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  • Nobuko Hosokawa, Yukiko Kamiya, Daiki Kamiya, Koichi Kato, Kazuhiro Nagata
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 2009 (First Publication: 3 April 2009)
  • In the endoplasmic reticulum (ER), lectins and processing enzymes are involved in quality control of newly synthesized proteins for productive folding as well as in the ER-associated degradationExpand
  • Yoshiki Yamaguchi, Mamiko Nishimura, +5 authors Koichi Kato
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 2006 (First Publication: 1 April 2006)
  • The Fc portion of immunoglobulin G (IgG) expresses the biantennary complex type oligosaccharides at Asn297 of the C(H)2 domain of each heavy chain with microheterogeneities depending on physiologicalExpand
  • Lindsey A Miles, C M Dahlberg, Janet Plescia, Jordi Félez, Koichi Kato, Edward F Plow
  • Chemistry, Medicine
  • Biochemistry
  • 1991 (First Publication: 1 February 1991)
  • Plasminogen binding to cell surfaces results in enhanced plasminogen activation, localization of the proteolytic activity of plasmin on cell surfaces, and protection of plasmin from alphaExpand
  • Satoshi Horimoto, Satoshi Ninagawa, +6 authors Kazutoshi Mori
  • Medicine, Biology
  • The Journal of Biological Chemistry
  • 2013 (First Publication: 16 September 2013)
  • Background: SEL1L, a partner protein of the E3 HRD1, is not required for degradation of known transmembrane-type endoplasmic reticulum-associated degradation (ERAD-Lm) substrates. Results:Expand