메뉴 건너뛰기




Volumn 78, Issue 1, 1997, Pages 339-343

Antithrombin: Molecular basis of deficiency

Author keywords

[No Author keywords available]

Indexed keywords

ANTITHROMBIN; PROTEINASE;

EID: 0030858409     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0038-1657549     Document Type: Conference Paper
Times cited : (63)

References (35)
  • 1
    • 0014555003 scopus 로고
    • Binding of thrombin to antithrombin III
    • Abildgaard U. Binding of thrombin to antithrombin III. Scand J Clin Lab Invest 1969; 24: 23-7.
    • (1969) Scand J Clin Lab Invest , vol.24 , pp. 23-27
    • Abildgaard, U.1
  • 2
    • 0015821564 scopus 로고
    • The purification and mechanism of action of human antithrombin-heparin cofactor
    • Rosenberg RD, Damus PS. The purification and mechanism of action of human antithrombin-heparin cofactor. J Biol Chem 1973; 248: 6490-505.
    • (1973) J Biol Chem , vol.248 , pp. 6490-6505
    • Rosenberg, R.D.1    Damus, P.S.2
  • 6
    • 0028773279 scopus 로고
    • Biological implications of a 3a structure of dimeric antithrombin
    • Carrell RW, Stein PE, Fermi G, Wardell MR. Biological implications of a 3A structure of dimeric antithrombin. Structure 1994; 2: 257-70.
    • (1994) Structure , vol.2 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4
  • 7
    • 0027190863 scopus 로고
    • Complete nucleotide sequence of the antithrombin gene. Evidence for homologous recombination causing thrombophilia
    • Olds RJ, Lane DA, Chowdhury V, De Stefano V, Leone G, Thein SL. Complete nucleotide sequence of the antithrombin gene. Evidence for homologous recombination causing thrombophilia. Biochemistry 1993; 32: 4216-124.
    • (1993) Biochemistry , vol.32 , pp. 4216-5124
    • Olds, R.J.1    Lane, D.A.2    Chowdhury, V.3    De Stefano, V.4    Leone, G.5    Thein, S.L.6
  • 8
    • 0021863555 scopus 로고
    • Relationship between an enhancer element in the human antithrombin III gene and an immunoglobulin light-chain gene enhancer
    • Prochownik EV. Relationship between an enhancer element in the human antithrombin III gene and an immunoglobulin light-chain gene enhancer. Nature 1985; 316: 845-8.
    • (1985) Nature , vol.316 , pp. 845-848
    • Prochownik, E.V.1
  • 9
    • 0024534371 scopus 로고
    • Different liver nuclear proteins binds to similar DNA sequences in the 5′ flanking regions of three hepatic genes
    • Ochoa A, Brunel F, Mendelzon D, Cohen GN, Zakin MM. Different liver nuclear proteins binds to similar DNA sequences in the 5′ flanking regions of three hepatic genes. Nucleic Acid Res 1989; 17: 119-33.
    • (1989) Nucleic Acid Res , vol.17 , pp. 119-133
    • Ochoa, A.1    Brunel, F.2    Mendelzon, D.3    Cohen, G.N.4    Zakin, M.M.5
  • 10
    • 0029812840 scopus 로고    scopus 로고
    • Ligand-dependent enhancement of human antithrombin gene expression by retinoid X receptor a and thyroid hormone receptor b
    • Niessen RWLM, Rezaee F, Reitsma P, Peters M, De Vijlder JJM. Ligand-dependent enhancement of human antithrombin gene expression by retinoid X receptor a and thyroid hormone receptor b. Biochem J 1996; 318: 263-70.
    • (1996) Biochem J , vol.318 , pp. 263-270
    • Niessen, R.W.L.M.1    Rezaee, F.2    Reitsma, P.3    Peters, M.4    De Vijlder, J.J.M.5
  • 11
    • 0029830748 scopus 로고    scopus 로고
    • Regions flanking exon 1 regulate constitutive expression of the human antithrombin gene
    • Fernandez-Rachubinski FA, Weiner JH, Blajchman MA. Regions flanking exon 1 regulate constitutive expression of the human antithrombin gene. J Biol Chem 1996; 271: 29502-12.
    • (1996) J Biol Chem , vol.271 , pp. 29502-29512
    • Fernandez-Rachubinski, F.A.1    Weiner, J.H.2    Blajchman, M.A.3
  • 12
    • 0029008238 scopus 로고
    • Partial glycosylation of antithrombin III asparagine 135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the b-antithrombin III isoform with enhanced heparin affinity
    • Picard V, Ersdal-Badju E, Bock SC. Partial glycosylation of antithrombin III asparagine 135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the b-antithrombin III isoform with enhanced heparin affinity. Biochemistry 1995; 34: 8433-40.
    • (1995) Biochemistry , vol.34 , pp. 8433-8440
    • Picard, V.1    Ersdal-Badju, E.2    Bock, S.C.3
  • 13
    • 0027374374 scopus 로고
    • Carbohydrate isoforms of anti-thrombin variant N135Q with different heparin affinities
    • Turko IV, Fan B, Gettins PGW. Carbohydrate isoforms of anti-thrombin variant N135Q with different heparin affinities. FEBS Lett 1993; 335: 9-12.
    • (1993) FEBS Lett , vol.335 , pp. 9-12
    • Turko, I.V.1    Fan, B.2    Gettins, P.G.W.3
  • 14
    • 0025866580 scopus 로고
    • Substrate properties of C1 inhibitor Ma (A434E). Genetic and structural evidence suggesting that the 'P12-region' contains critical determinants of serpin inhibitor/substrate status
    • Skriver K, Wikoff WR, Patston PA, Tausk F, Schapira M, Kaplan AP, Bock SC. Substrate properties of C1 inhibitor Ma (A434E). Genetic and structural evidence suggesting that the 'P12-region' contains critical determinants of serpin inhibitor/substrate status. J Biol Chem 1991; 266: 9216-21.
    • (1991) J Biol Chem , vol.266 , pp. 9216-9221
    • Skriver, K.1    Wikoff, W.R.2    Patston, P.A.3    Tausk, F.4    Schapira, M.5    Kaplan, A.P.6    Bock, S.C.7
  • 15
    • 0001973353 scopus 로고
    • Molecular mechanisms of the accelerating effect of heparin on the reactions between antithrombin and the clotting proteinases
    • Lane DA, Lindahl U (eds). Edward Arnold, London
    • Bjork I, Olson ST, Shore JD. Molecular mechanisms of the accelerating effect of heparin on the reactions between antithrombin and the clotting proteinases. In: Heparin: Chemical and Biological Properties, Clinical Applications. Lane DA, Lindahl U (eds). Edward Arnold, London 1989; pp 229-55.
    • (1989) Heparin: Chemical and Biological Properties, Clinical Applications , pp. 229-255
    • Bjork, I.1    Olson, S.T.2    Shore, J.D.3
  • 16
    • 0025831251 scopus 로고
    • Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithromaûn-thrombin reaction. Elucidation from salt concentration effects
    • Olson ST, Bjork I. Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithromaûn-thrombin reaction. Elucidation from salt concentration effects. J Biol Chem 1991; 266: 6353-64.
    • (1991) J Biol Chem , vol.266 , pp. 6353-6364
    • Olson, S.T.1    Bjork, I.2
  • 17
    • 0021344246 scopus 로고
    • Anti-coagulant activities of heparin oligosaccharides and their neutralization by platelet factor 4
    • Lane DA, Denton J, Flynn AM, Thunberg L, Lindahl U. Anti-coagulant activities of heparin oligosaccharides and their neutralization by platelet factor 4. Biochem J 1984; 218: 725-32.
    • (1984) Biochem J , vol.218 , pp. 725-732
    • Lane, D.A.1    Denton, J.2    Flynn, A.M.3    Thunberg, L.4    Lindahl, U.5
  • 18
    • 0019801543 scopus 로고
    • The structure of heparin oligosaccharide fragments with high anti-(factor Xa) activity containing the minimal antithrombin III binding sequence
    • Casu B, Oreste P, Torri G. The structure of heparin oligosaccharide fragments with high anti-(factor Xa) activity containing the minimal antithrombin III binding sequence. Biochem J 1981; 80: 599-609.
    • (1981) Biochem J , vol.80 , pp. 599-609
    • Casu, B.1    Oreste, P.2    Torri, G.3
  • 19
    • 0020108082 scopus 로고
    • Further characterization of the antithrombin-binding sequence in heparin
    • Thunberg L, Backstrom G, Lindahl U. Further characterization of the antithrombin-binding sequence in heparin. Carbohydr Res 1982; 100: 393-410.
    • (1982) Carbohydr Res , vol.100 , pp. 393-410
    • Thunberg, L.1    Backstrom, G.2    Lindahl, U.3
  • 20
    • 0012346044 scopus 로고
    • Evaluation of critical groups required for binding of heparin to antithrombin
    • Atha DH, Stephens AW, Rosenberg RD. Evaluation of critical groups required for binding of heparin to antithrombin. Proc Natl Acad Sci USA 1984; 81: 1030-4.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 1030-1034
    • Atha, D.H.1    Stephens, A.W.2    Rosenberg, R.D.3
  • 21
    • 0027169743 scopus 로고
    • Transmission of conformational change from the heparin binding site to the reactive centre of antithrombin
    • Gettins PGW, Fan B, Crews BC, Turko IV, Olson ST, Streusand VJ. Transmission of conformational change from the heparin binding site to the reactive centre of antithrombin. Biochemistry 1993; 32: 8385-9.
    • (1993) Biochemistry , vol.32 , pp. 8385-8389
    • Gettins, P.G.W.1    Fan, B.2    Crews, B.C.3    Turko, I.V.4    Olson, S.T.5    Streusand, V.J.6
  • 22
    • 0028325823 scopus 로고
    • The conformational change in antithrombin induced by heparin, probed with a monoclonal antibody against the 1C/4B region
    • Dawes J, James K, Lane DA. The conformational change in antithrombin induced by heparin, probed with a monoclonal antibody against the 1C/4B region. Biochemistry 1994; 33: 4375-83.
    • (1994) Biochemistry , vol.33 , pp. 4375-4383
    • Dawes, J.1    James, K.2    Lane, D.A.3
  • 23
    • 0027985254 scopus 로고
    • Lysine-heparin interactions in antithrombin. Properties of K125M and K290M, K294M, K297M variants
    • Fan B, Turko IV, Gettins PGW. Lysine-heparin interactions in antithrombin. Properties of K125M and K290M, K294M, K297M variants. Biochemistry 1994; 33: 14156-61.
    • (1994) Biochemistry , vol.33 , pp. 14156-14161
    • Fan, B.1    Turko, I.V.2    Gettins, P.G.W.3
  • 25
    • 0029897204 scopus 로고    scopus 로고
    • Mechanism of heparin activation of antithrombin. Evidence for reactive centre loop preinsertion with expulsion upon heparin binding
    • Huntington JA, Olson ST, Fan B, Gettins PGW. Mechanism of heparin activation of antithrombin. Evidence for reactive centre loop preinsertion with expulsion upon heparin binding. Biochemistry 1996; 35: 8495-503.
    • (1996) Biochemistry , vol.35 , pp. 8495-8503
    • Huntington, J.A.1    Olson, S.T.2    Fan, B.3    Gettins, P.G.W.4
  • 28
    • 0019579602 scopus 로고
    • Antithrombin III deficiency and thromboembolism
    • Thaler E, Lechner K. Antithrombin III deficiency and thromboembolism. Clin Haematol 1981; 10: 369-90.
    • (1981) Clin Haematol , vol.10 , pp. 369-390
    • Thaler, E.1    Lechner, K.2
  • 32
    • 0027270899 scopus 로고
    • Heparin binding affinity of normal and genetically modified antithrombin III measured using a monoclonal antibody to the heparin binding site of antithrombin III
    • Watton J, Longstaff C, Lane DA, Barrowcliffe TW. Heparin binding affinity of normal and genetically modified antithrombin III measured using a monoclonal antibody to the heparin binding site of antithrombin III. Biochemistry 1993; 32: 7286-93.
    • (1993) Biochemistry , vol.32 , pp. 7286-7293
    • Watton, J.1    Longstaff, C.2    Lane, D.A.3    Barrowcliffe, T.W.4
  • 34
    • 0027945752 scopus 로고
    • Role of N and C terminal amino acids in antithrombin binding to pentasaccharide
    • Mille B, Watton J, Barrowcliffe TW, Mani JC, Lane DA. Role of N and C terminal amino acids in antithrombin binding to pentasaccharide. J Biol Chem 1994; 269: 29435-43.
    • (1994) J Biol Chem , vol.269 , pp. 29435-29443
    • Mille, B.1    Watton, J.2    Barrowcliffe, T.W.3    Mani, J.C.4    Lane, D.A.5
  • 35
    • 0028858172 scopus 로고
    • Intracellular events determine the fate of antithrombin Utah
    • Sheffield WP, Castillo JE, Blajchman MA. Intracellular events determine the fate of antithrombin Utah. Blood 1995; 86: 3461-7.
    • (1995) Blood , vol.86 , pp. 3461-3467
    • Sheffield, W.P.1    Castillo, J.E.2    Blajchman, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.