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Integrin function: Molecular hierarchies of cytoskeletal and signaling molecules
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Mutational evidence for control of cell adhesion through integrin recruitment, independent of ligand binding
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A conserved sequence motif in the integrin β3 cytoplasmic domain is required for its specific interaction with β3-endonexin
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Affinity modulation of platelet integrin aIIbβ3 by β3 endonexin, a selective binding partner of the β3 integrin cytoplasmic tail
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of outstanding interest. This is perhaps the first clear demonstration that integrin affinity for ligand can be modulated by a directly associated protein. Also, this may help to explain why β3 integrins undergo such dramatic affinity modulation
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Regulation of endothelial cell motility by complexes of tetraspan molecules CD81/TAPA-1 and CD151/PETA-3 with α3β1 integrin localized at endothelial lateral junctions
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Yánez-Mó M, Alfranca A, Cabañas C, Marazuela M, Tejedor R, Ursa MA, Ashman LK, De Landázuri MO, Sánchez-Madrid F. Regulation of endothelial cell motility by complexes of tetraspan molecules CD81/TAPA-1 and CD151/PETA-3 with α3β1 integrin localized at endothelial lateral junctions. J Cell Biol. 141:1998;791-804.
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Association between rat homologue of CO-029, a metastasis-associated tetraspanin molecule and consumption coagulopathy
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Engaging CD19 or target of an antiproliferative antibody 1 on human B lymphocytes induces binding of B cells to the interfollicular stroma of human tonsils via integrin α4/β1 and fibronectin
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An epitope on VLA-6 (α6β1) integrin involved in migration but not adhesion is required for extravasation of murine melanoma B16F1 cells in liver
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of special interest. This is an important demonstration that integrins may do more than just mediate cell adhesion
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Hangan D, Morris VL, Boeters L, von Ballestrem C, Uniyal S, Chan BM. An epitope on VLA-6 (α6β1) integrin involved in migration but not adhesion is required for extravasation of murine melanoma B16F1 cells in liver. of special interest Cancer Res. 57:1997;3812-3817 This is an important demonstration that integrins may do more than just mediate cell adhesion.
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NAG-2, a novel transmembrane-4 superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins
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Tachibana I, Bodorova J, Berditchevski F, Zutter MM, Hemler ME. NAG-2, a novel transmembrane-4 superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins. J Biol Chem. 272:1997;29181-29189.
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(1997)
J Biol Chem
, vol.272
, pp. 29181-29189
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Tachibana, I.1
Bodorova, J.2
Berditchevski, F.3
Zutter, M.M.4
Hemler, M.E.5
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87
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0031660652
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Highly stoichiometric, stable and specific association of integrin α3β1 with CD151 provides a major link to phosphatigylinositol 4-kinase and may regulate cell migration
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of special interest
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Yauch RL, Berditchevski F, Harler MB, Reichner J, Hemler ME. Highly stoichiometric, stable and specific association of integrin α3β1 with CD151 provides a major link to phosphatigylinositol 4-kinase and may regulate cell migration. of special interest Mol Cell Biol. 1998; One of the most highly stoichometric, stable and specific associations of an integrin with another transmembrane protein is described here.
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(1998)
Mol Cell Biol
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Yauch, R.L.1
Berditchevski, F.2
Harler, M.B.3
Reichner, J.4
Hemler, M.E.5
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