메뉴 건너뛰기




Volumn 40, Issue 2, 2008, Pages 237-243

Full-length cDNA cloning and protein three-dimensional structure modeling of factor VII of rhesus monkey, Macaca mulatta

Author keywords

FVII; Hemostasis; Prothrombin time test; Rhesus monkey; Three dimensional structure

Indexed keywords

BLOOD CLOTTING FACTOR 7;

EID: 38949179181     PISSN: 10799796     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcmd.2007.08.003     Document Type: Article
Times cited : (6)

References (25)
  • 1
    • 0004330552 scopus 로고
    • Nucleotide sequence of the gene coding for human factor VII, a vitamin K-dependent protein participating in blood coagulation
    • O'Hara P.J., Grant F.J., Haldeman B.A., et al. Nucleotide sequence of the gene coding for human factor VII, a vitamin K-dependent protein participating in blood coagulation. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 5158-5162
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 5158-5162
    • O'Hara, P.J.1    Grant, F.J.2    Haldeman, B.A.3
  • 2
    • 0018731365 scopus 로고
    • Activation of human factor VII in plasma and in purified systems: roles of activated factor IX, kallikrein, and activated factor XII
    • Seligsohn U., Osterud B., Brown S.F., et al. Activation of human factor VII in plasma and in purified systems: roles of activated factor IX, kallikrein, and activated factor XII. J. Clin. Invest. 64 (1979) 1056-1065
    • (1979) J. Clin. Invest. , vol.64 , pp. 1056-1065
    • Seligsohn, U.1    Osterud, B.2    Brown, S.F.3
  • 3
    • 0017200878 scopus 로고
    • Mechanism of activation of bovine factor VII. Products of cleavage by factor Xa
    • Radcliffe R., and Nemerson Y. Mechanism of activation of bovine factor VII. Products of cleavage by factor Xa. J. Biol. Chem. 251 (1976) 4797-4802
    • (1976) J. Biol. Chem. , vol.251 , pp. 4797-4802
    • Radcliffe, R.1    Nemerson, Y.2
  • 4
    • 0017695404 scopus 로고
    • Activation of bovine factor VII (proconvertin) by factor XIIa (activated Hageman factor)
    • Kisiel W., Fujikawa K., and Davie E.W. Activation of bovine factor VII (proconvertin) by factor XIIa (activated Hageman factor). Biochemistry 16 (1977) 4189-4194
    • (1977) Biochemistry , vol.16 , pp. 4189-4194
    • Kisiel, W.1    Fujikawa, K.2    Davie, E.W.3
  • 5
    • 0016631180 scopus 로고
    • Activation and control of factor VII by activated factor X and thrombin. Isolation and characterization of a single chain form of factor VII
    • Radcliffe R., and Nemerson Y. Activation and control of factor VII by activated factor X and thrombin. Isolation and characterization of a single chain form of factor VII. J. Biol. Chem. 250 (1975) 388-395
    • (1975) J. Biol. Chem. , vol.250 , pp. 388-395
    • Radcliffe, R.1    Nemerson, Y.2
  • 6
    • 0015581799 scopus 로고
    • Activation of a proteolytic system by a membrane lipoprotein: mechanism of action of tissue factor
    • Nemerson Y., and Esnouf M.P. Activation of a proteolytic system by a membrane lipoprotein: mechanism of action of tissue factor. Proc. Natl. Acad. Sci. U. S. A. 70 (1973) 310-314
    • (1973) Proc. Natl. Acad. Sci. U. S. A. , vol.70 , pp. 310-314
    • Nemerson, Y.1    Esnouf, M.P.2
  • 7
    • 0037090624 scopus 로고    scopus 로고
    • A frequent human coagulation Factor VII mutation (A294V, c152) in loop 140 s affects the interaction with activators, tissue factor and substrates
    • Toso R., Pinotti M., High K.A., et al. A frequent human coagulation Factor VII mutation (A294V, c152) in loop 140 s affects the interaction with activators, tissue factor and substrates. Biochem. J. 363 (2002) 411-416
    • (2002) Biochem. J. , vol.363 , pp. 411-416
    • Toso, R.1    Pinotti, M.2    High, K.A.3
  • 8
    • 0032530610 scopus 로고    scopus 로고
    • Discordant organ xenotransplantation in primates: world experience and current status
    • Lambrigts, Denis, Sachs, et al. Discordant organ xenotransplantation in primates: world experience and current status. Transplantation 66 (1998) 547-561
    • (1998) Transplantation , vol.66 , pp. 547-561
    • Lambrigts1    Denis2    Sachs3
  • 9
    • 0035753428 scopus 로고    scopus 로고
    • Molecular incompatibilities in hemostasis between swine and men-impact on xenografting
    • Schulte Esch J., Rogiers X., and Robson S.C. Molecular incompatibilities in hemostasis between swine and men-impact on xenografting. Ann. Transplant. 6 (2001) 12-16
    • (2001) Ann. Transplant. , vol.6 , pp. 12-16
    • Schulte Esch, J.1    Rogiers, X.2    Robson, S.C.3
  • 10
    • 0036037340 scopus 로고    scopus 로고
    • Comprehensive analysis of blood coagulation pathways in teleostei: evolution of coagulation factor genes and identification of zebrafish factor VIIi
    • Hanumanthaiah R., Day K., and Jagadeeswaran P. Comprehensive analysis of blood coagulation pathways in teleostei: evolution of coagulation factor genes and identification of zebrafish factor VIIi. Blood Cells Mol. Dis. 29 (2002) 57-68
    • (2002) Blood Cells Mol. Dis. , vol.29 , pp. 57-68
    • Hanumanthaiah, R.1    Day, K.2    Jagadeeswaran, P.3
  • 11
    • 0034518078 scopus 로고    scopus 로고
    • Characterization of Zebrafish full-length prothrombin cDNA and linkage group mapping
    • Jagadeeswaran P., Gregory M., Zhou Y., Zon L., et al. Characterization of Zebrafish full-length prothrombin cDNA and linkage group mapping. Blood Cells Mol. Diseases 26 (2000) 479-489
    • (2000) Blood Cells Mol. Diseases , vol.26 , pp. 479-489
    • Jagadeeswaran, P.1    Gregory, M.2    Zhou, Y.3    Zon, L.4
  • 12
    • 33845979756 scopus 로고    scopus 로고
    • Construction and characterization of a cDNA library from liver tissue of Chinese Banna minipig inbred line
    • Tan W., Chen Y., Zhang L., et al. Construction and characterization of a cDNA library from liver tissue of Chinese Banna minipig inbred line. Transplant. Proc. 38 (2006) 2264-2266
    • (2006) Transplant. Proc. , vol.38 , pp. 2264-2266
    • Tan, W.1    Chen, Y.2    Zhang, L.3
  • 13
    • 33846579240 scopus 로고    scopus 로고
    • Full-length cDNA cloning and protein three-dimensional structure modeling of porcine prothrombin
    • Chen Y., Tan W., Lu X., et al. Full-length cDNA cloning and protein three-dimensional structure modeling of porcine prothrombin. Blood Cells Mol. Dis. 38 (2007) 93-99
    • (2007) Blood Cells Mol. Dis. , vol.38 , pp. 93-99
    • Chen, Y.1    Tan, W.2    Lu, X.3
  • 14
    • 0043133845 scopus 로고    scopus 로고
    • The Drosophila dysfusion basic helix-loop-helix (bHLH)-PAS gene controls tracheal fusion and levels of the trachealess bHLH-PAS protein
    • Jiang L., and Crews S.T. The Drosophila dysfusion basic helix-loop-helix (bHLH)-PAS gene controls tracheal fusion and levels of the trachealess bHLH-PAS protein. Mol. Cell. Biol. 23 (2003) 5625-5637
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5625-5637
    • Jiang, L.1    Crews, S.T.2
  • 15
    • 38949181065 scopus 로고    scopus 로고
    • Asymptomatic factor VII Padua in African Americans
    • Tidd T.M., Ptashkin B., and Pollak E.S. Asymptomatic factor VII Padua in African Americans. Blood 106 (2005) 4069
    • (2005) Blood , vol.106 , pp. 4069
    • Tidd, T.M.1    Ptashkin, B.2    Pollak, E.S.3
  • 16
  • 17
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31 (2003) 3381-3385
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 18
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 19
    • 0029861673 scopus 로고    scopus 로고
    • Molecular mechanism of tissue factor-mediated acceleration of factor VIIa activity
    • Higashi S., Matsumoto N., and Iwanaga S. Molecular mechanism of tissue factor-mediated acceleration of factor VIIa activity. J. Biol. Chem. 271 (1996) 26569-26574
    • (1996) J. Biol. Chem. , vol.271 , pp. 26569-26574
    • Higashi, S.1    Matsumoto, N.2    Iwanaga, S.3
  • 20
    • 0029992658 scopus 로고    scopus 로고
    • Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease factor VIIa
    • Dickinson C.D., Kelly C.R., and Ruf W. Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease factor VIIa. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 14379-14384
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 14379-14384
    • Dickinson, C.D.1    Kelly, C.R.2    Ruf, W.3
  • 21
    • 0029093452 scopus 로고
    • Analysis of the factor VIIa binding site on human tissue factor: effects of tissue factor mutations on the kinetics and thermodynamics of binding
    • Kelley R.F., Costas K.E., O'Connell M.P., and Lazarus R.A. Analysis of the factor VIIa binding site on human tissue factor: effects of tissue factor mutations on the kinetics and thermodynamics of binding. Biochemistry 34 (1995) 10383-10392
    • (1995) Biochemistry , vol.34 , pp. 10383-10392
    • Kelley, R.F.1    Costas, K.E.2    O'Connell, M.P.3    Lazarus, R.A.4
  • 22
    • 0028299054 scopus 로고
    • Mutational mapping of functional residues in tissue factor: identification of factor VII recognition determinants in both structural modules of the predicted cytokine receptor homology domain
    • Ruf W., Schullek J.R., Stone M.J., and Edgington T.S. Mutational mapping of functional residues in tissue factor: identification of factor VII recognition determinants in both structural modules of the predicted cytokine receptor homology domain. Biochemistry 33 (1994) 1565-1572
    • (1994) Biochemistry , vol.33 , pp. 1565-1572
    • Ruf, W.1    Schullek, J.R.2    Stone, M.J.3    Edgington, T.S.4
  • 23
    • 0036265909 scopus 로고    scopus 로고
    • Structure, function, and activation of coagulation factor VII
    • Eigenbrot C. Structure, function, and activation of coagulation factor VII. Curr. Prot. Peptide Sc. 3 (2002) 287-299
    • (2002) Curr. Prot. Peptide Sc. , vol.3 , pp. 287-299
    • Eigenbrot, C.1
  • 24
    • 0029926396 scopus 로고    scopus 로고
    • The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor
    • Banner D.W., D'Arcy A., Chene C., et al. The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor. Nature 380 (1996) 41-46
    • (1996) Nature , vol.380 , pp. 41-46
    • Banner, D.W.1    D'Arcy, A.2    Chene, C.3
  • 25
    • 0028982831 scopus 로고
    • High affinity Ca(2+)-binding site in the serine protease domain of human factor VIIa and its role in tissue factor binding and development of catalytic activity
    • Sabharwal A.K., Birktoft J.J., Gorka J., et al. High affinity Ca(2+)-binding site in the serine protease domain of human factor VIIa and its role in tissue factor binding and development of catalytic activity. J. Biol. Chem. 270 (1995) 15523-15530
    • (1995) J. Biol. Chem. , vol.270 , pp. 15523-15530
    • Sabharwal, A.K.1    Birktoft, J.J.2    Gorka, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.