Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Mayumi Kanagawa"'
Autor:
Mayumi Kanagawa1, Seiki Baba1,2, Yuzo Watanabe3, Noriko Nakagawa1,4, Akio Ebihara1, Seiki Kuramitsu4, Shigeyuki Yokoyama1, Gen-ichi Sampei1,5 sampei@pc.uec.ac.jp, Gota Kawai1,3 gkawai@sea.it-chiba.ac.jp
Publikováno v:
Journal of Biochemistry. Mar2016, Vol. 159 Issue 3, p313-321. 9p.
Autor:
Lirong Chen, Yuzo Watanabe, Gota Kawai, Bi-Cheng Wang, Zheng-Qing Fu, Akio Ebihara, Sakiko Suzuki, Hisaaki Yanai, Ryoji Masui, Satoko Tamura, Kiyoshi Okada, Seiki Kuramitsu, Shigeyuki Yokoyama, Mayumi Kanagawa, John Chrzas, Seiki Baba, Yoshihiro Agari, Takashi Kumasaka, Noriko Nakagawa, Gen Ichi Sampei
Publikováno v:
Acta Crystallographica Section F Structural Biology Communications. 72:627-635
The crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, fromThermus thermophilus,Sulfolobus tokodaiiandMethanocaldococcus jannaschiiwere determined and their structural characteristics were analyzed. For Pu
Autor:
Mayumi Kanagawa, H. Yasue, Tomoyuki Tsuchiyama, Kazuki Hori, Ken Kitajima, Estelle Garénaux, Yoshiki Yamaguchi, Akemi Ikeda, Chihiro Sato, Ami Goshima, Mitsuru Chiba, Takeru Kanazawa
Publikováno v:
Journal of Biological Chemistry. 290:5484-5501
Mammalian sperm acquire fertility through a functional maturation process called capacitation, where sperm membrane molecules are drastically remodeled. In this study, we found that a wheat germ agglutinin (WGA)-reactive protein on lipid rafts, named
Autor:
Kana Morita-Matsumoto, Yoshiki Yamaguchi, Naoyuki Taniguchi, Masamichi Nagae, Shinya Hanashima, Yasuhiko Kizuka, Mayumi Kanagawa
Publikováno v:
Scientific Reports
Glycans normally exist as a dynamic equilibrium of several conformations. A fundamental question concerns how such molecules bind lectins despite disadvantageous entropic loss upon binding. Bisected glycan, a glycan possessing bisecting N-acetylgluco
Autor:
Akio Ebihara, Mayumi Kanagawa, Seiki Kuramitsu, Akeo Shinkai, Hitoshi Iino, Miho Manzoku, Shigeyuki Yokoyama
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 71:2097-2101
Crystal structure of uncharacterized protein TTHA1756 from Thermus thermophilus HB8: Structural variety in UPF0150 family proteins Akio Ebihara, Miho Manzoku, Hitoshi Iino, Mayumi Kanagawa, Akeo Shinkai, Shigeyuki Yokoyama, and Seiki Kuramitsu* 1 RIK
Autor:
Akio Ebihara, Seiki Kuramitsu, Seiki Baba, Yuzo Watanabe, Mayumi Kanagawa, Shigeyuki Yokoyama, Noriko Nakagawa, Gota Kawai, Gen-ichi Sampei
Publikováno v:
Journal of biochemistry. 159(3)
Crystal structures of 5-aminoimidazole ribonucleotide (AIR) synthetase, also known as PurM, from Thermus thermophilus (Tt) and Geobacillus kaustophilus (Gk) were determined. For TtPurM, the maximum resolution was 2.2 A and the space group was P21212
Autor:
Yasufumi Ueda, Yota Iio, Makoto Nakabayashi, Noriko Nakagawa, Yoshiki Higuchi, Mayumi Kanagawa, Emi Ishido-Nakai, Naoki Shibata, Hirofumi Komori, Seiki Kuramitsu
Publikováno v:
Extremophiles : life under extreme conditions. 20(3)
TTHA0829 from Thermus thermophilus HB8 has a molecular mass of 22,754 Da and is composed of 210 amino acid residues. The expression of TTHA0829 is remarkably elevated in the latter half of logarithmic growth phase. TTHA0829 can form either a tetramer
Autor:
Mayumi, Kanagawa, Yan, Liu, Shinya, Hanashima, Akemi, Ikeda, Wengang, Chai, Yukiko, Nakano, Kyoko, Kojima-Aikawa, Ten, Feizi, Yoshiki, Yamaguchi
Publikováno v:
The Journal of Biological Chemistry
Background: ZG16p is a soluble mammalian lectin with a Jacalin-related β-prism-fold. Results: ZG16p binds to short α-mannose-related glycans and glycosaminoglycans via the canonical shallow mannose-binding pocket and an adjacent basic surface area,
Autor:
Mayumi Kanagawa, Shinji Fujiwara, Yoko Fukai, Hiroya Kawai, Gen-ichi Sampei, Toshiaki Shimasaki, Yuki Yanagida, Noriko Nakagawa, Shohei Mitsui, Hiroyuki Taka, Sakiko Suzuki, Shigeyuki Yokoyama, Mayumi Kusano, Seiki Kuramitsu, Gota Kawai, Kayoko Terao, Seiki Baba, Akio Ebihara
Publikováno v:
Journal of biochemistry. 154(6)
The crystal structures of glycinamide ribonucleotide transformylases (PurNs) from Aquifex aeolicus (Aa), Geobacillus kaustophilus (Gk) and Symbiobacterium toebii (St), and of formyltetrahydrofolate hydrolase (PurU) from Thermus thermophilus (Tt) were
Publikováno v:
Journal of Glycomics & Lipidomics.
Na+/K+-ATPase is a membrane glycoprotein composed of α, β, and γ subunits, generating ion gradients across plasma membranes. Ion pumping is mainly accomplished by the α subunit, while the glycosylated β subunit binds tightly to the α subunit to