David Lane is a Professor of Molecular Haematology in the Centre for Haematology. He obtained a BA in Physics (1969) from the University of Essex and his PhD in 1974 from the University of London. He joined Imperial College (in the then Charing Cross and Westminster Medical School) in 1979. He was joint Editor-in-Chief of the Journal of Thrombosis & Haemostasis between 2007-2012. He was awarded a Distinguished Career Award from the International Society on Thrombosis and Haemostasis in 2011.
Highlighted recent publications:
South, K., Luken, B. M., Crawley, J. T., Phillips, R., Thomas, M., Collins, R. F., Deforche, L., Vanhoorelbeke, K., and Lane, D. A. (2014) Conformational activation of ADAMTS13, Proceedings of the National Academy of Sciences of the United States of America 111, 18578-18583.
Andersson, H. M., Siegerink, B., Luken, B. M., Crawley, J. T., Algra, A., Lane, D. A., and Rosendaal, F. R. (2012) High VWF, low ADAMTS13, and oral contraceptives increase the risk of ischemic stroke and myocardial infarction in young women, Blood 119, 1555-1560.
Xiang, Y., de Groot, R., Crawley, J. T., and Lane, D. A. (2011) Mechanism of von Willebrand factor scissile bond cleavage by a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13 (ADAMTS13), Proceedings of the National Academy of Sciences of the United States of America 108, 11602-11607.
Crawley, J. T., de Groot, R., Xiang, Y., Luken, B. M., and Lane, D. A. (2011) Unraveling the scissile bond: how ADAMTS13 recognizes and cleaves von Willebrand factor, Blood 118, 3212-3221.
He is a member of the Haemostasis and Thrombosis Research Group, see http://www1.imperial.ac.uk/departmentofmedicine/divisions/experimentalmedicine/haematology/coag/
et al., 2018, Biphasic activation of complement and fibrinolysis during the human nasal allergic response., J Allergy Clin Immunol
South K, Lane DA, 2018, ADAMTS-13 and von Willebrand factor: a dynamic duo, Journal of Thrombosis and Haemostasis, Vol:16, ISSN:1538-7933, Pages:6-18
et al., 2017, Factor V has an anticoagulant cofactor activity that targets the early phase of coagulation, Journal of Biological Chemistry, Vol:292, ISSN:0021-9258, Pages:9335-9344
South K, Freitas MO, Lane DA, 2017, A model for the conformational activation of the structurally quiescent metalloprotease ADAMTS13 by Von Willebrand factor, Journal of Biological Chemistry, Vol:292, ISSN:0021-9258, Pages:5760-5769
et al., 2017, A common mechanism by which type 2A von Willebrand disease mutations enhance ADAMTS13 proteolysis revealed with a von Willebrand factor A2 domain FRET construct, Plos One, Vol:12, ISSN:1932-6203