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Proteolytic properties of single-chain factor XII: a mechanism for triggering contact activation (2017)
Journal Article
Ivanov, I., Matafonov, A., Sun, M., Cheng, Q., Dickeson, S. K., Verhamme, I. M., …Gailani, D. (in press). Proteolytic properties of single-chain factor XII: a mechanism for triggering contact activation. Blood, 129, doi:10.1182/blood-2016-10-744110. ISSN 0006-4971

When blood is exposed to variety of artificial surfaces and biologic substances, the plasma proteins factor XII (FXII) and prekallikrein undergo reciprocal proteolytic conversion to the proteases αFXIIa and α-kallikrein by a process called contact ac... Read More

A novel DFP tripeptide motif interacts with the coagulation factor XI apple 2 domain (2016)
Journal Article
Wong, S. S., Østergaard, S., Hall, G., Li, C., Williams, P. M., Stennicke, H., & Emsley, J. (in press). A novel DFP tripeptide motif interacts with the coagulation factor XI apple 2 domain. Blood, 127(23), doi:10.1182/blood-2015-10-676122. ISSN 0006-4971

Factor XI (FXI) is the zymogen of FXIa, which cleaves FIX in the intrinsic pathway of coagulation. FXI is known to exist as a dimer and interacts with multiple proteins via its 4 apple domains in the “saucer section” of the enzyme; however, to date,... Read More

Coagulation factor XII protease domain crystal structure (2015)
Journal Article
Pathak, M., Wilmann, P., Awford, J., Li, C., Hamad, B., Fischer, P., …Emsley, J. (2015). Coagulation factor XII protease domain crystal structure. Journal of Thrombosis and Haemostasis, 13(4), 580-591. doi:10.1111/jth.12849

Background: Coagulation factor XII is a serine protease that is important for kinin generation and blood coagulation, cleaving the substrates plasma kallikrein and FXI. Objective: To investigate FXII zymogen activation and substrate recognition by d... Read More

Exploiting the kinetic interplay between GPIb -VWF binding interfaces to regulate hemostasis and thrombosis (2014)
Journal Article
Chen, J., Zhou, H., Diacovo, A., Zheng, X. L., Emsley, J., & Diacovo, T. G. (2014). Exploiting the kinetic interplay between GPIb -VWF binding interfaces to regulate hemostasis and thrombosis. Blood, 124(25), doi:10.1182/blood-2014-04-569392. ISSN 0006-4971

Platelet–von Willebrand factor (VWF) interactions must be tightly regulated in order to promote effective hemostasis and prevent occlusive thrombus formation. However, it is unclear what role the inherent properties of the bond formed between the pla... Read More

Structure and catalytic regulatory function of ubiquitin specific protease 11 N-terminal and ubiquitin-like domains (2014)
Journal Article
Harper, S., Gratton, H. E., Cornaciu, I., Oberer, M., Scott, D. J., Emsley, J., & Dreveny, I. (in press). Structure and catalytic regulatory function of ubiquitin specific protease 11 N-terminal and ubiquitin-like domains. Biochemistry, 53(18), doi:10.1021/bi500116x. ISSN 1520-4995

The ubiquitin specific protease 11 (USP11) is implicated in DNA repair, viral RNA replication, and TGFβ signaling. We report the first characterization of the USP11 domain architecture and its role in regulating the enzymatic activity. USP11 consists... Read More