N-Glycosylation of Laminin-332 Regulates Its Biological Functions
Yoshinobu Kariya(Fukushima Medical University), Jianguo Gu(Tohoku Medical and Pharmaceutical University)
Cited by 52
Related Papers
N-Glycosylation of the I-like Domain of β1 Integrin Is Essential for β1 Integrin Expression and Biological Function
|Journal of Biological Chemistry|2009|112
Inhibition of fucosylation by 2-fluorofucose suppresses human liver cancer HepG2 cell proliferation and migration as well as tumor formation
|Scientific Reports|2017|102
Loss of αl,6‐fucosyltransferase inhibits chemical‐induced hepatocellular carcinoma and tumorigenesis by down‐regulating several cell signaling pathways
|The FASEB Journal|2015|96
Bisecting GlcNAc Residues on Laminin-332 Down-regulate Galectin-3-dependent Keratinocyte Motility
|Journal of Biological Chemistry|2009|78