uPAR: a versatile signalling orchestrator
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
http://www.nature.com/articles/nrm977.pdf
Reference126 articles.
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3. Ploug, M. & Ellis, V. Structure–function relationship in the receptor for urokinase-type plasminogen activator. Comparison to other members of the Ly-6 family and snake venom a-neurotoxins. FEBS Lett. 349, 163–168 (1994).
4. Behrendt, N., Roenne, E. & Danoe, K. Domain interplay in the urokinase receptor-requirement for the third domain in high affinity ligand binding and demonstration of ligand contact sites in distinct receptor domains. J. Biol. Chem. 271, 22885–22894 (1996).
5. Ploug, M. Identification of specific sites involved in ligand binding by photoaffinity labeling of the receptor for the urokinase-type plasminogen activator. Residues located at equivalent positions in uPAR domains I and III participate in the assembly of a composite ligand-binding site. Biochemistry 37, 16494–16505 (1998).
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