Novel Sulfated Lymphocyte Homing Receptors and Their Control by a Core1 Extension β1,3-N-Acetylglucosaminyltransferase

@article{Yeh2001NovelSL,
  title={Novel Sulfated Lymphocyte Homing Receptors and Their Control by a Core1 Extension $\beta$1,3-N-Acetylglucosaminyltransferase},
  author={Jiunn‐chern Yeh and Nobuyoshi Hiraoka and Bronislawa Petryniak and Jun Nakayama and Lesley G. Ellies and David Rabuka and Ole Hindsgaul and Jamey D Marth and John B. Lowe and Minoru Fukuda},
  journal={Cell},
  year={2001},
  volume={105},
  pages={957-969}
}

Figures from this paper

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Endoglycan, a Member of the CD34 Family, Functions as an L-selectin Ligand through Modification with Tyrosine Sulfation and Sialyl Lewis x*

Endoglycan employs a different binding mechanism, interacting with L-selectin through sulfation on two tyrosine residues and O-linked sLex structures that are presented within its highly acidic amino-terminal region, suggesting several potential settings for endoglycan-mediated adhesion events.

Significant decrease in alpha1,3-linked fucose in association with increase in 6-sulfated N-acetylglucosamine in peripheral lymph node addressin of FucT-VII-deficient mice exhibiting diminished lymphocyte homing.

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