Stuhrmann, H.B.2
  • 20
    • 33847774117 scopus 로고    scopus 로고
    • Forced unfolding of coiled-coils in fibrinogen by single-molecule AFM
    • Brown AE, Litvinov RI, Discher DE, Weisel JW (2007) Forced unfolding of coiled-coils in fibrinogen by single-molecule AFM. Biophys J 92:L39-L41.
    • (2007) Biophys J , vol.92
    • Brown, A.E.1    Litvinov, R.I.2    Discher, D.E.3    Weisel, J.W.4
  • 22
    • 33947443359 scopus 로고
    • Preparation and properties of serum and plasma Proteins. VIII: The conversion of human fibrinogen to fibrin under various conditions
    • Ferry JD, Morrison, PR (1947) Preparation and properties of serum and plasma Proteins. VIII: the conversion of human fibrinogen to fibrin under various conditions J Am Chem Soc 69:388-400.
    • (1947) J Am Chem Soc , vol.69 , pp. 388-400
    • Ferry, J.D.1    Morrison, P.R.2
  • 23
    • 4744363257 scopus 로고
    • Polymerization of fibrinogen
    • Ferry JD (1954) Polymerization of fibrinogen. Physiol Rev 34:753-760.
    • (1954) Physiol Rev , vol.34 , pp. 753-760
    • Ferry, J.D.1
  • 24
    • 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 (1992) Computer modeling of fibrin polymerization Kinetics correlated with electron microscope and turbidity observations: clot structure And assembly are kinetically controlled. Biophys J 63:111-128.
    • (1992) Biophys J , vol.63 , pp. 111-128
    • Weisel, J.W.1    Nagaswami, C.2
  • 26
    • 46749153500 scopus 로고    scopus 로고
    • Dynamic imaging of fibrin network formation correlated with other measures of polymerization
    • Chernysh IN, Weisel JW (2008) Dynamic imaging of fibrin network formation correlated with other measures of polymerization. Blood 111:4854-4861.
    • (2008) Blood , vol.111 , pp. 4854-4861
    • Chernysh, I.N.1    Weisel, J.W.2
  • 27
    • 0001454124 scopus 로고
    • Preparation and properties of serum and plasma proteins. IX: Human fibrin in the form of an elastic film
    • Ferry JD, Morrison PR (1947) Preparation and properties of serum and plasma proteins. IX: human fibrin in the form of an elastic film. J Am Chem Soc 69:400-409.
    • (1947) J Am Chem Soc , vol.69 , pp. 400-409
    • Ferry, J.D.1    Morrison, P.R.2
  • 28
    • 34547942696 scopus 로고    scopus 로고
    • Functional analysis of fibrin {gamma}-chain cross-linking by activated factor XIII: Determination of a cross-linking pattern that maximizes clot stiffness
    • Standeven KF, et al. (2007) Functional analysis of fibrin {gamma}-chain cross-linking by activated factor XIII: determination of a cross-linking pattern that maximizes clot stiffness. Blood 110:902-907.
    • (2007) Blood , vol.110 , pp. 902-907
    • Standeven, K.F.1
  • 29
    • 0011844102 scopus 로고
    • Sequences in the formation of clots from purified bovine fibrinogen and thrombin; a study with the electron microscope
    • Porter KR, Hawn CV (1949) Sequences in the formation of clots from purified bovine fibrinogen and thrombin; a study with the electron microscope. J Exp Med 90:225-232.
    • (1949) J Exp Med , vol.90 , pp. 225-232
    • Porter, K.R.1    Hawn, C.V.2
  • 30
    • 0004731623 scopus 로고
    • Electron microscopy of fibrinogen and fibrin
    • Hall CE (1949) Electron microscopy of fibrinogen and fibrin. J Biol Chem 179:857-865.
    • (1949) J Biol Chem , vol.179 , pp. 857-865
    • Hall, C.E.1
  • 31
    • 0025270643 scopus 로고
    • A new concept of fibrin formation based upon the linear growth of interlacing and branching polymers and molecular alignment into interlocked single-stranded segments
    • Hunziker EB, Straub PW, Haeberli A (1990) A new concept of fibrin formation based upon the linear growth of interlacing and branching polymers and molecular alignment into interlocked single-stranded segments. J Biol Chem 265:7455-7463.
    • (1990) J Biol Chem , vol.265 , pp. 7455-7463
    • Hunziker, E.B.1    Straub, P.W.2    Haeberli, A.3
  • 32
    • 0022354752 scopus 로고
    • Characterization of the kinetic pathway for liberation of fibrinopeptides during assembly of fibrin
    • Lewis SD, Shields PP, Shafer J (1985) Characterization of the kinetic pathway for liberation of fibrinopeptides during assembly of fibrin. J Biol Chem 260:10192-10199.
    • (1985) J Biol Chem , vol.260 , pp. 10192-10199
    • Lewis, S.D.1    Shields, P.P.2    Shafer, J.3
  • 33
    • 18844389128 scopus 로고    scopus 로고
    • Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy
    • Kuhn J, Pollard T (2005) Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy. Biophys J 88:1387-1402.
    • (2005) Biophys J , vol.88 , pp. 1387-1402
    • Kuhn, J.1    Pollard, T.2
  • 34
    • 0024094432 scopus 로고
    • Dynamic instability of individual microtubules analyzed by video light microscopy: Rate constants and transition frequencies
    • Walker RA, et al. (1988) Dynamic instability of individual microtubules analyzed by video light microscopy: rate constants and transition frequencies. J Cell Biol 107(4):1437-1448.
    • (1988) J Cell Biol , vol.107 , Issue.4 , pp. 1437-1448
    • Walker, R.A.1
  • 37
    • 0023039293 scopus 로고
    • Lateral packing of protofibrils in fibrin fibers and fibrinogen polymers
    • Voter WA, Lucaveche C, Blaurock AE, Erickson HP (1986) Lateral packing of protofibrils in fibrin fibers and fibrinogen polymers. Biopolymers 25:2359-2373.
    • (1986) Biopolymers , vol.25 , pp. 2359-2373
    • Voter, W.A.1    Lucaveche, C.2    Blaurock, A.E.3    Erickson, H.P.4
  • 38
    • 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, Wall JS, Hainfeld JF (1993) Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular junction. Blood 82:1517-1521.
    • (1993) Blood , vol.82 , pp. 1517-1521
    • Mosesson, M.W.1    DiOrio, J.P.2    Siebenlist, K.R.3    Wall, J.S.4    Hainfeld, J.F.5
  • 39
    • 33745755197 scopus 로고    scopus 로고
    • Changes in adsorbed fibrinogen upon conversion to fibrin
    • Evans-Nguyen KM, et al. (2006) Changes in adsorbed fibrinogen upon conversion to fibrin. Langmuir 22:5115-5121.
    • (2006) Langmuir , vol.22 , pp. 5115-5121
    • Evans-Nguyen, K.M.1
  • 40
    • 0344584910 scopus 로고    scopus 로고
    • Conformational changes in the plasma protein fibrinogen upon adsorption to graphite and mica investigated by atomic force microscopy
    • Marchin KL, Berrie CL (2003) Conformational changes in the plasma protein fibrinogen upon adsorption to graphite and mica investigated by atomic force microscopy. Langmuir 19:9883-9888.
    • (2003) Langmuir , vol.19 , pp. 9883-9888
    • Marchin, K.L.1    Berrie, C.L.2
  • 41
    • 5444270593 scopus 로고    scopus 로고
    • Time-dependent conformational changes in fibrinogen measured by atomic force microscopy
    • Agnihotri A, Siedlecki CA (2004) Time-dependent conformational changes in fibrinogen measured by atomic force microscopy. Langmuir 20:8846-8852.
    • (2004) Langmuir , vol.20 , pp. 8846-8852
    • Agnihotri, A.1    Siedlecki, C.A.2
  • 42
    • 0032046426 scopus 로고    scopus 로고
    • Real-time observation of plasma protein film formation on well-defined surfaces with scanning force microscopy
    • Ta TC, Sykes MT, McDermott MT (1998) Real-time observation of plasma protein film formation on well-defined surfaces with scanning force microscopy. Langmuir 14:2435-2443.
    • (1998) Langmuir , vol.14 , pp. 2435-2443
    • Ta, T.C.1    Sykes, M.T.2    McDermott, M.T.3
  • 44
    • 33745891494 scopus 로고    scopus 로고
    • Structural changes in the fibrin network of a pretoria family with dysfibrinogenemia: A scanning electron microscopical study
    • Pretorius E, Briedenhann S, Marx J, Franz RC (2006) Structural changes in the fibrin network of a pretoria family with dysfibrinogenemia: a scanning electron microscopical study. Ultrastruct Pathol 30:167-176.
    • (2006) Ultrastruct Pathol , vol.30 , pp. 167-176
    • Pretorius, E.1    Briedenhann, S.2    Marx, J.3    Franz, R.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.