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dc.contributor.authorMuroski, John M-
dc.contributor.authorFu, Janine Y-
dc.contributor.authorNyugen, Hong Hanh-
dc.date.accessioned2024-04-15T07:45:07Z-
dc.date.available2024-04-15T07:45:07Z-
dc.date.issued2020-
dc.identifier.otherOER000000723vi
dc.identifier.urihttp://dlib.hust.edu.vn/handle/HUST/24422-
dc.descriptionTài liệu này được phát hành theo giấy phép CC-BY-NC-ND 4.0vi
dc.description.abstractAcyl-lysine modifications come in a variety of elemental compositions. There is increasing evidence that these modifications can have a functional effect on protein and are present in proteomes across all domains of life. Here we describe a new method that can allow for more confident identification of acyl modifications in proteomes by utilizing the immonium ion of these modifications. Our utilization of these ions allows for more comprehensive insight into the role of acyl modifications at the systems level.vi
dc.description.urihttps://www.biorxiv.org/content/10.1101/2020.04.20.052191v1vi
dc.formatPDFvi
dc.language.isoenvi
dc.publisherBiochemical Journalvi
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Vietnam*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/vn/*
dc.subjectProteinvi
dc.subjectProteomicvi
dc.subject.lccQD405vi
dc.titleLeveraging immonium ions for identifying and targeting acyl-lysine modifications in proteomic datasetsvi
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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