Zobrazeno 1 - 10
of 361
pro vyhledávání: '"Koike-Takeshita A"'
Publikováno v:
Genes and Environment, Vol 46, Iss 1, Pp 1-13 (2024)
Abstract Background An in vitro micronucleus assay is a standard genotoxicity test. Although the technique and interpretation of the results are simple, manual counting of the total and micronucleus-containing cells in a microscopic field is tedious.
Externí odkaz:
https://doaj.org/article/23e86f25788044859da58719d1203b97
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:
Hideki Taguchi, Ayumi Koike-Takeshita
Publikováno v:
Frontiers in Molecular Biosciences, Vol 10 (2023)
Protein folding is often hampered by intermolecular protein aggregation, which can be prevented by a variety of chaperones in the cell. Bacterial chaperonin GroEL is a ring-shaped chaperone that forms complexes with its cochaperonin GroES, creating c
Externí odkaz:
https://doaj.org/article/88232c7cd24d4c249d274dc29ed69a83
Akademický článek
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Akademický článek
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Publikováno v:
In Journal of Biological Chemistry 24 October 2014 289(43):30005-30011
Publikováno v:
In Journal of Molecular Biology 23 October 2014 426(21):3634-3641
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:
Ayumi Koike-Takeshita, Hiromi Yoda
Publikováno v:
Microscopy. 70:289-296
Escherichia coli chaperonin GroEL, which is a large cylindrical protein complex comprising two heptameric rings with cavities of 4.5 nm each in the center, assists in intracellular protein folding with the aid of GroES and adenosine triphosphate (ATP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2936b33976581c5192ddcbf881aed7f5
https://doi.org/10.1093/jmicro/dfaa064
https://doi.org/10.1093/jmicro/dfaa064
Autor:
Yoda, Hiromi, Koike-Takeshita, Ayumi
Publikováno v:
Microscopy; Jun2021, Vol. 70 Issue 3, p289-296, 8p