Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Hisayoshi, Makyio"'
Autor:
Hiromune Ando, Akihiro Imamura, Yosuke Nishikawa, Ryuichi Kato, Makoto Kiso, Hideharu Ishida, Hisayoshi Makyio, Tatsuya Suzuki, Junpei Shimabukuro, Masato Kawasaki
Publikováno v:
Bioorganic & Medicinal Chemistry. 25:1132-1142
Selenium-incorporated fucoses (seleno-fucoses) differing in the position of the seleno-substituent were synthesized and applied to the X-ray structural determination of a carbohydrate-lectin complex using single/multi-wavelength anomalous dispersion
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93c9db8dd8922864b4f0b845e523b3a0
https://doi.org/10.1016/j.bmc.2016.12.021
https://doi.org/10.1016/j.bmc.2016.12.021
Autor:
Hideharu Ishida, Makoto Kiso, Tatsuya Suzuki, Ryuichi Kato, Hisayoshi Makyio, Akihiro Imamura, Hiromune Ando, Junpei Shimabukuro
Publikováno v:
Biochemical and Biophysical Research Communications. 477:477-482
The crystal structure of AOL (a fucose-specific lectin of Aspergillus oryzae) has been solved by SAD (single-wavelength anomalous diffraction) and MAD (multi-wavelength anomalous diffraction) phasing of seleno-fucosides. The overall structure is a si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c86f6a8e36723b43b3b804c65e278c1
https://doi.org/10.1016/j.bbrc.2016.06.069
https://doi.org/10.1016/j.bbrc.2016.06.069
Autor:
Ryuichi Kato, Hisayoshi Makyio
Publikováno v:
Trends in Glycoscience and Glycotechnology. 28:J25-J38
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a61faf910aabe90f97c139b5966e39ff
https://doi.org/10.4052/tigg.1429.1j
https://doi.org/10.4052/tigg.1429.1j
Autor:
Yohei Katoh, Hisayoshi Makyio, Masato Kawasaki, Hironari Kamikubo, Ryuichi Kato, Kazuhisa Nakayama, Hye-Won Shin, Minako Ohgi, Yasunori Kanaho, Hiroyuki Takatsu, Yong Xie, Ayako Hanai, Tomoko Ueda, Mikio Kataoka, Senye Takahashi, Soichi Wakatsuki, Tomomi Takei
Publikováno v:
The EMBO Journal. 31:2590-2603
A small GTPase, Arf6, is involved in cytokinesis by localizing to the Flemming body (the midbody). However, it remains unknown how Arf6 contributes to cytokinesis. Here, we demonstrate that Arf6 directly interacts with mitotic kinesin-like protein 1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f58633904fd69ed006953c22024518ff
https://doi.org/10.1038/emboj.2012.89
https://doi.org/10.1038/emboj.2012.89
Autor:
Masatada Tamakoshi, Hisayoshi Makyio, Hiromi Imamura, Ricardo A. Bernal, Ken Yokoyama, Elisabeth P. Carpenter, Daniela Stock, So Iwata, Chiyo Ikeda, Momi Iwata, Ryota Iino, Masasuke Yoshida
Publikováno v:
The EMBO Journal. 24:3974-3983
The crystal structure of subunit F of vacuole-type ATPase/synthase (prokaryotic V-ATPase) was determined to of 2.2 A resolution. The subunit reveals unexpected structural similarity to the response regulator proteins that include the Escherichia coli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::791b13f4787d01310153e3337a38ff5e
https://doi.org/10.1038/sj.emboj.7600859
https://doi.org/10.1038/sj.emboj.7600859
Autor:
Masatada Tamakoshi, James Barber, Masasuke Yoshida, Ken Yokoyama, Hisayoshi Makyio, Elizabeth Stambouli, So Iwata, Koji Nagata, Hiromi Imamura, Ben Hankamer, Momi Iwata, Chiyo Ikeda
Publikováno v:
Proceedings of the National Academy of Sciences. 101:59-64
The vacuole-type ATPases (V-ATPases) exist in various intracellular compartments of eukaryotic cells to regulate physiological processes by controlling the acidic environment. The crystal structure of the subunit C of Thermus thermophilus V-ATPase, h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3a1b9599856aa43f2927cbf0c8ac35f
https://doi.org/10.1073/pnas.0305165101
https://doi.org/10.1073/pnas.0305165101
Publikováno v:
Structure. 10(10):1415-1424
FtsH is a cytoplasmic membrane-integrated, ATP-dependent metalloprotease, which processively degrades both cytoplasmic and membrane proteins in concert with unfolding. The FtsH protein is divided into the N-terminal transmembrane region and the large
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b7db6017ff12977595e97bdb7cc940a
Publikováno v:
Biochemical and Biophysical Research Communications. 296:8-12
The function of an ATP-dependent membrane protease FtsH was investigated using the enzyme from Thermus thermophilus HB8. An FtsH mutant with replacement of Glu-419 in the zinc-binding motif by Cys lost the activity to digest casein, a model unfolded
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00c8d234aed60b1aeedb2163cef4c12e
https://doi.org/10.1016/s0006-291x(02)00830-6
https://doi.org/10.1016/s0006-291x(02)00830-6
Autor:
Hisayoshi, Makyio, Ryuichi, Kato
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1200
Phase determination is essential for solving X-ray crystal structures of proteins and their complexes. Conventional phase-determination methods using heavy atoms (Pt, Au, Hg, etc.) or the selenium (Se) atom are routinely utilized in structure determi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::43bd2b591741526409255c7f705f0e2b
https://pubmed.ncbi.nlm.nih.gov/25117259
https://pubmed.ncbi.nlm.nih.gov/25117259
Autor:
Makoto Kiso, Tatsuya Suzuki, Masanori Menjo, Hiromune Ando, Ryuichi Kato, Naoko Komura, Hideharu Ishida, Soichi Wakatsuki, Hisayoshi Makyio, Yusuke Yamada, Akihiro Imamura
Publikováno v:
Bioorganicmedicinal chemistry. 22(7)
Seleno-lactoses have been successfully synthesized as candidates for mimicking carbohydrate ligands for human galectin-9 N-terminal carbohydrate recognition domain (NCRD). Selenium was introduced into the mono- or di-saccharides using p-methylselenob
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d48f352a73930a05c8266d7f30368c4f
https://pubmed.ncbi.nlm.nih.gov/24631362
https://pubmed.ncbi.nlm.nih.gov/24631362