메뉴 건너뛰기




Volumn 90, Issue 10, 1997, Pages 3967-3977

Mutations in the human factor XII gene

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; BLOOD CLOTTING FACTOR 12; GLUTAMINE; LEUCINE; METHIONINE;

EID: 0030812723     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (55)

References (40)
  • 2
    • 0027524482 scopus 로고
    • Structural biology cellular interactions and pathophysiology of the contact system
    • Wachtfogel Y, DeLa Cadena RA, Colman RW: Structural biology cellular interactions and pathophysiology of the contact system. Thromb Res 72:1, 1993
    • (1993) Thromb Res , vol.72 , pp. 1
    • Wachtfogel, Y.1    DeLa Cadena, R.A.2    Colman, R.W.3
  • 3
    • 0024853669 scopus 로고
    • Coagulation factor XII (Hageman factor) Washington D.C.: Inactive factor XIIa results from Cys-571-Ser substitution
    • Miyata T, Kawabata SI, Iwanaga S, Takahashi I, Alving B, Saito H: Coagulation factor XII (Hageman factor) Washington D.C.: Inactive factor XIIa results from Cys-571-Ser substitution. Proc Natl Acad Sci USA 86:8319, 1989
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 8319
    • Miyata, T.1    Kawabata, S.I.2    Iwanaga, S.3    Takahashi, I.4    Alving, B.5    Saito, H.6
  • 4
    • 0028017572 scopus 로고
    • Coagulation factor XII Locarno: The functional defect is caused by the amino acid substitution Arg 353 → Pro leading to loss of a kallikrein cleavage site
    • Kremer Hovinga J, Schaller J, Stricker H, Wuillemin WA, Furlan M, Lämmle B: Coagulation factor XII Locarno: The functional defect is caused by the amino acid substitution Arg 353 → Pro leading to loss of a kallikrein cleavage site. Blood 84:1173, 1994
    • (1994) Blood , vol.84 , pp. 1173
    • Kremer Hovinga, J.1    Schaller, J.2    Stricker, H.3    Wuillemin, W.A.4    Furlan, M.5    Lämmle, B.6
  • 5
    • 0022407061 scopus 로고
    • Characterization of human blood coagulation factor XII cDNA. Prediction of the primary structure of factor XII and the tertiary structure of beta-factor XIIa
    • Cool DE, Edgell CJ, Louie GV, Zoller MJ, Brayer GD, MacGillivray RT: Characterization of human blood coagulation factor XII cDNA. Prediction of the primary structure of factor XII and the tertiary structure of beta-factor XIIa. J Biol Chem 260:13666, 1985
    • (1985) J Biol Chem , vol.260 , pp. 13666
    • Cool, D.E.1    Edgell, C.J.2    Louie, G.V.3    Zoller, M.J.4    Brayer, G.D.5    MacGillivray, R.T.6
  • 7
    • 0023265140 scopus 로고
    • Characterization of the human blood coagulation factor XII gene: Intron/exon gene organization and analysis of the 5-prime flanking region
    • Cool DE, MacGillivray RTA: Characterization of the human blood coagulation factor XII gene: Intron/exon gene organization and analysis of the 5-prime flanking region. J Biol Chem 262:13662, 1987
    • (1987) J Biol Chem , vol.262 , pp. 13662
    • Cool, D.E.1    MacGillivray, R.T.A.2
  • 10
    • 0029944742 scopus 로고    scopus 로고
    • A novel 5′upstream mutation in the factor XII gene is associated with a TaqI restriction site in an Alu repeat in factor XII-deficient patients
    • Hofferbert S, Müller J, Köstering H, von Ohlen WD, Schloesser M: A novel 5′upstream mutation in the factor XII gene is associated with a TaqI restriction site in an Alu repeat in factor XII-deficient patients. Hum Genet 97:838, 1996
    • (1996) Hum Genet , vol.97 , pp. 838
    • Hofferbert, S.1    Müller, J.2    Köstering, H.3    Von Ohlen, W.D.4    Schloesser, M.5
  • 11
    • 0029075651 scopus 로고
    • The novel acceptor splice site mutation 11396(G → A) in the factor XII gene causes a truncated transcript in cross-reacting material negative patients
    • Schloesser M, Hofferbert S, Bartz U, Lutze G, Lämmle B, Engel W: The novel acceptor splice site mutation 11396(G → A) in the factor XII gene causes a truncated transcript in cross-reacting material negative patients. Hum Mol Genet 4:1235, 1995
    • (1995) Hum Mol Genet , vol.4 , pp. 1235
    • Schloesser, M.1    Hofferbert, S.2    Bartz, U.3    Lutze, G.4    Lämmle, B.5    Engel, W.6
  • 12
    • 0026333358 scopus 로고
    • A cystic fibrosis patient with the nonsense mutation G542X and the splice site mutation 1717-1
    • Schloesser M, Arleth S, Lenz U, Bertele RM, Reiss J: A cystic fibrosis patient with the nonsense mutation G542X and the splice site mutation 1717-1. J Med Genet 28:878, 1991
    • (1991) J Med Genet , vol.28 , pp. 878
    • Schloesser, M.1    Arleth, S.2    Lenz, U.3    Bertele, R.M.4    Reiss, J.5
  • 13
    • 0027473306 scopus 로고
    • Factor XII (Hageman) deficiency in women with habitual abortion: A new subpopulation of recurrent aborters?
    • Braulke I, Pruggmayer M, Melloh P, Hinney B, Koestering H, Guenther E: Factor XII (Hageman) deficiency in women with habitual abortion: A new subpopulation of recurrent aborters? Fertil Steril 59:98, 1993
    • (1993) Fertil Steril , vol.59 , pp. 98
    • Braulke, I.1    Pruggmayer, M.2    Melloh, P.3    Hinney, B.4    Koestering, H.5    Guenther, E.6
  • 15
    • 0026065260 scopus 로고
    • Thromboembolism and bleeding tendency in congenital factor XII deficiency - A study on 74 subjects from 14 Swiss families
    • Lämmle B, Wuillemin WA, Huber I, Krauskopf M, Zürcher C, Pflugshaupt R, Furlan M: Thromboembolism and bleeding tendency in congenital factor XII deficiency - A study on 74 subjects from 14 Swiss families. Thromb Haemost 65:117, 1991
    • (1991) Thromb Haemost , vol.65 , pp. 117
    • Lämmle, B.1    Wuillemin, W.A.2    Huber, I.3    Krauskopf, M.4    Zürcher, C.5    Pflugshaupt, R.6    Furlan, M.7
  • 16
    • 0026803207 scopus 로고
    • The prevalence of factor XII deficiency in 103 anticoagulated outpatients suffering from recurrent venous and/or arterial thromboembolism
    • Halbmayer WM, Mannhalter C, Feichtinger C, Rubi K, Fischer M: The prevalence of factor XII deficiency in 103 anticoagulated outpatients suffering from recurrent venous and/or arterial thromboembolism. Thromb Haemost 68:285, 1992
    • (1992) Thromb Haemost , vol.68 , pp. 285
    • Halbmayer, W.M.1    Mannhalter, C.2    Feichtinger, C.3    Rubi, K.4    Fischer, M.5
  • 17
    • 0027346111 scopus 로고
    • Untersuchungen zur Genetik des Faktor-XII-Mangels
    • Kretschmer V, Stangel W, Eckstein R (eds): Freiburg, Germany, Karger
    • Kemptner B, Rueth S, Epple I, Lohse P: Untersuchungen zur Genetik des Faktor-XII-Mangels, in Kretschmer V, Stangel W, Eckstein R (eds): Beitr Infusionsther: 31. Freiburg, Germany, Karger, 1993, p 174
    • (1993) Beitr Infusionsther: 31 , pp. 174
    • Kemptner, B.1    Rueth, S.2    Epple, I.3    Lohse, P.4
  • 18
    • 0026794668 scopus 로고
    • The mutational spectrum of single base-pair substitutions in mRNA splice site junctions of human genes: Causes and consequences
    • Krawczak M, Reiss J, Cooper DN: The mutational spectrum of single base-pair substitutions in mRNA splice site junctions of human genes: Causes and consequences. Hum Genet 90:41, 1992
    • (1992) Hum Genet , vol.90 , pp. 41
    • Krawczak, M.1    Reiss, J.2    Cooper, D.N.3
  • 20
    • 0026672907 scopus 로고
    • Primary structure of guinea-pig Hageman factor: Sequence around the cleavage site differs from the human molecule
    • Semba U, Yamamoto T, Kunisada T, Shibuya Y, Tanase S, Kambara T, Okabe H: Primary structure of guinea-pig Hageman factor: Sequence around the cleavage site differs from the human molecule. Biochim Biophys Acta 1159:113, 1992
    • (1992) Biochim Biophys Acta , vol.1159 , pp. 113
    • Semba, U.1    Yamamoto, T.2    Kunisada, T.3    Shibuya, Y.4    Tanase, S.5    Kambara, T.6    Okabe, H.7
  • 21
    • 0028235065 scopus 로고
    • Primary structure of bovine Hageman factor (blood coagulation factor XII): Comparison with human and guinea pig molecules
    • Shibuya Y, Semba U, Okabe H, Kambara T, Yamamoto T: Primary structure of bovine Hageman factor (blood coagulation factor XII): Comparison with human and guinea pig molecules. Biochem Biophys Acta 1206:63, 1994
    • (1994) Biochem Biophys Acta , vol.1206 , pp. 63
    • Shibuya, Y.1    Semba, U.2    Okabe, H.3    Kambara, T.4    Yamamoto, T.5
  • 22
  • 23
    • 0025009050 scopus 로고
    • Isolation and nucleotide sequence of cDNA clone for bovine pancreatic anionic trypsinogen. Structural identity within the trypsin family
    • Huerou L, Wicker C, Guilloteau P, Toullec R, Puigserver A: Isolation and nucleotide sequence of cDNA clone for bovine pancreatic anionic trypsinogen. Structural identity within the trypsin family. Eur J Biochem 193:767, 1990
    • (1990) Eur J Biochem , vol.193 , pp. 767
    • Huerou, L.1    Wicker, C.2    Guilloteau, P.3    Toullec, R.4    Puigserver, A.5
  • 24
    • 0022728916 scopus 로고
    • Isolation and expression in Escherichia coli of a cDNA clone encoding porcine pancreatic elastase
    • Shirasu Y, Yoshida H, Mikayama T, Matsuki S, Tanaka J, Ikenaga H: Isolation and expression in Escherichia coli of a cDNA clone encoding porcine pancreatic elastase. J Biochem 99:1707, 1986
    • (1986) J Biochem , vol.99 , pp. 1707
    • Shirasu, Y.1    Yoshida, H.2    Mikayama, T.3    Matsuki, S.4    Tanaka, J.5    Ikenaga, H.6
  • 25
    • 0019873323 scopus 로고
    • Refined crystal structure of gamma chymotrypsin at 1.9 A resolution. Comparison with other pancreatic serine proteases
    • Cohen GH, Silverton EW, Davies DR: Refined crystal structure of gamma chymotrypsin at 1.9 A resolution. Comparison with other pancreatic serine proteases. J Mol Biol 148:449, 1981
    • (1981) J Mol Biol , vol.148 , pp. 449
    • Cohen, G.H.1    Silverton, E.W.2    Davies, D.R.3
  • 27
    • 0027422822 scopus 로고
    • Characterization of Xenopus laevis complement factor I structure - Conservation of modular structure except for an unusual insert not present in human factor I
    • Kunnath-Muglia LM, Chang GH, Sim RB, Day AJ, Ezekowitz RA: Characterization of Xenopus laevis complement factor I structure - Conservation of modular structure except for an unusual insert not present in human factor I. Mol Immunol 30:1249, 1993
    • (1993) Mol Immunol , vol.30 , pp. 1249
    • Kunnath-Muglia, L.M.1    Chang, G.H.2    Sim, R.B.3    Day, A.J.4    Ezekowitz, R.A.5
  • 28
    • 0023105043 scopus 로고
    • Characterization of primary amino acid sequence of human complement control protein factor I from an analysis of cDNA clones
    • Catterall CF, Lyons A, Sim RB, Day AJ, Harris TJ: Characterization of primary amino acid sequence of human complement control protein factor I from an analysis of cDNA clones. Biochem J 242:849, 1987
    • (1987) Biochem J , vol.242 , pp. 849
    • Catterall, C.F.1    Lyons, A.2    Sim, R.B.3    Day, A.J.4    Harris, T.J.5
  • 30
    • 0029153564 scopus 로고
    • The consensus sequence of a major Alu subfamily contains a functional retinoic acid response element
    • Vansant G, Reynolds WF: The consensus sequence of a major Alu subfamily contains a functional retinoic acid response element. Proc Natl Acad Sci USA 92:8229, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8229
    • Vansant, G.1    Reynolds, W.F.2
  • 32
    • 0028857910 scopus 로고
    • An active-site mutation in the human immunodeficiency virus type 1 proteinase (PR) causes reduced PR activity and loss of PR-mediated cytotoxicity without apparent effect on virus maturation and infectivity
    • Konvalinka J, Litterst MA, Welker R, Kottier H, Rippmann F, Heuser AM, Krausslich HG: An active-site mutation in the human immunodeficiency virus type 1 proteinase (PR) causes reduced PR activity and loss of PR-mediated cytotoxicity without apparent effect on virus maturation and infectivity. J Virol 69:7180, 1995
    • (1995) J Virol , vol.69 , pp. 7180
    • Konvalinka, J.1    Litterst, M.A.2    Welker, R.3    Kottier, H.4    Rippmann, F.5    Heuser, A.M.6    Krausslich, H.G.7
  • 33
    • 0023204278 scopus 로고
    • The catalytical role of the active site aspartic acid in serine proteases
    • Craik CS, Roczniak S, Largman C, Rutter WJ: The catalytical role of the active site aspartic acid in serine proteases. Science 237:909, 1987
    • (1987) Science , vol.237 , pp. 909
    • Craik, C.S.1    Roczniak, S.2    Largman, C.3    Rutter, W.J.4
  • 34
    • 0026766968 scopus 로고
    • Transcriptional and posttranscriptional activation of urokinase plasminogen activator gene expression in metastatic tumor cells
    • Henderson BR, Tansey WP, Phillips SM, Ramshaw IA, Kefford RF: Transcriptional and posttranscriptional activation of urokinase plasminogen activator gene expression in metastatic tumor cells. Cancer Res 52:2489, 1992
    • (1992) Cancer Res , vol.52 , pp. 2489
    • Henderson, B.R.1    Tansey, W.P.2    Phillips, S.M.3    Ramshaw, I.A.4    Kefford, R.F.5
  • 35
    • 0021817726 scopus 로고
    • Differential regulation of trypsinogen mRNA translation: Full-length mRNA sequences encoding two oppositely charged trypsinogen isoenzymes in the dog pancreas
    • Pinsky SD, LaForge KS, Scheele G: Differential regulation of trypsinogen mRNA translation: Full-length mRNA sequences encoding two oppositely charged trypsinogen isoenzymes in the dog pancreas. Mol Cell Biol 5:2669, 1985
    • (1985) Mol Cell Biol , vol.5 , pp. 2669
    • Pinsky, S.D.1    LaForge, K.S.2    Scheele, G.3
  • 36
    • 0020565895 scopus 로고
    • Thrombosis or myocardial infarction in congenital clotting factor abnormalities and chronic thrombocytopenias: A report of 21 patients and a review of 50 previously reported cases
    • Baltimore
    • Goodnough LT, Saito M, Radnoff OD: Thrombosis or myocardial infarction in congenital clotting factor abnormalities and chronic thrombocytopenias: A report of 21 patients and a review of 50 previously reported cases. Medicine (Baltimore) 62:248, 1983
    • (1983) Medicine , vol.62 , pp. 248
    • Goodnough, L.T.1    Saito, M.2    Radnoff, O.D.3
  • 37
    • 0003371207 scopus 로고
    • Factor XII activity and antigen concentrations in patients suffering from recurrent thrombosis
    • Mannhalter C, Fischer M, Hopmeier P, Deutsch E: Factor XII activity and antigen concentrations in patients suffering from recurrent thrombosis. Fibrinolysis 1:259, 1987
    • (1987) Fibrinolysis , vol.1 , pp. 259
    • Mannhalter, C.1    Fischer, M.2    Hopmeier, P.3    Deutsch, E.4
  • 38
    • 0026458603 scopus 로고
    • Factor XII clotting activity and antigen levels in patients with thromboembolic disease
    • von Känel R, Wuillemin WA, Furlan M, Lämmle B: Factor XII clotting activity and antigen levels in patients with thromboembolic disease. Blood Coagul Fibrinolysis 3:555, 1992
    • (1992) Blood Coagul Fibrinolysis , vol.3 , pp. 555
    • Von Känel, R.1    Wuillemin, W.A.2    Furlan, M.3    Lämmle, B.4
  • 40
    • 0028234054 scopus 로고
    • John Hageman's factor and deep-vein thrombosis: Leiden Thrombophilia Study
    • Koster T, Rosendaal FR, Briet E, Vandenbroucke JP: John Hageman's factor and deep-vein thrombosis: Leiden Thrombophilia Study. Br J Haematol 87:422, 1994
    • (1994) Br J Haematol , vol.87 , pp. 422
    • Koster, T.1    Rosendaal, F.R.2    Briet, E.3    Vandenbroucke, J.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.