Birgit Leitinger joined Imperial College London in 2005 as a Lecturer and has been a Senior Lecturer since October 2009.
She obtained her PhD in Biochemistry from the University of Basel, Switzerland. In 1996 she joined the Imperial Cancer Research Fund in London as a postdoctoral fellow, working with Dr Nancy Hogg in cell adhesion. In 2001 she moved to UCL, Department of Medicine, where she started her independent research as a Senior Research Fellow.
Her group's principal research interests are in cell adhesion, the interactions of cells with the extracellular matrix, and the mechanism of activation of cellular receptors. Work in her lab has been funded by the BBSRC and MRC.
Juskaite V, Corcoran DS, Leitinger B, 2017, Collagen induces activation of DDR1 through lateral dimer association and phosphorylation between dimers, Elife, Vol:6, ISSN:2050-084X
et al., 2016, Multi-organ Site Metastatic Reactivation Mediated by Non-canonical Discoidin Domain Receptor 1 Signaling, Cell, Vol:166, ISSN:0092-8674, Pages:47-62
et al., 2016, Recombinant Collagen Engineered to Bind to Discoidin Domain Receptor Functions as a Receptor Inhibitor, Journal of Biological Chemistry, Vol:291, ISSN:0021-9258, Pages:4343-4355
et al., 2014, Normal Activation of Discoidin Domain Receptor 1 Mutants with Disulfide Cross-links, Insertions, or Deletions in the Extracellular Juxtamembrane Region, Journal of Biological Chemistry, Vol:289, ISSN:0021-9258, Pages:13565-13574
et al., 2012, Discoidin Domain Receptors Promote alpha 1 beta 1-and alpha 2 beta 1-Integrin Mediated Cell Adhesion to Collagen by Enhancing Integrin Activation, PLOS One, Vol:7, ISSN:1932-6203
et al., 2012, Structure of the Discoidin Domain Receptor 1 Extracellular Region Bound to an Inhibitory Fab Fragment Reveals Features Important for Signaling, Structure, Vol:20, ISSN:0969-2126, Pages:688-697
Leitinger B, 2011, Transmembrane Collagen Receptors, Annual Review of Cell and Developmental Biology, Vol:27, ISSN:1081-0706, Pages:265-290
et al., 2011, Collective cell migration requires suppression of actomyosin at cell-cell contacts mediated by DDR1 and the cell polarity regulators Par3 and Par6, Nature Cell Biology, Vol:13, ISSN:1465-7392, Pages:49-U123
et al., 2008, Characterization of high affinity binding motifs for the discoidin domain receptor DDR2 in collagen, Journal of Biological Chemistry, Vol:283, ISSN:0021-9258, Pages:6861-6868
et al., 2010, Trafficking defects and loss of ligand binding are the underlying causes of all reported DDR2 missense mutations found in SMED-SL patients, Human Molecular Genetics, Vol:19, ISSN:0964-6906, Pages:2239-2250