Professor JONAS EMSLEY's Outputs (29)

Proteolytic properties of single-chain factor XII: a mechanism for triggering contact activation (2017)
Journal Article
Ivanov, I., Matafonov, A., Sun, M.-F., Cheng, Q., Dickeson, S. K., Verhamme, I. M., Emsley, J., & Gailani, D. (2017). Proteolytic properties of single-chain factor XII: a mechanism for triggering contact activation. Blood, 129(11), 1527-1537. https://doi.org/10.1182/blood-2016-10-744110

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 about Proteolytic properties of single-chain factor XII: a mechanism for triggering contact activation.

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), https://doi.org/10.1182/blood-2015-10-676122

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 about A novel DFP tripeptide motif interacts with the coagulation factor XI apple 2 domain.

PqsBC, a condensing enzyme in the biosynthesis of the Pseudomonas aeruginosa quinolone signal: crystal structure, inhibition, and reaction mechanism (2016)
Journal Article
Drees, S. L., Li, C., Prasetya, F., Saleem, M., Dreveny, I., Williams, P., Hennecke, U., Emsley, J., & Fetzner, S. (2016). PqsBC, a condensing enzyme in the biosynthesis of the Pseudomonas aeruginosa quinolone signal: crystal structure, inhibition, and reaction mechanism. Journal of Biological Chemistry, 291(13), https://doi.org/10.1074/jbc.M115.708453

Pseudomonas aeruginosa produces a number of alkylquinolone-type secondary metabolites best known for their antimicrobial effects and involvement in cell-cell communication. In the alkylquinolone biosynthetic pathway, the β-ketoacyl-(acyl carrier prot... Read More about PqsBC, a condensing enzyme in the biosynthesis of the Pseudomonas aeruginosa quinolone signal: crystal structure, inhibition, and reaction mechanism.

Coagulation factor XII protease domain crystal structure (2015)
Journal Article
Pathak, M., Wilmann, P., Awford, J., Li, C., Hamad, B., Fischer, P., Dreveny, I., Dekker, L., & Emsley, J. (2015). Coagulation factor XII protease domain crystal structure. Journal of Thrombosis and Haemostasis, 13(4), 580-591. https://doi.org/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 about Coagulation factor XII protease domain crystal structure.

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), https://doi.org/10.1182/blood-2014-04-569392

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 about Exploiting the kinetic interplay between GPIb -VWF binding interfaces to regulate hemostasis and thrombosis.

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. (2014). Structure and Catalytic Regulatory Function of Ubiquitin Specific Protease 11 N-Terminal and Ubiquitin-like Domains. Biochemistry, 53(18), 2966-2978. https://doi.org/10.1021/bi500116x

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 about Structure and Catalytic Regulatory Function of Ubiquitin Specific Protease 11 N-Terminal and Ubiquitin-like Domains.

The mechanism underlying activation of factor IX by factor XIa (2014)
Journal Article
Gailani, D., Geng, Y., Verhamme, I., Sun, M.-F., Bajaj, S. P., Messer, A., & Emsley, J. (2014). The mechanism underlying activation of factor IX by factor XIa. Thrombosis Research, 133(Supplement 1), S48-S51. https://doi.org/10.1016/j.thromres.2014.03.020

Factor XI (fXI) is the zymogen of a plasma protease, factor XIa (fXIa), that contributes to thrombin generation during blood coagulation by proteolytic conversion of factor IX (fIX) to factor IXaβ (fIXaβ). There is considerable interest in fXIa as a... Read More about The mechanism underlying activation of factor IX by factor XIa.

Structural basis for native agonist and synthetic inhibitor recognition by the Pseudomonas aeruginosa quorum sensing regulator PqsR (MvfR) (2013)
Journal Article
Ilangovan, A., Fletcher, M., Rampioni, G., Pustelny, C., Rumbaugh, K., Heeb, S., Cámara, M., Truman, A., Chhabra, S. R., Emsley, J., & Williams, P. (2013). Structural basis for native agonist and synthetic inhibitor recognition by the Pseudomonas aeruginosa quorum sensing regulator PqsR (MvfR). PLoS Pathogens, 9(7), Article e1003508. https://doi.org/10.1371/journal.ppat.1003508

Bacterial populations co-ordinate gene expression collectively through quorum sensing (QS), a cell-to-cell communication mechanism employing diffusible signal molecules. The LysR-type transcriptional regulator (LTTR) protein PqsR (MvfR) is a key comp... Read More about Structural basis for native agonist and synthetic inhibitor recognition by the Pseudomonas aeruginosa quorum sensing regulator PqsR (MvfR).

End-stapled homo and hetero collagen triple helices: A click chemistry approach (2010)
Journal Article
Byrne, C., McEwan, P. A., Emsley, J., Fischer, P. M., & Chan, W. C. (2011). End-stapled homo and hetero collagen triple helices: A click chemistry approach. Chemical Communications, 47(9), 2589-2591. https://doi.org/10.1039/c0cc04795c

A CuAAC reaction was established for modular synthesis of end-stapled homo- and hetero-triple helical peptides, generating "clicked" macro-assemblies with enhanced thermal stability. © 2011 The Royal Society of Chemistry.