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dc.contributor.authorK, Tauchmannová-
dc.contributor.authorDH, Ho-
dc.contributor.authorH, Nůsková-
dc.date.accessioned2024-05-08T10:01:42Z-
dc.date.available2024-05-08T10:01:42Z-
dc.date.issued2020-
dc.identifier.otherOER000000904vi
dc.identifier.urihttp://dlib.hust.edu.vn/handle/HUST/24686-
dc.descriptionTài liệu này được phát hành theo giấy phép CC-BY-NC-ND 4.0vi
dc.description.abstractBased on our data, we conclude that MLQ and Fo-a closely associate and their incorporation into the enzyme complex depends on each another. On the contrary, DAPIT protein seems to be incorporated at the very last step and its presence stabilises the holoenzyme.vi
dc.description.urihttps://www.biorxiv.org/content/10.1101/2020.02.03.931709v1vi
dc.formatPDFvi
dc.language.isoenvi
dc.publisherBiochemical Journalvi
dc.subjectATP synthasevi
dc.subjectAssemblyvi
dc.subjectOxidative phosphorylationvi
dc.subjectFo domainvi
dc.subject.lccQD405vi
dc.titleMLQ is responsible for stabilisation of subunit a in the holoenzyme of mammalian ATP synthasevi
dc.typeJournal articlevi
Appears in Collections:OER - Kỹ thuật hóa học; Công nghệ sinh học - Thực phẩm; Công nghệ môi trường

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