Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Masato Ikawa"'
Autor:
Takeshi Kurihara, Takasuke Fukuhara, Chikako Ono, Satomi Yamamoto, Kentaro Uemura, Toru Okamoto, Masaya Sugiyama, Daisuke Motooka, Shota Nakamura, Masato Ikawa, Masashi Mizokami, Yoshihiko Maehara, Yoshiharu Matsuura
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
Abstract Complete removal of hepatitis B virus (HBV) DNA from nuclei is difficult by the current therapies. Recent reports have shown that a novel genome-editing tool using Cas9 with a single-guide RNA (sgRNA) system can cleave the HBV genome in vitr
Externí odkaz:
https://doaj.org/article/6a0a9b8099f94b9897ea32cd37e0cdaf
Autor:
Yoshiharu Matsuura, Daisuke Motooka, Takasuke Fukuhara, Kentaro Uemura, Satomi Yamamoto, Masaya Sugiyama, Shota Nakamura, Yoshihiko Maehara, Toru Okamoto, Takeshi Kurihara, Masashi Mizokami, Chikako Ono, Masato Ikawa
Publikováno v:
Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
Scientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
Kurihara, T., Fukuhara, T., Ono, C. et al. Suppression of HBV replication by the expression of nickase- and nuclease dead-Cas9. Sci Rep 7, 6122 (2017). https://doi.org/10.1038/s41598-017-05905-w
Complete removal of hepatitis B virus (HBV) DNA fr
Complete removal of hepatitis B virus (HBV) DNA fr
Autor:
Masato Ikawa, Ryota Shirakura, Hikaru Matsuda, Shoki Mikata, Masao Yoshitatsu, Masaru Okabe, Shuji Miyagawa
Publikováno v:
Transplant Immunology. 6:107-110
Complement receptor type 1 (CR1, CD35) contains both factor I cofactor activity and convertase decay accelerating activity, but is, in general, thought to be an extrinsic regulator of complement activation. In this study, we prepared a phosphatidylin
Autor:
Kiyoe Ura, Keisuke Nimura, Yasufumi Kaneda, Masato Ikawa, Hidetaka Shiratori, Robert J. Schwartz, Masaru Okabe
Publikováno v:
Nature. 460(7252)
Diverse histone modifications are catalysed and recognized by various specific proteins, establishing unique modification patterns that act as transcription signals. In particular, histone H3 trimethylation at lysine 36 (H3K36me3) is associated with