Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Taro Q.P. Noguchi"'
Autor:
Kyohei Kuroda, Takashi Narihiro, Yuki Nakaya, Taro Q.P. Noguchi, Ryota Maeda, Masaru K. Nobu, Yuki Ohnishi, Yasuhiro Kumaki, Tomoyasu Aizawa, Hisashi Satoh
Publikováno v:
Chemical Engineering Journal. 450:137916
Autor:
Kyohei Kuroda, Takashi Narihiro, Futaba Shinshima, Mio Yoshida, Haruka Yamaguchi, Hazuki Kurashita, Nozomi Nakahara, Masaru K. Nobu, Taro Q.P. Noguchi, Masahito Yamauchi, Masayoshi Yamada
Publikováno v:
Water Research. 219:118581
Polyethylene terephthalate (PET) is produced worldwide, mainly as material for plastic drink bottles. PET is produced by polymerization of purified terephthalate (PTA) or dimethyl terephthalate (DMT) with ethylene glycol. During the synthetic manufac
Autor:
Taro Q.P. Noguchi, Masahiro Kuragano, Xuguang Lin, Kiyotaka Tokuraku, Reina Tainaka, Keiya Shimamori, Nuomin Galaqin
Publikováno v:
International Journal of Molecular Sciences
Volume 21
Issue 6
International Journal of Molecular Sciences, Vol 21, Iss 6, p 1978 (2020)
Volume 21
Issue 6
International Journal of Molecular Sciences, Vol 21, Iss 6, p 1978 (2020)
Amyloidosis refers to aggregates of protein that accumulate and are deposited as amyloid fibrils into plaques. When these are detected in organs, they are the main hallmark of Alzheimer&rsquo
s disease, Parkinson&rsquo
s disease, and other
s disease, Parkinson&rsquo
s disease, and other
Autor:
Taro Q.P. Noguchi, Taro Q.P. Uyeda, Yasushi Sako, Keitaro Shibata, Nobuhisa Umeki, Keiko Hirose
Publikováno v:
Scientific Reports
Scientific Reports, Vol 9, Iss 1, Pp 1-10 (2019)
Scientific Reports, Vol 9, Iss 1, Pp 1-10 (2019)
Mutation of the Lys-336 residue of actin to Ile (K336I) or Asp (K336E) causes congenital myopathy. To understand the effect of this mutation on the function of actin filaments and gain insight into the mechanism of disease onset, we prepared and bioc
Autor:
Jun Nakajima, Taro Q.P. Uyeda, Nobuhisa Umeki, Kohji Ito, Akira Nagasaki, Keiko Hirose, Taro Q.P. Noguchi, Kiyotaka Tokuraku
Publikováno v:
JOURNAL OF BIOLOGICAL CHEMISTRY. 288(3):1739-1749
Conserved Asp-11 of actin is a part of the nucleotide binding pocket, and its mutation to Gln is dominant lethal in yeast, whereas the mutation to Asn in human alpha-actin dominantly causes congenital myopathy. To elucidate the molecular mechanism of
Autor:
Saku T. Kijima, Nobuhisa Umeki, Nozomi Furutani-Umezu, Noriyuki Kodera, Kien Xuan Ngo, Jun Nakajima, Akira Nagasaki, Taro Q.P. Noguchi, Kiyotaka Tokuraku, Hiroaki Ueno, Taro Q.P. Uyeda
Publikováno v:
Scientific Reports
Heavy meromyosin (HMM) of myosin II and cofilin each binds to actin filaments cooperatively and forms clusters along the filaments, but it is unknown whether the two cooperative bindings are correlated and what physiological roles they have. Fluoresc
Autor:
Noriyuki Demizu, Kiyotaka Tokuraku, Nobuhisa Umeki, Taro Q.P. Noguchi, Taro Q.P. Uyeda, Toshio Yanagida, Kohji Ito, Atsuko H. Iwane, Tomotaka Komori
Publikováno v:
Journal of Biological Chemistry. 287:24339-24345
The G146V mutation in actin is dominant lethal in yeast. G146V actin filaments bind cofilin only minimally, presumably because cofilin binding requires the large and small actin domains to twist with respect to one another around the hinge region con
Autor:
Kien Xuan Ngo, Taro Q.P. Uyeda, Taro Q.P. Noguchi, Kenji Murakami, Takuo Yasunaga, Takeyuki Wakabayashi, Yuki Gomibuchi
Publikováno v:
Cell. 143(2):275-287
SummaryAssembled actin filaments support cellular signaling, intracellular trafficking, and cytokinesis. ATP hydrolysis triggered by actin assembly provides the structural cues for filament turnover in vivo. Here, we present the cryo-electron microsc
Publikováno v:
Biochemical and Biophysical Research Communications. 396:1006-1011
A number of studies suggested that the structure of actin filaments changes by interaction with actin-binding proteins such as cofilin and myosin, and that the conformational changes of the actin subunits within a filament are cooperative. To underst
Publikováno v:
Journal of Biological Chemistry. 282:27721-27727
We have developed a novel system for expressing recombinant actin in Dictyostelium. In this system, the C terminus of actin is fused to thymosin beta via a glycine-based linker. The fusion protein is purified using a His tag attached to the thymosin