메뉴 건너뛰기




Volumn 78, Issue 5, 2007, Pages 410-416

A novel fibrinogen variant - Praha I: Hypofibrinogenemia associated with γ Gly351Ser substitution

Author keywords

Fibrinogen; Hypofibrinogenemia; Missense mutation

Indexed keywords

FIBRINOGEN; FIBRINOPEPTIDE; PRAHA 1; UNCLASSIFIED DRUG;

EID: 34147187348     PISSN: 09024441     EISSN: 16000609     Source Type: Journal    
DOI: 10.1111/j.1600-0609.2007.00838.x     Document Type: Article
Times cited : (12)

References (24)
  • 1
    • 77957222558 scopus 로고
    • Fibrinogen, fibrin and factor XIII
    • Zwaal RFA, Hemker HC, eds, Amsterdam: Elsevier Science Publishers
    • Henschen AH, McDonagh J. Fibrinogen, fibrin and factor XIII. In: Zwaal RFA, Hemker HC, eds. Blood Coagulation. Amsterdam: Elsevier Science Publishers, 1986:171-241.
    • (1986) Blood Coagulation , pp. 171-241
    • Henschen, A.H.1    McDonagh, J.2
  • 3
    • 0036707542 scopus 로고    scopus 로고
    • Novel fibrinogen γ375 Arg → Trp mutation (fibrinogen Aguadilla) causes hepatic endoplasmic reticulum storage and hypofibrinogenemia
    • Brennan SO, Maghzal G, Shneider BL, Gordon R, Magid MS, George PM. Novel fibrinogen γ375 Arg → Trp mutation (fibrinogen Aguadilla) causes hepatic endoplasmic reticulum storage and hypofibrinogenemia. Hepatology 2002;36:652-8.
    • (2002) Hepatology , vol.36 , pp. 652-658
    • Brennan, S.O.1    Maghzal, G.2    Shneider, B.L.3    Gordon, R.4    Magid, M.S.5    George, P.M.6
  • 4
    • 0033882702 scopus 로고    scopus 로고
    • Fibrinogen Brescia: Hepatic endoplasmic reticulum storage and hypofibrinogenemia because of a γ284 Gly → Arg mutation
    • Brennan SO, Wyatt JM, Medicina D, Callea F, George PM. Fibrinogen Brescia: hepatic endoplasmic reticulum storage and hypofibrinogenemia because of a γ284 Gly → Arg mutation. Am J Pathol 2000;157:189- 96.
    • (2000) Am J Pathol , vol.157 , pp. 189-196
    • Brennan, S.O.1    Wyatt, J.M.2    Medicina, D.3    Callea, F.4    George, P.M.5
  • 6
    • 10444250235 scopus 로고    scopus 로고
    • Hypofibrinogenaemia associated with a novel heterozygous γ289 Ala → Val substitution (fibrinogen Dorfen)
    • Dear A, Brennan SO, Dempfle CE, Kirschstein W, George PM. Hypofibrinogenaemia associated with a novel heterozygous γ289 Ala → Val substitution (fibrinogen Dorfen). Thromb Haemost 2004;92:1291- 5.
    • (2004) Thromb Haemost , vol.92 , pp. 1291-1295
    • Dear, A.1    Brennan, S.O.2    Dempfle, C.E.3    Kirschstein, W.4    George, P.M.5
  • 8
    • 33745551242 scopus 로고
    • Schnell-methode zur Bestimmung des Fibrinogens
    • Clauss A. Gerinnungsphysiologische Schnell-methode zur Bestimmung des Fibrinogens. Acta Haematol 1957;17:237-46.
    • (1957) Acta Haematol , vol.17 , pp. 237-246
    • Gerinnungsphysiologische, C.A.1
  • 9
    • 0028881825 scopus 로고
    • Aberrant hepatic processing causes removal of activation peptide and primary polymerization site from fibrinogen Canterbury (Aα Val → Asp)
    • Brennan SO, Hammonds B, George PM. Aberrant hepatic processing causes removal of activation peptide and primary polymerization site from fibrinogen Canterbury (Aα Val → Asp). J Clin Invest 1995;96:2854- 8.
    • (1995) J Clin Invest , vol.96 , pp. 2854-2858
    • Brennan, S.O.1    Hammonds, B.2    George, P.M.3
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 0024520910 scopus 로고
    • Determination of fibrinopeptides by high performance liquid chromatography
    • Suttnar J, Dyr JE, Fořtová H, Pristach J. Determination of fibrinopeptides by high performance liquid chromatography. Biochem Clin Bohemoslov 1989;18:17-25.
    • (1989) Biochem Clin Bohemoslov , vol.18 , pp. 17-25
    • Suttnar, J.1    Dyr, J.E.2    Fořtová, H.3    Pristach, J.4
  • 12
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M. Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels. Anal Chem 1996;68:850-8.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 13
    • 0030848486 scopus 로고    scopus 로고
    • Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin
    • Spraggon G, Everse SJ, Doolittle RF. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature 1997;389:455-62.
    • (1997) Nature , vol.389 , pp. 455-462
    • Spraggon, G.1    Everse, S.J.2    Doolittle, R.F.3
  • 15
    • 34147145115 scopus 로고    scopus 로고
    • Available at:, last accessed September 17, 2006
    • Fibrinogen Variants. Available at: http://www.geht.org/fr/pages/ pratiqueBase_UK_Bgamma.html (last accessed September 17, 2006).
    • Fibrinogen Variants
  • 16
    • 33947290263 scopus 로고
    • γ-γ cross-linking sites in human and bovine fibrinogen
    • Chen R, Doolittle RF. γ-γ cross-linking sites in human and bovine fibrinogen. Biochemistry 1971;10:4486-91.
    • (1971) Biochemistry , vol.10 , pp. 4486-4491
    • Chen, R.1    Doolittle, R.F.2
  • 17
    • 13244252406 scopus 로고    scopus 로고
    • Fibrinogen Mannheim II: A novel γ307 His → Tyr substitution in the γD domain causes hypofibrinogenemia
    • Dear A, Dempfle CE, Brennan SO, Kirschstein W, George PM. Fibrinogen Mannheim II: a novel γ307 His → Tyr substitution in the γD domain causes hypofibrinogenemia. J Thromb Haemost 2004;2:2194-9.
    • (2004) J Thromb Haemost , vol.2 , pp. 2194-2199
    • Dear, A.1    Dempfle, C.E.2    Brennan, S.O.3    Kirschstein, W.4    George, P.M.5
  • 18
    • 34147173535 scopus 로고    scopus 로고
    • Swiss - Prot Protein Knowledgebase at ExPASy Proteomics Server. Available at: http://www.expasy.ch, accession numbers P12799, P02679, Q8VCM7, P04115, P02680, P17634 (last accessed September 20, 2006).
    • Swiss - Prot Protein Knowledgebase at ExPASy Proteomics Server. Available at: http://www.expasy.ch, accession numbers P12799, P02679, Q8VCM7, P04115, P02680, P17634 (last accessed September 20, 2006).
  • 20
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson JS. The anatomy and taxonomy of protein structure. Adv Protein Chem 1981;34:167-339.
    • (1981) Adv Protein Chem , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 22
    • 0029785476 scopus 로고    scopus 로고
    • In vitro assembly of the component chains of fibrinogen requires endoplasmic reticulum factors
    • Roy S, Sun A, Redman C. In vitro assembly of the component chains of fibrinogen requires endoplasmic reticulum factors. J Biol Chem 1996;271:24544-50.
    • (1996) J Biol Chem , vol.271 , pp. 24544-24550
    • Roy, S.1    Sun, A.2    Redman, C.3
  • 23
    • 0027418768 scopus 로고
    • Biosynthesis of human fibrinogen. Subunit interactions and potential intermediates in assembly
    • Huang S, Mulvihill ER, Farrell DH, Chung DW, Davie EW. Biosynthesis of human fibrinogen. Subunit interactions and potential intermediates in assembly. J Biol Chem 1993;268:8919-26.
    • (1993) J Biol Chem , vol.268 , pp. 8919-8926
    • Huang, S.1    Mulvihill, E.R.2    Farrell, D.H.3    Chung, D.W.4    Davie, E.W.5
  • 24
    • 0035146448 scopus 로고    scopus 로고
    • Database analysis of O-glycosylation sites in proteins
    • Thanka Christlet TH, Veluraja K. Database analysis of O-glycosylation sites in proteins. Biophys J 2001;80:952-60.
    • (2001) Biophys J , vol.80 , pp. 952-960
    • Thanka Christlet, T.H.1    Veluraja, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.