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Volumn 106, Issue 3, 1999, Pages 809-811

A family with hereditary factor X deficiency with a point mutation Gla32 to Gln in the Gla domain (factor X Tokyo)

Author keywords

Bleeding diathesis; Coagulation factor X; Genetics; Gla domain; Mutation

Indexed keywords

BLOOD CLOTTING FACTOR 10;

EID: 0032877038     PISSN: 00071048     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2141.1999.01614.x     Document Type: Article
Times cited : (16)

References (11)
  • 2
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    • Molecular defect in coagulation factor X 'Friuli' results from substitution of serine for proline at position 343
    • James, H., Girolami, A. & Fair, D.S. (1991) Molecular defect in coagulation factor X 'Friuli' results from substitution of serine for proline at position 343. Blood, 77, 317-323.
    • (1991) Blood , vol.77 , pp. 317-323
    • James, H.1    Girolami, A.2    Fair, D.S.3
  • 3
    • 0028984931 scopus 로고
    • Factor X Ketchikan: A variant molecule in which Gly replaces Gla residue at position 14 in the light chain
    • Kim, D.J., Thompson, A.R. & James, H.L. (1995) Factor X Ketchikan: a variant molecule in which Gly replaces Gla residue at position 14 in the light chain. Human Genetics, 95, 212-214.
    • (1995) Human Genetics , vol.95 , pp. 212-214
    • Kim, D.J.1    Thompson, A.R.2    James, H.L.3
  • 4
    • 0032492690 scopus 로고    scopus 로고
    • Structure/function analysis of recombinant variants of human factor Xa: Factor Xa incorporation into prothrombinase on the thrombin-activated platelet surface is not mimicked by synthetic phospholipid vesicles
    • Larson, P., Camire, R.M., Wong, D., Fasano, N.C., Monroe, D.M., Tracy, P.B. & High, K.A. (1998) Structure/function analysis of recombinant variants of human factor Xa: factor Xa incorporation into prothrombinase on the thrombin-activated platelet surface is not mimicked by synthetic phospholipid vesicles. Biochemistry, 37, 5029-5038.
    • (1998) Biochemistry , vol.37 , pp. 5029-5038
    • Larson, P.1    Camire, R.M.2    Wong, D.3    Fasano, N.C.4    Monroe, D.M.5    Tracy, P.B.6    High, K.A.7
  • 6
    • 0022871419 scopus 로고
    • Gene for human factor X: A blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C
    • Leytus, S.P., Foster, D.C., Kurachi, K. & Davie, E.W. (1986) Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C. Biochemistry, 25, 5098-5102.
    • (1986) Biochemistry , vol.25 , pp. 5098-5102
    • Leytus, S.P.1    Foster, D.C.2    Kurachi, K.3    Davie, E.W.4
  • 7
    • 0022979292 scopus 로고
    • Preparation and properties of derivatives of bovine factor X and factor Xa from which the γ-carboxyglutamic acid containing domain has been removed
    • Morita, T. & Jackson, C.M. (1986) Preparation and properties of derivatives of bovine factor X and factor Xa from which the γ-carboxyglutamic acid containing domain has been removed. Journal of Biological Chemistry, 261, 4015-4023.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 4015-4023
    • Morita, T.1    Jackson, C.M.2
  • 8
    • 0021322174 scopus 로고
    • Comparison of coagulation factor Xa and des-(1 44) factor Xa in the assembly of prothrombinase
    • Skogen, W.F., Esmon, C.T. & Cox, C. (1984) Comparison of coagulation factor Xa and des-(1 44) factor Xa in the assembly of prothrombinase. Journal of Biological Chemistry, 259, 2306-2310.
    • (1984) Journal of Biological Chemistry , vol.259 , pp. 2306-2310
    • Skogen, W.F.1    Esmon, C.T.2    Cox, C.3
  • 9
    • 0009742233 scopus 로고
    • Molecular defect (Gla 26-Asp) and its functional consequences in a hereditary FX deficiency (factor X 'Malmo 4')
    • Wallmark, A., Larson, P., Ljung, R., Monroe, D. & High, K.A. (1991) Molecular defect (Gla 26-Asp) and its functional consequences in a hereditary FX deficiency (factor X 'Malmo 4'). Blood, 78, (Suppl. 1), 229a.
    • (1991) Blood , vol.78 , Issue.SUPPL. 1
    • Wallmark, A.1    Larson, P.2    Ljung, R.3    Monroe, D.4    High, K.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.