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Springer Lab

Integrin

Content tagged with Integrin

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Bibliographic References tagged with Integrin

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Jo, M. H. et al. Single-molecule characterization of subtype-specific β1 integrin mechanics. Nat Commun 13, 7471 (2022).
Jo, M. H. et al. Single-molecule characterization of subtype-specific β1 integrin mechanics. Nat Commun 13, 7471 (2022).
Lin, F.-Y. et al. A general chemical principle for creating closure-stabilizing integrin inhibitors. Cell 185, 3533–3550.e27 (2022).
Lin, F.-Y. et al. A general chemical principle for creating closure-stabilizing integrin inhibitors. Cell 185, 3533–3550.e27 (2022).
Anderson, J., Li, J. & Springer, T. A. Regulation by metal ions and the ADMIDAS of integrin α5β1 conformational states and intrinsic affinities. Mol Biol Cell mbcE21110536 (2022) doi:10.1091/mbc.E21-11-0536.
Anderson, J., Li, J. & Springer, T. A. Regulation by metal ions and the ADMIDAS of integrin α5β1 conformational states and intrinsic affinities. Mol Biol Cell mbcE21110536 (2022) doi:10.1091/mbc.E21-11-0536.
Li, J., Yan, J. & Springer, T. Low affinity integrin states have faster ligand binding kinetics than the high affinity state. eLife 10, (2021).
Li, J., Yan, J. & Springer, T. Low affinity integrin states have faster ligand binding kinetics than the high affinity state. eLife 10, (2021).
Dong, Hudson, Lu & Springer. Structural determinants of integrin β-subunit specificity for latent TGF-β. Nat Struct Mol Biol. 21, 1091–6 (2014).
Dong, Hudson, Lu & Springer. Structural determinants of integrin β-subunit specificity for latent TGF-β. Nat Struct Mol Biol. 21, 1091–6 (2014).