메뉴 건너뛰기




Volumn 5, Issue 12, 2007, Pages 2340-2343

Which knobs fit into which holes in fibrin polymerization?

Author keywords

[No Author keywords available]

Indexed keywords

FIBRIN; FIBRINOGEN; FIBRINOPEPTIDE A; FIBRINOPEPTIDE B;

EID: 36349029706     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2007.02794.x     Document Type: Note
Times cited : (20)

References (27)
  • 1
    • 17444392120 scopus 로고    scopus 로고
    • Fibrinogen and fibrin
    • In: Parry DAD, Squire J, eds. San Diego: Elsevier
    • Weisel JW. Fibrinogen and fibrin. In: Parry DAD, Squire J, eds. Coiled-Coils, Collagen and Elastomers. San Diego: Elsevier, 2005: 247-99.
    • (2005) Coiled-Coils, Collagen and Elastomers , pp. 247-299
    • Weisel, J.W.1
  • 2
    • 0000946077 scopus 로고
    • Synthetic peptide derivatives that bind to fibrinogen and prevent the polymerization of fibrin monomers
    • Laudano AP, Doolittle RF. Synthetic peptide derivatives that bind to fibrinogen and prevent the polymerization of fibrin monomers. Proc Natl Acad Sci USA 1978; 75: 3085-9.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 3085-3089
    • Laudano, A.P.1    Doolittle, R.F.2
  • 3
    • 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 LR, 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: 2657-67.
    • (2006) Biochemistry , vol.45 , pp. 2657-2667
    • Doolittle, L.R.1    Pandi, L.2
  • 4
    • 34548490739 scopus 로고    scopus 로고
    • The beta-chain hole of fibrinogen with synthetic peptides that differ in their amino termini
    • Doolittle LR, Pandi L. The beta-chain hole of fibrinogen with synthetic peptides that differ in their amino termini. Biochemistry 2007; 46: 10033-8.
    • (2007) Biochemistry , vol.46 , pp. 10033-10038
    • Doolittle, L.R.1    Pandi, L.2
  • 5
    • 0030848486 scopus 로고    scopus 로고
    • Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin
    • Spraggon G, Everse SJ, Doolittle RF. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature 1997; 389: 455-62.
    • (1997) Nature , vol.389 , pp. 455-462
    • Spraggon, G.1    Everse, S.J.2    Doolittle, R.F.3
  • 6
    • 0034687693 scopus 로고    scopus 로고
    • A model for fibrin formation based on crystal structures of fibrinogen and fibrin fragments complexed with specific peptides
    • Yang Z, Mochalkin I, Doolittle LR. A model for fibrin formation based on crystal structures of fibrinogen and fibrin fragments complexed with specific peptides. Proc Natl Acad Sci U S A 2000; 97: 14156-61.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 14156-14161
    • Yang, Z.1    Mochalkin, I.2    Doolittle, L.R.3
  • 7
    • 0026071384 scopus 로고
    • Polymerization site in the beta chain of fibrin: Mapping of the Bbeta1-55 sequence
    • Pandya BV, Gabriel JL, O'Brien J, Budzynski AZ. Polymerization site in the beta chain of fibrin: Mapping of the Bbeta1-55 sequence. Biochemistry 1991; 30: 162-8.
    • (1991) Biochemistry , vol.30 , pp. 162-168
    • Pandya, B.V.1    Gabriel, J.L.2    O'Brien, J.3    Budzynski, A.Z.4
  • 8
    • 0141481996 scopus 로고    scopus 로고
    • Recombinant BbetaArg14His fibrinogen implies participation of N-terminus of Bbeta chain in desA fibrin polymerization
    • Moen JL, Gorkun OV, Weisel JW, Lord ST. Recombinant BbetaArg14His fibrinogen implies participation of N-terminus of Bbeta chain in desA fibrin polymerization. Blood 2003; 102: 2466-71.
    • (2003) Blood , vol.102 , pp. 2466-2471
    • Moen, J.L.1    Gorkun, O.V.2    Weisel, J.W.3    Lord, S.T.4
  • 10
    • 33645211889 scopus 로고    scopus 로고
    • Structural basis for sequential cleavage of fibrinopeptides upon fibrin assembly
    • Pechik I, Yakovlev S, Mosesson MW, Gilliland GL, Medved L. Structural basis for sequential cleavage of fibrinopeptides upon fibrin assembly. Biochemistry 2006; 45: 3588-97.
    • (2006) Biochemistry , vol.45 , pp. 3588-3597
    • Pechik, I.1    Yakovlev, S.2    Mosesson, M.W.3    Gilliland, G.L.4    Medved, L.5
  • 11
    • 0018129207 scopus 로고
    • A two-step fibrinogen-fibrin transition in blood coagulation
    • Blombäck B, Hessel B, Hogg D, Therkildsen L. A two-step fibrinogen-fibrin transition in blood coagulation. Nature 1978; 275: 501-5.
    • (1978) Nature , vol.275 , pp. 501-505
    • Blombäck, B.1    Hessel, B.2    Hogg, D.3    Therkildsen, L.4
  • 12
    • 0022967224 scopus 로고
    • Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides
    • Weisel JW. Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides. Biophys J 1986; 50: 1079-93.
    • (1986) Biophys J , vol.50 , pp. 1079-1093
    • Weisel, J.W.1
  • 13
    • 0018773510 scopus 로고
    • Fibrinopeptide B and aggregation of fibrinogen
    • Shainoff JR, Dardik BN. Fibrinopeptide B and aggregation of fibrinogen. Science 1979; 204: 200-2.
    • (1979) Science , vol.204 , pp. 200-202
    • Shainoff, J.R.1    Dardik, B.N.2
  • 16
    • 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, Shuman H, Weisel JW. Polymerization of fibrin: Specificity, strength, and stability of knob-hole interactions studied at the single-molecule level. Blood 2005; 106: 2944-51.
    • (2005) Blood , vol.106 , pp. 2944-2951
    • Litvinov, R.I.1    Gorkun, O.V.2    Owen, S.F.3    Shuman, H.4    Weisel, J.W.5
  • 17
    • 33846017609 scopus 로고    scopus 로고
    • Polymerization of fibrin: Direct observation and quantification of individual B:b knob-hole interactions
    • Litvinov RI, Gorkun OV, Galanakis DK, Yakovlev S, Medved L, Shuman H, Weisel JW. Polymerization of fibrin: Direct observation and quantification of individual B:b knob-hole interactions. Blood 2007; 109: 130-8.
    • (2007) Blood , vol.109 , 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
  • 19
    • 0027511259 scopus 로고
    • Unusual A alpha 16Arg->Cys dysfibrinogenaemic family: Absence of normal A alpha-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: 67-71.
    • (1993) Blood Coagul Fibrinolysis , vol.4 , pp. 67-71
    • Galanakis, D.1    Spitzer, S.2    Scharrer, I.3
  • 20
    • 34547753415 scopus 로고    scopus 로고
    • Direct evidence for specific interactions of the fibrinogen alpha-C domains with the central E region and with each other
    • Litvinov RI, Yakovlev S, Tsurupa G, Gorkun OV, Medved L, Weisel JW. Direct evidence for specific interactions of the fibrinogen alpha-C domains with the central E region and with each other. Biochemistry 2007; 46: 9133-42.
    • (2007) Biochemistry , vol.46 , pp. 9133-9142
    • Litvinov, R.I.1    Yakovlev, S.2    Tsurupa, G.3    Gorkun, O.V.4    Medved, L.5    Weisel, J.W.6
  • 21
    • 33845413237 scopus 로고    scopus 로고
    • Interactions mediated by the N-terminus of fibrinogen's Bbeta-chain
    • Gorkun OV, Litvinov RI, Veklich YI, Weisel JW. Interactions mediated by the N-terminus of fibrinogen's Bbeta-chain. Biochemistry 2006; 45: 14843-52.
    • (2006) Biochemistry , vol.45 , pp. 14843-14852
    • Gorkun, O.V.1    Litvinov, R.I.2    Veklich, Y.I.3    Weisel, J.W.4
  • 22
    • 0034682822 scopus 로고    scopus 로고
    • Recombinant fibrinogen studies reveal that thrombin specificity dictates order of fibrinopeptide release
    • Mullin JL, Gorkun OV, Binnie CG, Lord ST. Recombinant fibrinogen studies reveal that thrombin specificity dictates order of fibrinopeptide release. J Biol Chem 2000; 275: 25239-46.
    • (2000) J Biol Chem , vol.275 , pp. 25239-25246
    • Mullin, J.L.1    Gorkun, O.V.2    Binnie, C.G.3    Lord, S.T.4
  • 23
    • 9644275586 scopus 로고    scopus 로고
    • Fibrinopeptides and fibrin gel structure
    • Blomback B, Bark N. Fibrinopeptides and fibrin gel structure. Biophys J 2004; 112: 147-51.
    • (2004) Biophys J , vol.112 , pp. 147-151
    • Blomback, B.1    Bark, N.2
  • 24
    • 0033529539 scopus 로고    scopus 로고
    • An integrated study of fibrinogen during blood coagulation
    • Brummel KE, Butenas S, Mann KG. An integrated study of fibrinogen during blood coagulation. J Biol Chem 1999; 274: 22862-70.
    • (1999) J Biol Chem , vol.274 , pp. 22862-22870
    • Brummel, K.E.1    Butenas, S.2    Mann, K.G.3
  • 25
    • 0033537698 scopus 로고    scopus 로고
    • Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide
    • Everse SJ, Spraggon G, Veerapandian L, Doolittle RF. Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide. Biochemistry 1999; 38: 2941-6.
    • (1999) Biochemistry , vol.38 , pp. 2941-2946
    • Everse, S.J.1    Spraggon, G.2    Veerapandian, L.3    Doolittle, R.F.4
  • 26
    • 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, Lord ST. 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: 12124-32.
    • (2002) Biochemistry , vol.41 , pp. 12124-12132
    • Kostelansky, M.S.1    Betts, L.2    Gorkun, O.V.3    Lord, S.T.4
  • 27
    • 1542297673 scopus 로고    scopus 로고
    • Calcium-binding site beta 2, adjacent to the 'b' polymerization site, modulates lateral aggregation of protofibrils during fibrin polymerization
    • Kostelansky MS, Lounes KC, Ping LF, Dickerson SK, Gorkun OV, Lord ST. Calcium-binding site beta 2, adjacent to the 'b' polymerization site, modulates lateral aggregation of protofibrils during fibrin polymerization. Biochemistry 2004; 43: 2475-83.
    • (2004) Biochemistry , vol.43 , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.