Zobrazeno 1 - 10
of 118
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:
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
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
Publikováno v:
Journal of Molecular Biology. 426(No. 21):3634-3641
The chaperonin GroEL is an essential chaperone that assists in protein folding with the aid of GroES and ATP. GroEL forms a double-ring structure, and both rings can bind GroES in the presence of ATP. Recent progress on the GroEL mechanism has reveal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd2c871cf22afc512c989a73857471b6
http://t2r2.star.titech.ac.jp/cgi-bin/publicationinfo.cgi?q_publication_content_number=CTT100755254
http://t2r2.star.titech.ac.jp/cgi-bin/publicationinfo.cgi?q_publication_content_number=CTT100755254