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An excellent expert review that summarises the current knowledge on tight junctions with emphasis on the knowledge of the ultrastructure of tight junctions and on their molecular composition.
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Tsukita S., Furuse M., Itoh M. Multifunctional strands in tight junctions. Nature Reviews. Mol Cell Biol. 2:2001;285-292. An excellent expert review that summarises the current knowledge on tight junctions with emphasis on the knowledge of the ultrastructure of tight junctions and on their molecular composition.
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Junctional adhesion molecule (JAM) binds to PAR-3: A possible mechanism for the recruitment of PAR-3 to tight junctions
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Identifies JAM-1 at tight junction strands in epithelial cells and defines JAM-1 as a potential anchor for PAR-3, an essential factor for the establishment of cell polarity that is highly conserved among species.
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Antibodies to the junctional adhesion molecule cause disruption of endothelial cells and Do not prevent leukocyte influx into the meninges after viral or bacterial infection
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This report defines JAM-1 as a novel ligand for LFA-1 and presents the first anti human JAM-1 antibodies that block transendothelial migration of neutrophils and lymphocytes.
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This study demonstrates convincingly the dimerisation potential of JAM-1, which is in nice agreement with the important structural analysis in Kostrewa et al. (2001) [29•].
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Represents important structural evidence for the dimerisation of JAM-1, and suggests a zipper-like interaction mode reminiscent of the structural analysis of cadherin interactions.
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Kostrewa D., Brockhaus M., D'Arcy A., Dale G.E., Nelboeck P., Schmid G., Mueller F., Bazzoni G., Dejana E., Bartfai T., et al. X-ray structure of junctional adhesion molecule: structural basis for homophilic adhesion via a novel dimerization motif. EMBO J. 20:2001;4391-4398. Represents important structural evidence for the dimerisation of JAM-1, and suggests a zipper-like interaction mode reminiscent of the structural analysis of cadherin interactions.
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Cloning of Human Junctional Adhesion Molecule 3 (JAM-3) and its identification as the JAM-2 counter receptor
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The human homologue of mouse JAM-2 is identified as an inducible ligand on T-lymphocytes for the endothelial homologue of mouse JAM-3, suggesting the possibility that JAM-2/JAM-3 pairs participate in lymphocyte extravasation.
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Arrate M.P., Rodriguez J.M., Tran T.M., Brock T.A., Cunningham S.A. Cloning of Human Junctional Adhesion Molecule 3 (JAM-3) and its identification as the JAM-2 counter receptor. J Biol Chem. 276:2001;45826-45832. The human homologue of mouse JAM-2 is identified as an inducible ligand on T-lymphocytes for the endothelial homologue of mouse JAM-3, suggesting the possibility that JAM-2/JAM-3 pairs participate in lymphocyte extravasation.
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36
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Heterogeneity of endothelial junctions is reflected by differential expression and specific subcellular localization of the three JAM family members
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This paper defines mouse JAM-2 as specific for lymphatic endothelium and lymph node high endothelial venules and presents evidence that tight junction permeability is increased upon ectopic expression of JAM-2 in epithelial cells.
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Aurrand-Lions M., Johnson-Leger C., Wong C., Du Pasquier L., Imhof B.A. Heterogeneity of endothelial junctions is reflected by differential expression and specific subcellular localization of the three JAM family members. Blood. 98:2001;3699-3707. This paper defines mouse JAM-2 as specific for lymphatic endothelium and lymph node high endothelial venules and presents evidence that tight junction permeability is increased upon ectopic expression of JAM-2 in epithelial cells.
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