Zobrazeno 1 - 10
of 273
pro vyhledávání: '"Taro TAMADA"'
Autor:
Tomoto Ura, Nanako Sakakibara, Yu Hirano, Taro Tamada, Yoichi Takakusagi, Kentaro Shiraki, Tsutomu Mikawa
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-8 (2023)
Abstract Biological properties of protein molecules depend on their interaction with other molecules, and enzymes are no exception. Enzyme activities are controlled by their interaction with other molecules in living cells. Enzyme activation and thei
Externí odkaz:
https://doaj.org/article/da50f7594286463bb344da6730f57dfb
Autor:
Seigi Yamamoto, Fumiaki Kono, Kazuma Nakatani, Miwako Hirose, Katsunori Horii, Yoshitaka Hippo, Taro Tamada, Yusuke Suenaga, Tatsuhito Matsuo
Publikováno v:
Frontiers in Oncology, Vol 13 (2023)
NCYM, a Homininae-specific oncoprotein, is the first de novo gene product experimentally shown to have oncogenic functions. NCYM stabilizes MYCN and β-catenin via direct binding and inhibition of GSK3β and promotes cancer progression in various tum
Externí odkaz:
https://doaj.org/article/19950001310f4a32898ccdef6c04184d
Publikováno v:
Biophysics and Physicobiology, Vol 20 (2023)
Neutron crystallography is a highly effective method for visualizing hydrogen atoms in proteins. In our recent study, we successfully determined the high-resolution (1.2 Å) neutron structure of high-potential iron-sulfur protein, refining the coord
Externí odkaz:
https://doaj.org/article/dcdf95b6e8b34c63a23df8dc50beac0a
Publikováno v:
Current Research in Biotechnology, Vol 5, Iss , Pp 100126- (2023)
To improve the specific activity at low temperatures of Ef-EG2 and to maintain thermostability, five mutant enzymes (K273R, N372D, Q387E, N402D, D43R) were produced. The two mutant enzymes (K273R, N402D) lost the cellulase activity. The specific acti
Externí odkaz:
https://doaj.org/article/daaf4b0ea5ad4d9abea63527c982fbcc
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Protein crystals are generally fragile and sensitive to subtle changes such as pH, ionic strength, and/or temperature in their crystallization mother liquor. Here, using T4 phage lysozyme as a model protein, the three-dimensional rigidification of pr
Externí odkaz:
https://doaj.org/article/3bea86c3731d41ef9f32ada0c29561fa
Publikováno v:
Biophysics and Physicobiology, Vol 19 (2022)
Hydrogen atoms and hydration water molecules in proteins are essential for many biochemical processes, especially enzyme catalysis. Neutron crystallography enables direct observation of hydrogen atoms, and reveals molecular recognition through hydrog
Externí odkaz:
https://doaj.org/article/6952b6b96bb248c7b1a661760117ba67
Autor:
Hiroshi Nakagawa, Taro Tamada
Publikováno v:
Frontiers in Chemistry, Vol 9 (2021)
Protein hydration is crucial for the stability and molecular recognition of a protein. Water molecules form a hydration water network on a protein surface via hydrogen bonds. This study examined the hydration structure and hydrogen bonding state of a
Externí odkaz:
https://doaj.org/article/3f3abcb19fba4423817b4cc8ab3de2e2
Autor:
Tatsuhito Matsuo, Kazuma Nakatani, Taiki Setoguchi, Koichi Matsuo, Taro Tamada, Yusuke Suenaga
Publikováno v:
Frontiers in Oncology, Vol 11 (2021)
NCYM, a cis-antisense gene of MYCN, encodes a Homininae-specific protein that promotes the aggressiveness of human tumors. Newly evolved genes from non-genic regions are known as de novo genes, and NCYM was the first de novo gene whose oncogenic func
Externí odkaz:
https://doaj.org/article/7235fb6daa124866a9a6aa840711c066
Autor:
Takahiro Yoshinaka, Hidetaka Kosako, Takuma Yoshizumi, Ryo Furukawa, Yu Hirano, Osamu Kuge, Taro Tamada, Takumi Koshiba
Publikováno v:
iScience, Vol 19, Iss , Pp 1065-1078 (2019)
Summary: The coiled-coil motif mediates subunit oligomerization and scaffolding and underlies several fundamental biologic processes. Prohibitins (PHBs), mitochondrial inner membrane proteins involved in mitochondrial homeostasis and signal transduct
Externí odkaz:
https://doaj.org/article/0ed6ee3c13b942f9a6b513e140c35356
Autor:
Yuu, Hirano, Taro, Tamada
Publikováno v:
日本放射光学会誌「放射光」. 35(2):69-77
銅含有亜硝酸還元酵素（CuNIR）は、地球上の脱窒過程において重要な亜硝酸イオンから一酸化窒素への1電子還元反応を触媒する酵素であるが、X線結晶構造解析から提唱された反応機構モ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=jairo_______::ae8616da9c9aba66b4d8a9736e757ecf
https://repo.qst.go.jp/records/85200
https://repo.qst.go.jp/records/85200