Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Kensuke Iwasaki"'
Autor:
Kensuke Iwasaki, Hiroaki Nishizaka, Keisuke Matsuoka, Yu Otsuji, Osamu Shibata, Hiromichi Nakahara, Mika Sato
Publikováno v:
Journal of Molecular Liquids. 244:499-505
We report the role of a spacer chain in gemini surfactants for solubilization of poor soluble compounds to the aqueous medium. Solubilization of n -alkylbenzenes into micellar solutions of alkanediyl-1, s -bis(dimethyltetradecylammonium bromide) (14-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c96a28be4b5375affae584f63640b26f
https://doi.org/10.1016/j.molliq.2017.09.014
https://doi.org/10.1016/j.molliq.2017.09.014
Autor:
Yurika Naruo, Reiko Urade, Yuichiro Tsuchi, Katsunori Koishihara, Motonori Matsusaki, Ryuta Mita, Akiho Hirose, Kumiko Hara, Kensuke Iwasaki, Taro Masuda, Aya Okuda
Publikováno v:
Plant Physiology. 170:774-789
Most proteins produced in the endoplasmic reticulum (ER) of eukaryotic cells fold via disulfide formation (oxidative folding). Oxidative folding is catalyzed by protein disulfide isomerase (PDI) and PDI-related ER protein thiol disulfide oxidoreducta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffa59d2bdcdded77932dba733aeb94e9
https://doi.org/10.1104/pp.15.01781
https://doi.org/10.1104/pp.15.01781
Autor:
Keito Nishizawa, Masao Ishimoto, Kensuke Iwasaki, Fumio Arisaka, Reiko Urade, Kyoko Takagi, Hiroyuki Wadahama, Motonori Matsusaki
Publikováno v:
Plant Physiology. 158:1395-1405
β-Conglycinin, one of the major soybean (Glycine max) seed storage proteins, is folded and assembled into trimers in the endoplasmic reticulum and accumulated into protein storage vacuoles. Prior experiments have used soybean β-conglycinin extracte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ea43594d2adce7c7da0c17c22e215490
https://doi.org/10.1104/pp.111.189621
https://doi.org/10.1104/pp.111.189621
Autor:
Reiko Urade, Kensuke Iwasaki, Hiroyuki Wadahama, Masao Ishimoto, Teruo Kawada, Shinya Kamauchi
Publikováno v:
FEBS Journal. 276:4130-4141
Protein disulfide isomerase (PDI) and other PDI family proteins are members of the thioredoxin superfamily and are thought to play important roles in disulfide bond formation and isomerization in the endoplasmic reticulum (ER). The exact functions of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6617436a8f12af866eddd6aac43702f
https://doi.org/10.1111/j.1742-4658.2009.07123.x
https://doi.org/10.1111/j.1742-4658.2009.07123.x
Autor:
Reiko Urade, Shinya Kamauchi, Keito Nishizawa, Masao Ishimoto, Kensuke Iwasaki, Hiroyuki Wadahama, Yumi Nakamoto, Teruo Kawada
Publikováno v:
FEBS Journal. 275:2644-2658
Protein disulfide isomerase family proteins play important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum. In this study, we cloned two similar protein disulfide isomerase family genes f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6088863172862bfdfb159b8e9d489654
https://doi.org/10.1111/j.1742-4658.2008.06412.x
https://doi.org/10.1111/j.1742-4658.2008.06412.x
Autor:
Shinya, Kamauchi, Hiroyuki, Wadahama, Kensuke, Iwasaki, Yumi, Nakamoto, Keito, Nishizawa, Masao, Ishimoto, Teruo, Kawada, Reiko, Urade
Publikováno v:
The FEBS journal. 275(10)
Protein disulfide isomerase family proteins play important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum. In this study, we cloned two similar protein disulfide isomerase family genes f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b6ead1e93332a8236c8696ead3856f07
https://pubmed.ncbi.nlm.nih.gov/18422652
https://pubmed.ncbi.nlm.nih.gov/18422652
Autor:
Motonori Matsusaki, Aya Okuda, Taro Masuda, Katsunori Koishihara, Ryuta Mita, Kensuke Iwasaki, Kumiko Hara, Yurika Naruo, Akiho Hirose, Yuichiro Tsuchi, Reiko Urade
Publikováno v:
Plant Physiology; Feb2016, Vol. 170 Issue 2, p774-789, 16p