메뉴 건너뛰기




Volumn 83, Issue 11, 2008, Pages 884-885

Different genotypes are responsible for the normal Russell viper venom assays seen in some cases of congenital factor X deficiency

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 10; PHOSPHATIDYLETHANOLAMINE; VIPER VENOM;

EID: 55549124574     PISSN: 03618609     EISSN: 10968652     Source Type: Journal    
DOI: 10.1002/ajh.21276     Document Type: Letter
Times cited : (8)

References (19)
  • 1
    • 49149108816 scopus 로고    scopus 로고
    • Congenital factor X deficiencies with a defect only or predominantly in the extrinsic or in the intrinsic system: A critical evaluation
    • Girolami A, Scarparo P, Scandellari R, Allemand E. Congenital factor X deficiencies with a defect only or predominantly in the extrinsic or in the intrinsic system: A critical evaluation. Am J Hematol, 2008;83:668-671.
    • (2008) Am J Hematol , vol.83 , pp. 668-671
    • Girolami, A.1    Scarparo, P.2    Scandellari, R.3    Allemand, E.4
  • 2
    • 0014834193 scopus 로고
    • A new congenital haemorrhagic condition due to the presence of an abnormal factor X (factor X Friuli). A study of large kindred
    • Girolami A, Molaro G, Lazzarin M, et al. A new congenital haemorrhagic condition due to the presence of an abnormal factor X (factor X Friuli). A study of large kindred. Br J Haematol 1970;19:179-192.
    • (1970) Br J Haematol , vol.19 , pp. 179-192
    • Girolami, A.1    Molaro, G.2    Lazzarin, M.3
  • 3
    • 0030804838 scopus 로고    scopus 로고
    • Inherited factor X deficiency: Molecular genetics and pathophysiology
    • Cooper DN, Millar DS, Wacey A, et al. Inherited factor X deficiency: Molecular genetics and pathophysiology. Thromb Haemost 1997;78:161-172.
    • (1997) Thromb Haemost , vol.78 , pp. 161-172
    • Cooper, D.N.1    Millar, D.S.2    Wacey, A.3
  • 6
    • 15644383287 scopus 로고
    • A variant of factor X that is defective only in extrinsic coagulation
    • Bertina RM, Alderkamp GJ, de Nogy E. A variant of factor X that is defective only in extrinsic coagulation. Thromb Haemost 1981;46:88a.
    • (1981) Thromb Haemost , vol.46
    • Bertina, R.M.1    Alderkamp, G.J.2    de Nogy, E.3
  • 7
    • 0023789852 scopus 로고    scopus 로고
    • Factor X Roma: A congenital factor X variant defective at different degrees in the intrinsic and extrinsic activation
    • De Stefano V, Leone G, Ferrelli R, et al. Factor X Roma: A congenital factor X variant defective at different degrees in the intrinsic and extrinsic activation. Br J Haematol 1998;69:387-391.
    • (1998) Br J Haematol , vol.69 , pp. 387-391
    • De Stefano, V.1    Leone, G.2    Ferrelli, R.3
  • 8
    • 0033951964 scopus 로고    scopus 로고
    • The impact of Glu102Lys on the factor X function in a patient with a doubly homozygous factor X deficiency (Gla14Lys and Glu102Lys)
    • Forberg E, Huhmann I, Jimenez-Boj E, Watzke HH. The impact of Glu102Lys on the factor X function in a patient with a doubly homozygous factor X deficiency (Gla14Lys and Glu102Lys). Thromb Haemost 2000;85:234-238.
    • (2000) Thromb Haemost , vol.85 , pp. 234-238
    • Forberg, E.1    Huhmann, I.2    Jimenez-Boj, E.3    Watzke, H.H.4
  • 9
    • 0021957587 scopus 로고
    • Factor X Padua: A new congenital factor X abnormality
    • Girolami A, Vicariotto M, Ruzza G, et al. Factor X Padua: A new congenital factor X abnormality. Acta Haematol 1985;73:31-36.
    • (1985) Acta Haematol , vol.73 , pp. 31-36
    • Girolami, A.1    Vicariotto, M.2    Ruzza, G.3
  • 10
    • 2142662937 scopus 로고    scopus 로고
    • 2+ binding site of factor X protease domain appears to be responsible for the defect in the extrinsic pathway activation of factor X Padua. Clin Appl
    • 2+ binding site of factor X protease domain appears to be responsible for the defect in the extrinsic pathway activation of factor X Padua. Clin Appl Thromb Haemost 2004;10:5-8.
    • (2004) Thromb Haemost , vol.10 , pp. 5-8
    • Girolami, A.1    Vianello, F.2    Cabrio, L.3    Lombardi, A.M.4
  • 11
    • 0026020326 scopus 로고
    • Molecular defect in coagulation factor X Friuli results from a substitution of Serine for Proline at position 343
    • James HL, Girolami A, Fair DS. Molecular defect in coagulation factor X Friuli results from a substitution of Serine for Proline at position 343. Blood 1991;77:317-323.
    • (1991) Blood , vol.77 , pp. 317-323
    • James, H.L.1    Girolami, A.2    Fair, D.S.3
  • 12
    • 0021813191 scopus 로고
    • Normal partial thromboplastin time and associated spindle cell thymoma
    • Nora RE, Bell WR, Noe DA, Sholar PW. Normal partial thromboplastin time and associated spindle cell thymoma. Ann J Med 1985;79:122-126.
    • (1985) Ann J Med , vol.79 , pp. 122-126
    • Nora, R.E.1    Bell, W.R.2    Noe, D.A.3    Sholar, P.W.4
  • 13
    • 0028231019 scopus 로고
    • Five novel point mutations: Two causing haemophilia B and three causing factor X deficiency
    • Odom MW, Leone G, De Stefano V, et al. Five novel point mutations: Two causing haemophilia B and three causing factor X deficiency. Mol Cell Probes 1994;8:63-65.
    • (1994) Mol Cell Probes , vol.8 , pp. 63-65
    • Odom, M.W.1    Leone, G.2    De Stefano, V.3
  • 16
    • 0035864757 scopus 로고    scopus 로고
    • A dysfunctional factor X (factor X San Giovanni Rotondo) present at homozygous and double heterozygous level: Identification of a novel microdeletion (delC556) and missense mutation (Lys(408)->Asn) in the factor X gene. A study of an Italian family
    • Simioni P, Vianello F, Kalafatis M, et al. A dysfunctional factor X (factor X San Giovanni Rotondo) present at homozygous and double heterozygous level: Identification of a novel microdeletion (delC556) and missense mutation (Lys(408)->Asn) in the factor X gene. A study of an Italian family. Thromb Res 2001;101:219-230.
    • (2001) Thromb Res , vol.101 , pp. 219-230
    • Simioni, P.1    Vianello, F.2    Kalafatis, M.3
  • 18
    • 0025282475 scopus 로고
    • Molecular defect (Gla+14-Lys) and its functional consequences in a hereditary factor X deficiency (factor X "Vorarlberg")
    • Watzke HH, Lechner K, Roberts HR, et al. Molecular defect (Gla+14-Lys) and its functional consequences in a hereditary factor X deficiency (factor X "Vorarlberg"). J Biol Chem 1990;265:11982-11989.
    • (1990) J Biol Chem , vol.265 , pp. 11982-11989
    • Watzke, H.H.1    Lechner, K.2    Roberts, H.R.3
  • 19
    • 0028790160 scopus 로고
    • Functional consequences of the Ser 334 - Pro mutation in a human factor X variant (factor X Marseille)
    • Bezeaud A, Miyata T, Helley D, et al. Functional consequences of the Ser 334 - Pro mutation in a human factor X variant (factor X Marseille). Eur J Biochem 1995;234:140-147.
    • (1995) Eur J Biochem , vol.234 , pp. 140-147
    • Bezeaud, A.1    Miyata, T.2    Helley, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.