Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Takehiro Suzuki"'
Publikováno v:
FEBS Letters. 591:3259-3264
We recently revealed that positively charged amino acids of Psb31, an extrinsic subunit found in diatom photosystem II (PSII), are involved in electrostatic interactions with PSII intrinsic subunits. However, the molecular interactions of Psb31 with
Autor:
Miyu Tsuchiya, Takehiro Suzuki, Naoshi Dohmae, Yukiko Sasazawa, Shintaro Kato, Miho Fujiwara, Yuki Niwa, Siro Simizu
Publikováno v:
FEBS Letters. 590:2639-2649
R-spondin3 (Rspo3) is a secreted protein, which acts as an agonist of canonical Wnt/β-catenin signaling that plays an important role in embryonic development and homeostasis. In this study, we focused on C-mannosylation, a unique type of glycosylati
Publikováno v:
FEBS Letters. 589:3287-3293
The matricellular protein CCN1, also known as Cyr61, is a secreted ligand and has numerous functions. Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr242. In this report, we demonstrated t
Autor:
Siro Simizu, Keisuke Yoshida, Takehiro Suzuki, Yukiko Sasazawa, Takuma Mogi, Naoshi Dohmae, Ken Ichi Takao, So Miyazaki
Publikováno v:
FEBS letters. 590(8)
Phenotype-based chemical screening is an attractive strategy for the identification of bioactive compounds. We searched for a compound that induces cellular morphological change and identified a novel compound that we named seco-clavilactone B (Seco-
Autor:
Yuki Hashimoto, Hiroyuki Unoki-Kubota, Hideaki Ohno, Yoshitsugu Miyazaki, Takuya Miyakawa, Yasushi Kaburagi, Hideyuki Miyatake, Hai Zheng, Takehiro Suzuki, Satoshi Yamagoe, Masaru Tanokura, Akinori Okumura, Tomoya Okabe, Naoshi Dohmae
Publikováno v:
FEBS letters. 587(5)
Leukocyte cell-derived chemotaxin 2 (LECT2) is a secreted hepatic protein that has been associated with several physiological activities. LECT2 belongs to the peptidase M23 family, suggesting that it is a zinc-binding protein. To test this possibilit
Publikováno v:
FEBS letters. 586(20)
Cathepsin V (L2), a lysosomal cysteine protease, is a member of cathepsin family, relating to cancer invasion and metastasis. Cathepsin V contains two predicted N-glycosylation sites, but it has not been reported whether cathepsin V is glycosylated o
Autor:
Ryo Nagao, Akinori Okumura, Takehiro Suzuki, Masako Iwai, Isao Enami, Hiroyasu Tanaka, Masanori Sano, Hideyuki Adachi, Katsuyoshi Nakazato, Jian Ren Shen
Publikováno v:
FEBS Letters. (27):5255-5258
PsbU is one of the extrinsic proteins in red algal Photosystem II (PSII) and functions to optimize the availability of Ca2+ and Cl− cofactors for water oxidation. To determine the functional residue of PsbU, we constructed various PsbU mutants from