Papageorgiou, Irene, Nicholls, Peter K, Wang, Fang, Lackmann, Martin, Makanji, Yogeshwar, Salamonsen, Lois A, ...
Abstract Background The human endometrium is unique in its capacity to remodel constantly throughout adult reproductive life. Although the processes of tissue damage and breakdown in the endometrium...
Crystal structure of the human ephrin-A5 ectodomain (2007)
Nikolov, Dimitar, Li, Chen, Lackmann, Martin, Jeffrey, Philip, Himanen, Juha
The Eph receptors, the largest subfamily of receptor tyrosine kinases, and their ephrin ligands are important mediators of cell–cell communication regulating cell attachment, pathfinding, and...
Repelling class discrimination: ephrin-A5 binds to and activates EphB2 receptor signaling (2004)
Juha-Pekka Himanen, Michael J Chumley, Martin Lackmann, Chen Li, William A Barton, Phillip D Jeffrey, ...
This paper was part of our studies of Eph structure-function, in this case analysing the ability of Eph proteins to bind a number of ephrin ligands. Citations = 43
Dissecting the EphA3/Ephrin-A5 Interactions Using a Novel Functional Mutagenesis Screen (2004)
Fiona M. Smith, Christopher Vearing, Martin Lackmann, Herbert Treutlein, Juha Himanen, Ke Chen, ...
This study used a novel mutagenesis approach to define critical binding regions and individual residues affecting Eph-ephrin engagement. Citations = 14
Recruitment of Eph receptors into signaling clusters does not require ephrin contact (2004)
Wimmer-Kleikamp, Sabine H., Janes, Peter W., Squire, Anthony, Bastiaens, Philippe I. H., Lackmann, Martin
Dissecting the EphA3/Ephrin-A5 Interactions Using a Novel Functional Mutagenesis Screen (2004)
Fiona M. Smith, Christopher Vearing, Martin Lackmann, Herbert Treutlein, Juha Himanen, Ke Chen, ...
This study used a novel mutagenesis approach to define critical binding regions and individual residues affecting Eph-ephrin engagement. Citations = 14
Repelling class discrimination: ephrin-A5 binds to and activates EphB2 receptor signaling (2004)
Juha-Pekka Himanen, Michael J Chumley, Martin Lackmann, Chen Li, William A Barton, Phillip D Jeffrey, ...
This paper was part of our studies of Eph structure-function, in this case analysing the ability of Eph proteins to bind a number of ephrin ligands. Citations = 43
Lawrenson, Isobel D., Wimmer-Kleikamp, Sabine H., Lock, Peter, Schoenwaelder, Simone M., Down, Michelle, Boyd, Andrew W., ...
Eph receptor tyrosine kinases and ephrins regulate morphogenesis in the developing embryo where they effect adhesion and motility of interacting cells. Although scarcely expressed in adult tissues,...
Lawrenson, Isobel D., Wimmer-Kleikamp, Sabine H., Lock, Peter, Schoenwaelder, Simone M., Down, Michelle, Boyd, Andrew W., ...
Eph receptor tyrosine kinases and ephrins regulate morphogenesis in the developing embryo where they effect adhesion and motility of interacting cells. Although scarcely expressed in adult tissues,...
Purification and biochemical characterisation of two inflammatory murine cytokines (1992)
Bibliography: leaves 196-270.
The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity
Hinds, Mark G., Lackmann, Martin, Skea, Gretchen L., Harrison, Penny J., Huang, David C.S., Day, Catherine L.
Pro-survival Bcl-2-related proteins, critical regulators of apoptosis, contain a hydrophobic groove targeted for binding by the BH3 domain of the pro-apoptotic BH3-only proteins. The solution...
The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity
Hinds, Mark G., Lackmann, Martin, Skea, Gretchen L., Harrison, Penny J., Huang, David C.S., Day, Catherine L.
Pro-survival Bcl-2-related proteins, critical regulators of apoptosis, contain a hydrophobic groove targeted for binding by the BH3 domain of the pro-apoptotic BH3-only proteins. The solution...
Recruitment of Eph receptors into signaling clusters does not require ephrin contact
Wimmer-Kleikamp, Sabine H., Janes, Peter W., Squire, Anthony, Bastiaens, Philippe I.H., Lackmann, Martin
Eph receptors and their cell membrane–bound ephrin ligands regulate cell positioning and thereby establish or stabilize patterns of cellular organization. Although it is recognized that ephrin...
Crystal structure of the human ephrin-A5 ectodomain
Nikolov, Dimitar, Li, Chen, Lackmann, Martin, Jeffrey, Philip, Himanen, Juha
The Eph receptors, the largest subfamily of receptor tyrosine kinases, and their ephrin ligands are important mediators of cell–cell communication regulating cell attachment, pathfinding, and...
Wilson-Annan, Julie, O'Reilly, Lorraine A., Crawford, Simon A., Hausmann, George, Beaumont, Jennifer G., Parma, Loes P., ...
Prosurvival Bcl-2–like proteins, like Bcl-w, are thought to function on organelles such as the mitochondrion and to be targeted to them by their hydrophobic COOH-terminal domain. We unexpectedly...
Cytoplasmic Relaxation of Active Eph Controls Ephrin Shedding by ADAM10
Janes, Peter W., Wimmer-Kleikamp, Sabine H., Frangakis, Achilleas S., Treble, Kane, Griesshaber, Bettina, Sabet, Ola, ...
Novel imaging strategies reveal a conformational shift in a receptor tyrosine kinase domain that controls ligand shedding by an ADAM metalloprotease.