Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Syuzi Uno"'
Autor:
Chi-Chun Yang, Masahiro Suzuki, Shiori Yamakawa, Syuzi Uno, Ai Ishii, Satoshi Yamazaki, Rino Fukatsu, Ryo Fujisawa, Kenji Sakimura, Toshiki Tsurimoto, Hisao Masai
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-14 (2016)
Claspin mediates the transmission of a replication-stress signal from ATR to Chk1 and is necessary for efficient fork progression. Here the authors demonstrate that the C-terminal acidic patch is important for this role due to its interaction with Cd
Externí odkaz:
https://doaj.org/article/80ded932439f424cb6a70a103797b95e
Autor:
Toshiki Tsurimoto, Ryo Fujisawa, Ai Ishii, Rino Fukatsu, Kenji Sakimura, Chi Chun Yang, Hisao Masai, Shiori Yamakawa, Masahiro Suzuki, Satoshi Yamazaki, Syuzi Uno
Publikováno v:
Nature Communications
Nature Communications, Vol 7, Iss 1, Pp 1-14 (2016)
Nature Communications, Vol 7, Iss 1, Pp 1-14 (2016)
Claspin transmits replication stress signal from ATR to Chk1 effector kinase as a mediator. It also plays a role in efficient replication fork progression during normal growth. Here we have generated conditional knockout of Claspin and show that Clas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a47209e603ed203a7f024fb7198c2a87
http://europepmc.org/articles/PMC4945878
http://europepmc.org/articles/PMC4945878
Autor:
Hisao Masai, Syuzi Uno
Publikováno v:
Genes to Cells. 16:842-856
Purification of recombinant proteins of a large size often poses problems of instability or low expression in bacterial or insect cells. Here, we established a method for a high-level expression of large-sized recombinant proteins in mammalian cells
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c3d2775b7b38b75d0aee9236c0ce1853
https://doi.org/10.1111/j.1365-2443.2011.01535.x
https://doi.org/10.1111/j.1365-2443.2011.01535.x
Autor:
Syuzi, Uno, Hisao, Masai
Publikováno v:
Genes to cells : devoted to molecularcellular mechanisms. 16(8)
Purification of recombinant proteins of a large size often poses problems of instability or low expression in bacterial or insect cells. Here, we established a method for a high-level expression of large-sized recombinant proteins in mammalian cells
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3ae5b9312ae36be47e1243cdf5ae66bb
https://pubmed.ncbi.nlm.nih.gov/21790909
https://pubmed.ncbi.nlm.nih.gov/21790909