Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Yoda, Hiromi"'
Autor:
Nishijima, Masaki, Kobayashi, Kota, Masuda-Endo, Megumi, Yoda, Hiromi, Koike-Takeshita, Ayumi
Publikováno v:
In Journal of Bioscience and Bioengineering October 2024 138(4):283-289
Autor:
Yoda, Hiromi1,2 (AUTHOR), Abe, Kazuya1,3 (AUTHOR), Takeo, Hideya1,3 (AUTHOR), Takamura-Enya, Takeji1,4 (AUTHOR) takamura@chem.kanagawa-it.ac.jp, Koike-Takeshita, Ayumi1,2 (AUTHOR)
Publikováno v:
Genes & Environment. 4/24/2024, Vol. 46 Issue 1, p1-13. 13p.
Publikováno v:
神奈川工科大学研究報告.B,理工学編. 45:27-33
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Type I chaperonins (Cpn60/Hsp60) are essential proteins that mediate the correct folding of newly translated and stress-denatured proteins in bacteria, chloroplast and mitochondria. Despite the high sequence homology among chaper
Type I chaperonins (Cpn60/Hsp60) are essential proteins that mediate the correct folding of newly translated and stress-denatured proteins in bacteria, chloroplast and mitochondria. Despite the high sequence homology among chaper
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=jairo_______::b4d3d250dd13c5a178e329e95df84c12
https://kait.repo.nii.ac.jp/records/12116
https://kait.repo.nii.ac.jp/records/12116
Autor:
Shimizu, Makiko1 (AUTHOR), Yoda, Hiromi1 (AUTHOR), Igarashi, Narumi1 (AUTHOR), Makino, Miki1 (AUTHOR), Tokuyama, Emi1 (AUTHOR), Yamazaki, Hiroshi1 (AUTHOR) hyamazak@ac.shoyaku.ac.jp
Publikováno v:
Xenobiotica. Oct2019, Vol. 49 Issue 10, p1244-1250. 7p.
Autor:
Yoda, Hiromi
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神奈川工科大学 学位論文 令和3年3月20日授与(甲第43号)
神奈川工科大学 学位論文 令和3年3月20日授与(甲第43号)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=jairo_______::1b98575c43493fd4b86f37262265b6f9
https://kait.repo.nii.ac.jp/records/12110
https://kait.repo.nii.ac.jp/records/12110
Akademický článek
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Akademický článek
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Akademický článek
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Autor:
Yoda, Hiromi, Koike-Takeshita, Ayumi
Publikováno v:
神奈川工科大学研究報告.B,理工学編. 39:9-12
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Chaperonin GroEL is double ring structure which constructed with 14-mer of 57 kDa subunits. GroEL has two cavities to trap both newly polypeptides and denatured proteins, and folds them with co-chaperonin GroES and ATP. Both Asp-
Chaperonin GroEL is double ring structure which constructed with 14-mer of 57 kDa subunits. GroEL has two cavities to trap both newly polypeptides and denatured proteins, and folds them with co-chaperonin GroES and ATP. Both Asp-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=jairo_______::fb0bcf139d48bcdff17ea03d23ed23bf
https://kait.repo.nii.ac.jp/records/1122
https://kait.repo.nii.ac.jp/records/1122
Autor:
Yoda, Hiromi, Koike-Takeshita, Ayumi
Publikováno v:
神奈川工科大学研究報告.B,理工学編. 38:49-53
application/pdf
The chaperonin GroEL is a double-ring structure which is constructed with 7 subunit ring of 57 kD, and those ring forms back to back. GroEL is bound with ATP and the co chaperon GroES for assisting protein folding in the cell. Gr
The chaperonin GroEL is a double-ring structure which is constructed with 7 subunit ring of 57 kD, and those ring forms back to back. GroEL is bound with ATP and the co chaperon GroES for assisting protein folding in the cell. Gr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=jairo_______::f9d7273e0a7e9ae52e28c03f5acb999d
https://kait.repo.nii.ac.jp/records/1104
https://kait.repo.nii.ac.jp/records/1104