Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Kanako Kuwasako"'
Autor:
Mayu Mikami, Hidehiko Shimizu, Norika Iwama, Mihono Yajima, Kanako Kuwasako, Yoshitoshi Ogura, Hyouta Himeno, Daisuke Kurita, Nobukazu Nameki
Publikováno v:
npj Antimicrobials and Resistance, Vol 2, Iss 1, Pp 1-14 (2024)
Abstract Escherichia coli possesses three stalled-ribosome rescue factors, tmRNA·SmpB (primary factor), ArfA (alternative factor to tmRNA·SmpB), and ArfB. Here, we examined the susceptibility of rescue factor-deficient strains from E. coli SE15 to
Externí odkaz:
https://doaj.org/article/5e5134b9f38049c79bcdcb91cb1bbde7
Autor:
Hisashi Yoshida, Sam-Yong Park, Gyosuke Sakashita, Yuko Nariai, Kanako Kuwasako, Yutaka Muto, Takeshi Urano, Eiji Obayashi
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
U2AF1 binds to the 3’ splice site of introns and its mutation lead to abnormal splicing. Here the authors solve the crystal structures of wild type and pathogenic mutant U2AF1 bound to target RNA, showing that different target sequence is preferred
Externí odkaz:
https://doaj.org/article/bbcab2b8d7fe42eca46d1130a52a6b8e
Autor:
Kanako Kuwasako, Sakura Suzuki, Nobukazu Nameki, Masayuki Takizawa, Mari Takahashi, Kengo Tsuda, Takashi Nagata, Satoru Watanabe, Akiko Tanaka, Naohiro Kobayashi, Takanori Kigawa, Peter Güntert, Mikako Shirouzu, Shigeyuki Yokoyama, Yutaka Muto
Publikováno v:
Biomolecular NMR Assignments. 16:297-303
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b62ad3d30eb42027e0dfa9d1991ef9a1
https://doi.org/10.1007/s12104-022-10094-3
https://doi.org/10.1007/s12104-022-10094-3
Autor:
Nobukazu Nameki, Shin-ichi Terawaki, Masayuki Takizawa, Madoka Kitamura, Yutaka Muto, Kanako Kuwasako
Publikováno v:
The Journal of Biochemistry.
The pre-spliceosomal complex involves interactions between U1 and U2 snRNPs, where a ubiquitin-like domain (ULD) of SF3A1, a component of U2 snRNP, binds to the stem-loop 4 (SL4; the UUCG tetraloop) of U1 snRNA in U1 snRNP. Here, we reported the 1.80
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8ab27e88aaffca073362a408f1c6efe3
https://doi.org/10.1093/jb/mvad033
https://doi.org/10.1093/jb/mvad033
Autor:
Shigeyuki Yokoyama, Yutaka Muto, Fahu He, Kanako Kuwasako, Mikako Shirouzu, Peter Güntert, Takashi Nagata, Akiko Tanaka, Kengo Tsuda, Mari Takahashi, Takanori Kigawa, Masayuki Takizawa, Naohiro Kobayashi, Satoru Watanabe
Publikováno v:
Biomolecular NMR Assignments. 16:41-49
Matrin-3 is a multifunctional protein that binds to both DNA and RNA. Its DNA-binding activity is linked to the formation of the nuclear matrix and transcriptional regulation, while its RNA-binding activity is linked to mRNA metabolism including spli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9344141cd89702218811e2ace9bfdf34
https://doi.org/10.1007/s12104-021-10057-0
https://doi.org/10.1007/s12104-021-10057-0
Autor:
Nobukazu Nameki, Masayuki Takizawa, Takayuki Suzuki, Shoko Tani, Naohiro Kobayashi, Taiichi Sakamoto, Yutaka Muto, Kanako Kuwasako
Publikováno v:
Protein Science. 31
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::79d7fd0cb79ad1e8dc1e97a90ff2bd8d
https://doi.org/10.1002/pro.4437
https://doi.org/10.1002/pro.4437
Autor:
Nobukazu, Nameki, Masayuki, Takizawa, Takayuki, Suzuki, Shoko, Tani, Naohiro, Kobayashi, Taiichi, Sakamoto, Yutaka, Muto, Kanako, Kuwasako
Publikováno v:
Protein science : a publication of the Protein Society. 31(10)
SURP domains are exclusively found in splicing-related proteins in all eukaryotes. SF3A1, a component of the U2 snRNP, has two tandem SURP domains, SURP1, and SURP2. SURP2 is permanently associated with a specific short region of SF3A3 within the SF3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::75370dbb48c4893973140026b1ef49a2
https://pubmed.ncbi.nlm.nih.gov/36173164
https://pubmed.ncbi.nlm.nih.gov/36173164
Autor:
Fahu He, Naohiro Kobayashi, Yutaka Muto, Akiko Tanaka, Shigeyuki Yokoyama, Satoru Watanabe, Mikako Shirouzu, Takashi Nagata, Kanako Kuwasako, Kengo Tsuda, Peter Güntert, Takanori Kigawa, Mari Takahashi, Ryuta Endo
Publikováno v:
Biomolecular NMR Assignments. 15:1-7
In humans, YTH (YT521-B homology) domain containing protein 2 (YTHDC2) plays a crucial role in the phase-shift from mitosis to meiosis. YTH domains bind to methylated adenosine nucleotides such as m6A. In a phylogenic tree, the YTH domain of YTHDC2 (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::03671179ad258d418f75c6a61ba86f35
https://doi.org/10.1007/s12104-020-09974-3
https://doi.org/10.1007/s12104-020-09974-3
Autor:
Sam-Yong Park, Kanako Kuwasako, Yutaka Muto, Takeshi Urano, Gyosuke Sakashita, Hisashi Yoshida, Eiji Obayashi, Yuko Nariai
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Nature Communications
Nature Communications
The accurate exclusion of introns by RNA splicing is critical for the production of mature mRNA. U2AF1 binds specifically to the 3´ splice site, which includes an essential AG dinucleotide. Even a single amino acid mutation of U2AF1 can cause seriou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc926103e39d6ef66fbd6a791cdf5e20
http://link.springer.com/article/10.1038/s41467-020-18559-6
http://link.springer.com/article/10.1038/s41467-020-18559-6
Autor:
Seizo Takahashi, Makoto Inoue, Peter Güntert, Takaho Terada, Kanako Kuwasako, Takuhiro Ito, Kengo Tsuda, Nobukazu Nameki, Takanori Kigawa, Taiichi Sakamoto, Yutaka Muto, Naoya Tochio, Shigeyuki Yokoyama, Naohiro Kobayashi, Mikako Shirouzu, Kaori Wakamatsu, Mari Takahashi, Atsuko Sato
Publikováno v:
Protein Science. 26:280-291
The spliceosomal protein SF3b49, a component of the splicing factor 3b (SF3b) protein complex in the U2 small nuclear ribonucleoprotein, contains two RNA recognition motif (RRM) domains. In yeast, the first RRM domain (RRM1) of Hsh49 protein (yeast o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::61890bb872e542d51d96e653ca67f1cf
https://doi.org/10.1002/pro.3080
https://doi.org/10.1002/pro.3080