Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Akiko Jozuka"'
Autor:
Yoshimichi Kozuka, Takuya Ohkubo, Yoshio Takeuchi, Kenichi Sano, Kota Watanabe, Akiko Jozuka, Naomi S. Hachiya, Kiyotoshi Kaneko, Yuji Sakasegawa, Makiko Yamada
Publikováno v:
Neuroscience Letters. 374:98-103
Recent studies suggest that the disease isoform of prion protein (PrPSc) is non-neurotoxic in the absence of cellular isoform of prion protein (PrPC), indicating that PrPC may participate directly in the neurodegenerative damage by itself. Meanwhile,
Autor:
Kota Watanabe, Yuji Sakasegawa, Akiko Jozuka, Makiko Y. Kawabata, Yoshimichi Kozuka, Kiyotoshi Kaneko, Naomi S. Hachiya
Publikováno v:
Biochemical and Biophysical Research Communications. 327:894-899
A pathogenic truncation of an amber mutation at codon 145 (Y145STOP) in Gerstmann–Straussler–Scheinker disease (GSS) was investigated through the real-time imaging in living cells, by utilizing GFP-PrP constructs. GFP-PrP(1–144) exhibited an ab
Autor:
Akiko Jozuka, Hiroyuki Sasaki, Yuji Sakasegawa, Kiyotoshi Kaneko, Shoichiro Tsukita, Naomi S. Hachiya
Publikováno v:
Biochemical and Biophysical Research Communications. 323:339-344
Oligomeric actin-interacting protein 2 (Aip2p) [Nat. Struct. Biol. 2 (1995) 28]/D-lactate dehydrogenase protein 2 (Dld2p) [Yeast 15 (1999) 1377, Biochem. Biophys. Res. Commun. 295 (2002) 910] exhibits the unique grapple-like structure with an ATP-dep
Publikováno v:
Biochemical and Biophysical Research Communications. 319:78-82
d -Lactate dehydrogenase protein 2 [Yeast 15 (1999) 1377; Biochem. Biophys. Res. Commun. 295 (2002) 910] was initially identified as the actin interacting protein 2 (Aip2p) using a two-hybrid screen to search for proteins that interact with actin [Na
Autor:
Akiko Jozuka, Makiko Yamada, Yoshimichi Kozuka, Kiyotoshi Kaneko, Yuji Sakasegawa, Naomi S. Hachiya
Publikováno v:
Prions ISBN: 4431255397
We have isolated a novel ATP-dependent robust protein-unfolding activity from S. cerevisiae and designated Unfoldin. ATP, but not its hydrolysis, promoted binding of Unfoldin to substrates and unfolded their conformation. Protein sequencing revealed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5dbe7f2fd2c315b718af54fdaa1ca54e
https://doi.org/10.1007/4-431-29402-3_34
https://doi.org/10.1007/4-431-29402-3_34
Autor:
Kota Watanabe, Yoshimichi Kozuka, Naomi Hachiya, Makiko Yamada, Akiko Jozuka, Kiyotoshi Kaneko, Yuji Sakasegawa
Publikováno v:
Prions ISBN: 4431255397
Transgenic mice harboring a high-copy-number of wild-type mouse (Mo) cellular prion protein (PrPC) are known to develop a spontaneous neurological dysfunction in an age-dependent manner, even without inoculation of the scrapie isoform of prion protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::98f0ae9f2081f6bcf06452707e3f0186
https://doi.org/10.1007/4-431-29402-3_31
https://doi.org/10.1007/4-431-29402-3_31
Autor:
Akiko Jozuka, Kiyotoshi Kaneko, Naomi S. Hachiya, Yuji Sakasegawa, Shoichiro Tsukita, Hiroyuki Sasaki
Publikováno v:
Biochemical and biophysical research communications. 320(4)
In order to investigate the molecular mechanism of the F-actin conformation modifying activity [Biochem. Biophys. Res. Commun. 319 (2004) 78] of actin-interacting protein 2 (Aip2p) [Nat. Struct. Biol. 2 (1995) 28]/ d -lactate dehydrogenase protein 2