@article{oai:tohoku-mpu.repo.nii.ac.jp:00000784,
 author = {山口, 芳樹 and Yamaguchi, Yoshiki},
 issue = {66},
 journal = {東北医科薬科大学研究誌, Journal of Tohoku Medical and Pharmaceutical University},
 month = {Dec},
 note = {Antibodies are glycosylated proteins which play a central role in immune system. much attention has been paid for N-glycosylation at asn297 of igg Fc. it has been well established that the Fc N-glycan is essential for expressingproper effector functions such as Fc receptor binding and complement activation. The underlying mechanism how the N-glycan affect Fc receptor binding has been analyzed and discussed from the structural data. This review will focus on the current understanding how Fc N-glycosylation impacts on the structure and function of the Fc. Finally, techniques are introduced to remodel the N-glycan attached to Fc.},
 pages = {11--18},
 title = {免疫グロブリン結合糖鎖の構造−機能相関},
 year = {2019},
 yomi = {ヤマグチ, ヨシキ}
}