Imperial College London


Faculty of MedicineNational Heart & Lung Institute

Reader in Matrix Receptor Signalling



+44 (0)20 7594 1591b.leitinger Website




115Sir Alexander Fleming BuildingSouth Kensington Campus





Birgit Leitinger joined Imperial College London in 2005 as a Lecturer and is currently Reader in Matrix Receptor Signalling.

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.

She has major teaching roles in the BSc Medical Biosciences as Module Lead for one of the core modules in Year 1 and Head of Assessment and Feedback for the entire programme.

Selected Publications

Journal Articles

Jalan A, Sammon D, Hartgerink J, et al., 2020, Chain alignment of collagen I deciphered using computationally designed heterotrimers, Nature Chemical Biology, Vol:16, ISSN:1552-4450, Pages:423-429

Corcoran D, Juskaite V, Xu Y, et al., 2019, DDR1 autophosphorylation is a result of aggregation into dense clusters, Scientific Reports, Vol:9, ISSN:2045-2322

Vehlow A, Klapproth E, Jin S, et al., 2019, Interaction of discoidin domain receptor 1 with a 14-3-3-Beclin-Akt1 complex modulates glioblastoma therapy sensitivity, Cell Reports, Vol:26, ISSN:2211-1247, Pages:3672-3683

Malcor J-D, Juskaite V, Gavriilidou D, et al., 2018, Coupling of a specific photoreactive triple-helical peptide to crosslinked collagen films restores binding and activation of DDR2 and VWF, Biomaterials, Vol:182, ISSN:0142-9612, Pages:21-34

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

Gao H, Chakraborty G, Zhang Z, 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

An B, Abbonante V, Xu H, et al., 2015, Recombinant Collagen Engineered to Bind to Discoidin Domain Receptors Functions as a Receptor Inhibitor, Journal of Biological Chemistry, Vol:291, ISSN:1083-351X, Pages:4343-4355

Xu H, Abe T, Liu JKH, 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, Pages:13565-13574

Xu H, Bihan D, Chang F, 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

Carafoli F, Mayer MC, Shiraishi K, 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

Hidalgo-Carcedo C, Hooper S, Chaudhry SI, 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

Leitinger B, 2011, Transmembrane Collagen Receptors, Annual Review of Cell and Developmental Biology, Vol:27, ISSN:1081-0706, Pages:265-290

Ali BR, Xu H, Akawi NA, 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

Konitsiotis AD, Raynal N, Bihan D, 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

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