Zobrazeno 1 - 10
of 70
pro vyhledávání: '"Kenta Teruya"'
Autor:
Hideaki Kai, Kenta Teruya, Atsuko Takeuchi, Yoshikazu Nakamura, Hidehiro Mizusawa, Masahito Yamada, Tetsuyuki Kitamoto
Publikováno v:
Heliyon, Vol 9, Iss 3, Pp e13974- (2023)
The polymorphic heterozygosity of PRNP at codon 129 or 219 prevents the onset of sporadic Creutzfeldt-Jakob disease (sCJD). We investigated the association between polymorphic genotypes at codon 129 or 219 and comprehensive prion disease onset using
Externí odkaz:
https://doaj.org/article/cfe210c0f1af49a286d17a58750424fe
Autor:
Chiyuki Awahara, Daiki Oku, Saki Furuta, Kazuya Kobayashi, Kenta Teruya, Kenichi Akaji, Yasunao Hattori
Publikováno v:
Molecules, Vol 27, Iss 5, p 1646 (2022)
In this study, the effects of side-chain configurations of D-Ile residues of a retro–inverso (RI)-type inhibitor on the human T-cell leukemia virus type 1 (HTLV-1) protease containing a hydroxyethylamine dipeptide isostere were clarified. Prior to
Externí odkaz:
https://doaj.org/article/729c42ba1efe4d00ae669f19ffbe04f5
Publikováno v:
PLoS ONE, Vol 12, Iss 9, p e0185357 (2017)
Our previous study on prion-infected rodents revealed that hydroxypropyl methylcellulose compounds (HPMCs) with different molecular weights but similar composition and degree of substitution have different levels of long-lasting anti-prion activity.
Externí odkaz:
https://doaj.org/article/06599ca759124adaa35fef3def57aaee
Autor:
Kenta Teruya, Ayumi Oguma, Keiko Nishizawa, Maki Kawata, Yuji Sakasegawa, Hiroshi Kamitakahara, Katsumi Doh-Ura
Publikováno v:
PLoS Pathogens, Vol 12, Iss 12, p e1006045 (2016)
Prion diseases are fatal, progressive, neurodegenerative diseases caused by prion accumulation in the brain and lymphoreticular system. Here we report that a single subcutaneous injection of cellulose ethers (CEs), which are commonly used as inactive
Externí odkaz:
https://doaj.org/article/954ad1123584407cb827ca9f7b91f243
Autor:
Keita Arai, Ayumi Oguma, Miki Watanabe-Matsui, Kenta Teruya, Yuji Sakasegawa, Keiko Nishizawa, Sabine Gilch, Sara Iwabuchi, Katsumi Doh-ura, Hermann M. Schätzl
Publikováno v:
Biochemical and Biophysical Research Communications. 560:105-111
Anti-prion effects of cellulose ether (CE) are reported in rodents, but the molecular mechanism is fully unknown. Here, we investigated the genetic background of CE effectiveness by proteomic and genetic analysis in mice. Proteomic analysis in the tw
Autor:
Mingxuan Ding, Wen-Quan Zou, Weiguanliu Zhang, Justin J. Greenlee, Hae Weon Lee, Jue Yuan, Kenta Teruya, Katsumi Doh-ura, Marcus Mitchell, Manuel V. Camacho, Li Cui, Ayumi Oguma, Aaron Foutz, Qingzhong Kong
Publikováno v:
Molecular Neurobiology
Previous studies have revealed that the infectious scrapie isoform of prion protein (PrPSc) harbored in the skin tissue of patients or animals with prion diseases can be amplified and detected through the serial protein misfolding cyclic amplificatio
Autor:
Hiroyuki Konno, Kenta Teruya
Publikováno v:
HETEROCYCLES. 106:797
Autor:
Kenta Teruya, Ayumi Oguma, Satoko Takahashi, Miki Watanabe-Matsui, Sachiyo Tsuji-Kawahara, Masaaki Miyazawa, Katsumi Doh-ura
Publikováno v:
International immunopharmacology. 107
The anti-prion activity of cellulose ether (CE) has been reported in rodents, but the mechanism of action is not well understood. As defects in early T-cell development have been reported in Tga20 mice which show only a slight effect of CE administra
Autor:
Keiko Nishizawa, Sabine Gilch, Katsumi Doh-ura, Ayumi Oguma, Hermann M. Schätzl, Kenta Teruya, Yuji Sakasegawa
Publikováno v:
Journal of Pharmaceutical Sciences. 108:2814-2820
Prion accumulation in the brain and lymphoreticular system causes fatal neurodegenerative diseases. Our previous study revealed that cellulose ethers (CE) have anti-prion activities in vivo and in prion-infected cells when administered at high doses.
Autor:
Keiko Nishizawa, Kenta Teruya, Ayumi Oguma, Yuji Sakasegawa, Katsumi Doh-ura, Tetsuyuki Kitamoto
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1863:384-394
In prion diseases, infectious pathogenic particles that are composed of abnormal prion proteins (PrPSc) accumulate in the brain. PrPSc is biochemically characterized by its protease-resistance core (PrPres), but its structural features have not been