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Keywords: tissue factor
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Biochem J (2022) 479 (6): 731–750.
Published: 28 March 2022
... inflammasome which contains caspase-11. This leads to release of tissue factor (TF), a membrane glycoprotein receptor that forms a high-affinity complex with coagulation factor VII/VIIa to proteolytically activate factors IX to IXa and X to Xa, generating thrombin and leading to fibrin formation and platelet...
Biochem J (2016) 473 (2): 211–219.
Published: 05 January 2016
... the effect of plasma-derived and synthetic HDL on endothelial and monocyte expression of TF (tissue factor), the primary initiator of coagulation. HDL inhibited TF expression and activity in stimulated endothelial cells and monocytes in a dose-dependent way. Synthetic HDL fully retain the ability to inhibit...
Includes: Supplementary data
Biochem J (2012) 443 (1): 259–266.
Published: 14 March 2012
...Susan A. Maroney; Paul E. Ellery; Jeremy P. Wood; Josephine P. Ferrel; Catherine E. Bonesho; Alan E. Mast TFPI (tissue factor pathway inhibitor) is an anticoagulant protein that prevents intravascular coagulation through inhibition of fXa (Factor Xa) and the TF (tissue factor)–fVIIa (Factor VIIa...
Biochem J (2011) 437 (3): 455–460.
Published: 13 July 2011
...Hai Po Helena Liang; Teresa M. Brophy; Philip J. Hogg TF (tissue factor) is a transmembrane cofactor that initiates blood coagulation in mammals by binding Factor VIIa to activate Factors X and IX. The cofactor can reside in a cryptic configuration on primary cells and de-encryption may involve...
Biochem J (2003) 369 (3): 563–571.
Published: 01 February 2003
... of tissue factor (TF), suggests that the reduced V154G FVIIa activity is caused by impaired salt-bridge formation, thus resulting in a zymogen-like FVIIa form. The TF-mediated protection from chemical modification of V154A indicated that Gly 154 is responsible for this peculiar feature, and suggests...
Biochem J (2002) 363 (2): 387–393.
Published: 08 April 2002
... peptide followed by flexible linkers, an E-series peptide, and the Z-domain of protein A were expressed in Escherichia coli and purified using IgG—Sepharose affinity chromatography. The fusion peptides were potent anticoagulants and had steep concentration dependence curves in tissue factor-dependent...