Zobrazeno 1 - 10
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pro vyhledávání: '"Jo Franssen"'
Publikováno v:
Journal of Manual & Manipulative Therapy. 14:203-221
Thisarticleprovidesabestevidence-informedreviewofthecurrentscientificun- derstandingofmyofascialtriggerpointswithregardtotheiretiology,�pathophysiology,�and� clinicalimplications.�Evidence-informedmanualtherapyintegratesthebestavailablescien-
Publikováno v:
Journal of Biological Chemistry. 274:28225-28232
The physiological inhibitor of tissue factor (TF)zfactor VIIa (FVIIa), full-length tissue factor pathway inhibitor (TFPIFL) in complex with factor Xa (FXa), has a high affinity for anionic phospholipid membranes. The role of anionic phospholipids in
Autor:
H. Coenraad Hemker, Theo Lindhout, George M. Willems, Wun Tc, Anguo Li, Jo Franssen, Irene Salemink
Publikováno v:
Thrombosis and Haemostasis, 80(2), 273-280. Georg Thieme Verlag
SummaryTissue factor : factor VIIa induced activation of blood coagulation is inhibited by the complex between factor Xa and tissue factor pathway inhibitor (factor Xa : TFPI). We recently reported that phospholipid-bound factor Xa reduces the high b
Publikováno v:
Thrombosis and Haemostasis. 74:910-915
SummaryTissue factor-factor VIIa catalysed activation of factor X and factor IX is inhibited by the complex of tissue factor pathway inhibitor (TFPI) and factor Xa. At present, no information is available as to what extent the kinetics of complex for
Publikováno v:
Scopus-Elsevier
Thrombosis and Haemostasis, 66(4), 435-441. Georg Thieme Verlag
Thrombosis and Haemostasis, 66(4), 435-441. Georg Thieme Verlag
SummaryLow molecular weight (LMW) heparin preparations have unknown distributions of ATIII-binding material, so mean molecular weights as such might bear little information on their anti-factor Xa and anti-thrombin activities, and on the neutralizati
Publikováno v:
Biochemical Journal, 323(1), 33-37. Portland Press Ltd.
The inhibition of prothrombinase by tissue factor pathway inhibitor (TFPI) has been studied in the presence and absence of prothrombin, The rate constant of association of prothrombinase with full-length TFPI was 2.1 x 10(7) M(-1). s(-1) and 0.05 x 1
Publikováno v:
Thrombosis Research, 38(5), 447-458. Elsevier Science
We have investigated the antithrombin III independent effect of crude heparin, two heparin fractions and a heparinoid on in vitro thrombin-induced platelet activation. Thrombin-induced platelet factor Va generation and thrombin plus collagen-induced
Publikováno v:
Biochemistry, 25(20), 5962-5969. American Chemical Society
Scopus-Elsevier
Scopus-Elsevier
We have determined the rate constants of inactivation of factor X, and thrombin by antithrombin "heparin during the process of prothrombin activation. The second-order rate constant of inhibition of factor X, alone by antithrombin 111 as determined b
Publikováno v:
Thrombosis Research. 45:573-580
The neutralization of heparin by active site blocked meizothrombin and thrombin, prothrombin fragment 1.2, fragment 1 and fragment 2 was probed by the heparin-dependent factor Xa inactivation by antithrombin III (AT III). Meizothrombin had no effect
Publikováno v:
XIth International Congress on Thrombosis and Haemostasis.
The dependence of the anticoagulant properties of heparin upon charge density may reflect structural factors that are important in anti-thrombin effect. We have previously demonstrated that in the absence of antithrombin III (AT III) unfractionated h