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Journal Abstract Search

226 related items for PubMed ID: 26365066

  • 1. Structural transitions during prothrombin activation: On the importance of fragment 2.
    Adams TE, Huntington JA.
    Biochimie; 2016 Mar; 122():235-42. PubMed ID: 26365066
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  • 6. Prothrombin activation on the activated platelet surface optimizes expression of procoagulant activity.
    Wood JP, Silveira JR, Maille NM, Haynes LM, Tracy PB.
    Blood; 2011 Feb 03; 117(5):1710-8. PubMed ID: 21131592
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  • 9. Blood coagulation factor Xa interacts with a linear sequence of the kringle 2 domain of prothrombin.
    Taneda H, Andoh K, Nishioka J, Takeya H, Suzuki K.
    J Biochem; 1994 Sep 03; 116(3):589-97. PubMed ID: 7852276
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  • 10. Proteolysis of factor V by cathepsin G and elastase indicates that cleavage at Arg1545 optimizes cofactor function by facilitating factor Xa binding.
    Camire RM, Kalafatis M, Tracy PB.
    Biochemistry; 1998 Aug 25; 37(34):11896-906. PubMed ID: 9718313
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  • 11. Bothrojaracin, a proexosite I ligand, inhibits factor Va-accelerated prothrombin activation.
    Monteiro RQ, Zingali RB.
    Thromb Haemost; 2002 Feb 25; 87(2):288-93. PubMed ID: 11858489
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  • 12. Structural changes in the protease domain of prothrombin upon activation as assessed by N-bromosuccinimide modification of tryptophan residues in prethrombin-2 and thrombin.
    Stevens WK, Nesheim ME.
    Biochemistry; 1993 Mar 23; 32(11):2787-94. PubMed ID: 8457546
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  • 13. Regions remote from the site of cleavage determine macromolecular substrate recognition by the prothrombinase complex.
    Betz A, Krishnaswamy S.
    J Biol Chem; 1998 Apr 24; 273(17):10709-18. PubMed ID: 9553135
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  • 14. Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin.
    Arni RK, Padmanabhan K, Padmanabhan KP, Wu TP, Tulinsky A.
    Biochemistry; 1993 May 11; 32(18):4727-37. PubMed ID: 8387813
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  • 15. Activation of prothrombin by factor Xa bound to the membrane surface of human umbilical vein endothelial cells: its catalytic efficiency is similar to that of prothrombinase complex on platelets.
    Sugo T, Nakamikawa C, Tanabe S, Matsuda M.
    J Biochem; 1995 Feb 11; 117(2):244-50. PubMed ID: 7608107
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  • 16. The role of thrombin exosites I and II in the activation of human coagulation factor V.
    Segers K, Dahlbäck B, Bock PE, Tans G, Rosing J, Nicolaes GA.
    J Biol Chem; 2007 Nov 23; 282(47):33915-24. PubMed ID: 17878169
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  • 17. The second kringle domain of prothrombin promotes factor Va-mediated prothrombin activation by prothrombinase.
    Kotkow KJ, Deitcher SR, Furie B, Furie BC.
    J Biol Chem; 1995 Mar 03; 270(9):4551-7. PubMed ID: 7876224
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  • 18. Role of sequence and position of the cleavage sites in prothrombin activation.
    Stojanovski BM, Di Cera E.
    J Biol Chem; 2021 Aug 03; 297(2):100955. PubMed ID: 34265300
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  • 19. Exosite binding tethers the macromolecular substrate to the prothrombinase complex and directs cleavage at two spatially distinct sites.
    Boskovic DS, Krishnaswamy S.
    J Biol Chem; 2000 Dec 08; 275(49):38561-70. PubMed ID: 10984491
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  • 20. Prothrombin kringle 1 domain interacts with factor Va during the assembly of prothrombinase complex.
    Deguchi H, Takeya H, Gabazza EC, Nishioka J, Suzuki K.
    Biochem J; 1997 Feb 01; 321 ( Pt 3)(Pt 3):729-35. PubMed ID: 9032460
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