Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Kyoko Kojima-Aikawa"'
Autor:
Yumiko Kuranami, Yoshiki Yamaguchi, Miyuki Tsunooka‐Ota, Moeka Nakayama, Kyoko Kojima-Aikawa, Hitomi Miyagawa
Publikováno v:
Journal of Thrombosis and Haemostasis. 18:1357-1369
Background Factor XII (FXII) is a plasma serine protease that initiates the intrinsic pathway of blood coagulation upon contact with anionic substances, such as the sulfated glycolipid sulfatide. Annexins (ANXs) have been implicated in the regulation
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2132
ZG16p is a soluble 16-kDa protein abundantly expressed in the pancreas and gut, and has a β-prism fold structure similar to that of mannose-binding Jacalin-related lectins (mJRLs) such as BanLec, Heltuba, and Artocarpin. ZG16p binds to mannose via t
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2132
Among numerous heparin-binding proteins identified in animal tissues and body fluids, annexins are unique because their activies depend on their Ca
Publikováno v:
Methods in Molecular Biology ISBN: 9781071604298
ZG16p is a soluble 16-kDa protein abundantly expressed in the pancreas and gut, and has a β-prism fold structure similar to that of mannose-binding Jacalin-related lectins (mJRLs) such as BanLec, Heltuba, and Artocarpin. ZG16p binds to mannose via t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::60ed9573a5143e758a67794c0b4feb78
https://doi.org/10.1007/978-1-0716-0430-4_33
https://doi.org/10.1007/978-1-0716-0430-4_33
Autor:
Nobuo Sasaki, Takako Saitoh, Toshiro Sato, Yoshiki Yamaguchi, Kyoko Kojima-Aikawa, Sabine S. Gouraud, Yukiko Nakano, Akiko Mito
Publikováno v:
Glycobiology. 28:21-31
Zymogen granule protein 16 (ZG16p) is a soluble lectin that binds to both mannose and heparin/heparan sulfate. It is highly expressed in the human digestive tract and is secreted into the mucus. In this study, we investigated the effect of ZG16p on t
Autor:
Eiichiro Tominaga, Kyoko Kojima-Aikawa, Kyoko Tanaka, Fumiko Oikawa, Atsushi Suzuki, Daisuke Aoki, Fumika Inoue
Publikováno v:
Cancer Sci
HMMC‐1 is a human monoclonal antibody that reacts with a fucosylated and extended core 1 O‐glycan, Fucα1‐2Galβ1‐4GlcNAcβ1‐3Galβ1‐3GalNAc‐Ser/Thr, as an epitope. In the present study, we examined the effects of HMMC‐1 on cell proli
Autor:
Kyoko Kojima-Aikawa, Ping Wang, Minoru Fukuda, Kay-Hooi Khoo, Atsushi Suzuki, Tomoya O. Akama, Chi-Chi Chou, Daisuke Aoki, Peter H. Seeberger, Naohiro Kanayama, Fumiko Matsumura, Michiko N. Fukuda, Kazuko Kitayama, Toshiaki K. Shibata, Shin-Yi Yu, Kazuhiro Sugihara
Publikováno v:
Journal of Biological Chemistry
The Journal of Biological Chemistry
The Journal of Biological Chemistry
Background: We produced a humanized monoclonal antibody, designated HMOCC-1, against cell surface carbohydrates presented by malignant ovarian cancer. Results: Co-transfection experiments predicted HMOCC-1 antigenic oligosaccharides structures, which
Autor:
Naoshi Dohmae, Sachiko Hosokawa-Tamiya, Kyoko Kojima-Aikawa, Hidenao Toyoda, Yukiko Nakano, Akiko Kinoshita-Toyoda, Tomoko Mimura, Kaori Kumazawa-Inoue
Publikováno v:
Glycobiology. 22:258-266
ZG16p is a soluble 16 kDa pancreatic protein having structural similarities with plant β-prism fold lectins such as the banana lectin BanLec and the jackfruit lectin jacalin. ZG16p is postulated to be involved in the formation of zymogen granules by
Autor:
Jun Ichi Aikawa, Kazusa Nishiyama, Mayumi Tamura, Hideyo Takahashi, Hideaki Natsugari, Tomoharu Takeuchi, Ken-ichi Kasai, Kyoko Kojima-Aikawa, Yoichiro Arata, Atsushi Yamada
Publikováno v:
Carbohydrate Research. 346:1837-1841
Galβ1-4Fuc is a key structural motif in Caenorhabditis elegans glycans and is responsible for interaction with C. elegans galectins. In animals of the clade Protostomia, this unit seems to have important roles in glycan–protein interactions and co
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 17:5274-5278
Enzyme-linked lectin assay (ELLA) was performed for oligomannosylpeptoids, which were immobilized on microtiter plates through a streptavidin-biotin interaction. The other immobilization methods, a hydrophobic adsorption and a covalent attachment, we