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All Outputs (3)

Investigation of the filamin A-Dependent mechanisms of tissue factor incorporation into microvesicles (2017)
Journal Article
Collier, M. E. W., Ettelaie, C., Goult, B. T., Maraveyas, A., & Goodall, A. H. (2017). Investigation of the filamin A-Dependent mechanisms of tissue factor incorporation into microvesicles. Thrombosis and haemostasis, 117(11), 2034-2044. https://doi.org/10.1160/TH17-01-0009

We have previously shown that phosphorylation of tissue factor (TF) at Ser253 increases the incorporation of TF into microvesicles (MVs) following protease-activated receptor 2 (PAR2) activation through a process involving filamin-A, whereas Ser258 p... Read More about Investigation of the filamin A-Dependent mechanisms of tissue factor incorporation into microvesicles.

Tissue factor-bearing microparticles and inflammation: a potential mechanism for the development of venous thromboembolism in cancer (2017)
Journal Article
Date, K., Ettelaie, C., & Maraveyas, A. (2017). Tissue factor-bearing microparticles and inflammation: a potential mechanism for the development of venous thromboembolism in cancer. Journal of thrombosis and haemostasis : JTH, 15(12), 2289-2299. https://doi.org/10.1111/jth.13871

© 2017 International Society on Thrombosis and Haemostasis Summary: Cancer is associated with an increased risk of venous thromboembolism (VTE); the exact mechanisms for the induction of VTE remain to be fully elucidated, but it is widely acknowledge... Read More about Tissue factor-bearing microparticles and inflammation: a potential mechanism for the development of venous thromboembolism in cancer.

Peptidyl-prolyl isomerase 1 (Pin1) preserves the phosphorylation state of tissue factor and prolongs its release within microvesicles (2017)
Journal Article
Ettelaie, C., Collier, M., Featherby, S., Greenman, J., & Maraveyas, A. (2018). Peptidyl-prolyl isomerase 1 (Pin1) preserves the phosphorylation state of tissue factor and prolongs its release within microvesicles. BBA - Molecular Cell Research, 1865(1), 12-24. https://doi.org/10.1016/j.bbamcr.2017.09.016

© 2017 Elsevier B.V. The exposure and release of TF is regulated by post-translational modifications of its cytoplasmic domain. Here, the potential of Pin1 to interact with the cytoplasmic domain of TF, and the outcome on TF function was examined. MD... Read More about Peptidyl-prolyl isomerase 1 (Pin1) preserves the phosphorylation state of tissue factor and prolongs its release within microvesicles.