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. 2023 Dec 14;25(1):378–403. doi: 10.1038/s44319-023-00012-6

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. Creative Commons Public Domain Dedication waiver http://creativecommons.org/publicdomain/zero/1.0/ applies to the data associated with this article, unless otherwise stated in a credit line to the data, but does not extend to the graphical or creative elements of illustrations, charts, or figures. This waiver removes legal barriers to the re-use and mining of research data. According to standard scholarly practice, it is recommended to provide appropriate citation and attribution whenever technically possible.

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(A) Schematic of the tandem mass tag (TMT) 6plex-based quantitative proteomics of WT and NME4-KO cells. (B) Volcano plot showing the levels of proteins in WT and NME4-KO cells. P values was estimated by Student’s t test and adjusted by Benjamini and Hochberg FDR (BH). Biological replicates, n = 3. Proteins whose levels were significantly changed are highlighted (fold change > 1.5, P values ≤ 0.05). (C) Significantly changed proteins in the NME4 knockout group were enriched in biological processes and analyzed in Hitplot. The top ten biological processes enriched by upregulated proteins was shown. P values ≤ 0.05. (D) KEGG pathways of upregulated proteins were mapped using proteomap. (E) Proteins were mapped to the corresponding pathways using proteomap. (D, E) The area of the polygon represents the protein abundance, which was normalized by protein size. Similar colors indicate similar or closely related pathways and proteins. Source data are available online for this figure.