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Journal Abstract Search

139 related items for PubMed ID: 2071611

  • 1. A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the gamma-chain gene, causing defective calcium binding and impaired fibrin polymerization.
    Koopman J, Haverkate F, Briët E, Lord ST.
    J Biol Chem; 1991 Jul 15; 266(20):13456-61. PubMed ID: 2071611
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  • 2. Fibrinogen Bastia (gamma 318 Asp-->Tyr) a novel abnormal fibrinogen characterized by defective fibrin polymerization.
    Lounes KC, Soria C, Valognes A, Turchini MF, Soria J, Koopman J.
    Thromb Haemost; 1999 Dec 15; 82(6):1639-43. PubMed ID: 10613648
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  • 3. Fibrinogen Bern I: substitution gamma 337 Asn-->Lys is responsible for defective fibrin monomer polymerization.
    Steinmann C, Reber P, Jungo M, Lämmle B, Heinemann G, Wermuth B, Furlan M.
    Blood; 1993 Oct 01; 82(7):2104-8. PubMed ID: 8400260
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  • 4. Fibrinogen St. Gallen I (gamma 292 Gly--> Val): evidence for structural alterations causing defective polymerization and fibrinogenolysis.
    Stucki B, Schmutz P, Schmid L, Haeberli A, Lämmle B, Furlan M.
    Thromb Haemost; 1999 Feb 01; 81(2):268-74. PubMed ID: 10064005
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  • 6. A new substitution, gamma 358 Ser-->Cys, in fibrinogen Milano VII causes defective fibrin polymerization.
    Steinmann C, Bögli C, Jungo M, Lämmle B, Heinemann G, Wermuth B, Redaelli R, Baudo F, Furlan M.
    Blood; 1994 Sep 15; 84(6):1874-80. PubMed ID: 8080993
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  • 8. Characterization of an apparently lower molecular weight gamma-chain variant in fibrinogen Kyoto I. The replacement of gamma-asparagine 308 by lysine which causes accelerated cleavage of fragment D1 by plasmin and the generation of a new plasmin cleavage site.
    Yoshida N, Terukina S, Okuma M, Moroi M, Aoki N, Matsuda M.
    J Biol Chem; 1988 Sep 25; 263(27):13848-56. PubMed ID: 2971046
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  • 9. Heterozygous abnormal fibrinogen Osaka III with the replacement of gamma arginine-275 by histidine has an apparently higher molecular weight gamma-chain variant.
    Yoshida N, Imaoka S, Hirata H, Matsuda M, Asakura S.
    Thromb Haemost; 1992 Nov 10; 68(5):534-8. PubMed ID: 1455400
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  • 10. Recombinant fibrinogen Vlissingen/Frankfurt IV. The deletion of residues 319 and 320 from the gamma chain of firbinogen alters calcium binding, fibrin polymerization, cross-linking, and platelet aggregation.
    Hogan KA, Gorkun OV, Lounes KC, Coates AI, Weisel JW, Hantgan RR, Lord ST.
    J Biol Chem; 2000 Jun 09; 275(23):17778-85. PubMed ID: 10748039
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  • 13. The mutation in fibrinogen Bicêtre II (gamma Asn308-->Lys) does not affect the binding of t-PA and plasminogen to fibrin.
    Grailhe P, Boyer-Neumann C, Haverkate F, Grimbergen J, Larrieu MJ, Anglés-Cano E.
    Blood Coagul Fibrinolysis; 1993 Oct 09; 4(5):679-87. PubMed ID: 8292717
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  • 15. A frameshift mutation in Exon V of the A alpha-chain gene leading to truncated A alpha-chains in the homozygous dysfibrinogen Milano III.
    Furlan M, Steinmann C, Jungo M, Bögli C, Baudo F, Redaelli R, Fedeli F, Lämmle B.
    J Biol Chem; 1994 Dec 30; 269(52):33129-34. PubMed ID: 7806542
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  • 16. Fibrinogen Milano V: a congenital dysfibrinogenaemia with a gamma 275 Arg-->Cys substitution.
    Steinmann C, Bögli C, Jungo M, Lämmle B, Heinemann G, Wermuth B, Redaelli R, Baudo F, Furlan M.
    Blood Coagul Fibrinolysis; 1994 Aug 30; 5(4):463-71. PubMed ID: 7841300
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  • 17. Substitution of gamma Arg-275 by Cys in an abnormal fibrinogen, "fibrinogen Osaka II". Evidence for a unique solitary cystine structure at the mutation site.
    Terukina S, Matsuda M, Hirata H, Takeda Y, Miyata T, Takao T, Shimonishi Y.
    J Biol Chem; 1988 Sep 25; 263(27):13579-87. PubMed ID: 2971042
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  • 18. Gene analyses of abnormal fibrinogens with a mutation in the gamma chain.
    Mimuro J, Muramatsu S, Maekawa H, Sakata Y, Kaneko M, Yoshitake S, Okuma M, Ito Y, Takeda Y, Matsuda M.
    Int J Hematol; 1992 Oct 25; 56(2):129-34. PubMed ID: 1421174
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  • 20. Abnormal fibrinogens IJmuiden (B beta Arg14----Cys) and Nijmegen (B beta Arg44----Cys) form disulfide-linked fibrinogen-albumin complexes.
    Koopman J, Haverkate F, Grimbergen J, Engesser L, Nováková I, Kerst AF, Lord ST.
    Proc Natl Acad Sci U S A; 1992 Apr 15; 89(8):3478-82. PubMed ID: 1565641
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