L-selectin dimerization enhances tether formation to properly spaced ligand.

@article{Dwir2002LselectinDE,
  title={L-selectin dimerization enhances tether formation to properly spaced ligand.},
  author={Oren Dwir and Douglas A. Steeber and Ulrich S. Schwarz and Raymond T. Camphausen and Geoffrey S. Kansas and Thomas F. Tedder and Ronen Alon},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 24},
  pages={21130-9}
}
Selectin counterreceptors are glycoprotein scaffolds bearing multiple carbohydrate ligands with exceptional ability to tether flowing cells under disruptive shear forces. Bond clusters may facilitate formation and stabilization of selectin tethers. L-selectin ligation has been shown to enhance L-selectin rolling on endothelial surfaces. We now report that monoclonal antibodies-induced L-selectin dimerization enhances L-selectin leukocyte tethering to purified physiological L-selectin ligands… CONTINUE READING

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Effects of L-selectin Dimerization on Adhesion under Flow

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