Mechanisms and Research Methods of Protein Modification in Virus Entry.
Gespeichert in:
| Titel: | Mechanisms and Research Methods of Protein Modification in Virus Entry. |
|---|---|
| Autoren: | Xiao Y; Xiangya School of Medicine, Central South University, Changsha, 410013, Hunan Province, China., Gao M; Xiangya School of Medicine, Central South University, Changsha, 410013, Hunan Province, China., Mo X; Xiangya School of Medicine, Central South University, Changsha, 410013, Hunan Province, China.; Xiangya School of Public Health, Central South University, Changsha, 410013, Hunan Province, China., Lang J; Xiangya School of Medicine, Central South University, Changsha, 410013, Hunan Province, China., Wang Z; Xiangya School of Medicine, Central South University, Changsha, 410013, Hunan Province, China., Ma Z; Xiangya School of Medicine, Central South University, Changsha, 410013, Hunan Province, China., Yang M; Xiangya School of Medicine, Central South University, Changsha, 410013, Hunan Province, China., Tang B; Changde Research Center for Agricultural Biomacromolecule, College of Life and Environmental Sciences, Hunan University of Arts and Science, Changde, 415000, Hunan Province, China., Liu D; Guangxi Colleges and Universities Key Laboratory of Biological Molecular Medicine Research, Department of Biochemistry and Molecular Biology, School of Pre-Clinical Medicine, Guangxi Medical University, Nanning, 530021, Guangxi Province, China. liudan.forever@163.com., He H; Xiangya School of Medicine, Central South University, Changsha, 410013, Hunan Province, China. helenhe@csu.edu.cn.; School of Life Sciences, Central South University, Changsha, 410013, Hunan Province, China. helenhe@csu.edu.cn. |
| Quelle: | Applied biochemistry and biotechnology [Appl Biochem Biotechnol] 2025 Oct; Vol. 197 (10), pp. 6283-6313. Date of Electronic Publication: 2025 Jul 19. |
| Publikationsart: | Journal Article; Review |
| Sprache: | English |
| Info zur Zeitschrift: | Publisher: Humana Press Country of Publication: United States NLM ID: 8208561 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1559-0291 (Electronic) Linking ISSN: 02732289 NLM ISO Abbreviation: Appl Biochem Biotechnol Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: Clifton, N.J. : Humana Press, c1981- |
| MeSH-Schlagworte: | Protein Processing, Post-Translational* , Virus Internalization*, Humans ; Glycosylation ; Phosphorylation ; Ubiquitination ; Animals ; Protein Array Analysis |
| Abstract: | Protein interactions are of paramount importance for the performance of biological functions within organisms. Post-translational modifications, including glycosylation and phosphorylation, regulate protein-protein interactions through non-covalent mechanisms. Glycosylation typically facilitates binding by altering surface properties, whereas phosphorylation can either enhance or disrupt interactions depending on context, collectively amplifying the biological impact of proteins. The entry of viruses and certain intracellular parasites into host cells is facilitated by these modifications, which permit the binding of ligands to receptors and the traversal of the cell membrane barrier. As research in this domain progresses, innovative methodologies are being developed, including protein microarrays and proximity-labeling techniques. These developments are being increasingly employed in disease prevention, therapeutics, and fundamental medical research. In light of the recent surge in emerging infectious diseases, the study of protein interactions has assumed heightened relevance. This review explores protein modifications, including glycosylation, phosphorylation, and ubiquitination, and focuses on their roles in viral entry. It highlights advanced methods for analyzing protein-protein interactions (PPIs), notably proximity labeling and protein microarrays, and concludes with novel insights into therapeutic development, aiming to inspire innovation in this evolving field. (© 2025. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.) |
| Competing Interests: | Declarations. Ethics Approval and Consent to Participate: Not applicable. Consent for Publication: All authors agree to publish the paper in your esteemed journal. Competing interests: The authors declare no competing interests. |
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| Grant Information: | 2021GXNSFBA220053 Natural Science Foundation of Guangxi Province; AD23026316 Specific Research Project of Guangxi for Research Bases and Talents; 2021KY0106 Middle-aged and Young Teachers' Basic Ability Promotion Project of Guangxi; 2021JJ30029 Natural Science Foundation of Hunan Province; 42306136 National Natural Science Foundation of China; M2022-04 State Key Laboratory of Microbial Resources, Chinese Academy of Sciences |
| Contributed Indexing: | Keywords: Glycosylation; Phosphorylation; Protein modification; Protein–protein interaction |
| Entry Date(s): | Date Created: 20250719 Date Completed: 20251115 Latest Revision: 20251115 |
| Update Code: | 20251115 |
| DOI: | 10.1007/s12010-025-05333-x |
| PMID: | 40682621 |
| Datenbank: | MEDLINE |
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Nájsť tento článok vo Web of Science | Abstract: | Protein interactions are of paramount importance for the performance of biological functions within organisms. Post-translational modifications, including glycosylation and phosphorylation, regulate protein-protein interactions through non-covalent mechanisms. Glycosylation typically facilitates binding by altering surface properties, whereas phosphorylation can either enhance or disrupt interactions depending on context, collectively amplifying the biological impact of proteins. The entry of viruses and certain intracellular parasites into host cells is facilitated by these modifications, which permit the binding of ligands to receptors and the traversal of the cell membrane barrier. As research in this domain progresses, innovative methodologies are being developed, including protein microarrays and proximity-labeling techniques. These developments are being increasingly employed in disease prevention, therapeutics, and fundamental medical research. In light of the recent surge in emerging infectious diseases, the study of protein interactions has assumed heightened relevance. This review explores protein modifications, including glycosylation, phosphorylation, and ubiquitination, and focuses on their roles in viral entry. It highlights advanced methods for analyzing protein-protein interactions (PPIs), notably proximity labeling and protein microarrays, and concludes with novel insights into therapeutic development, aiming to inspire innovation in this evolving field.<br /> (© 2025. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.) |
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| ISSN: | 1559-0291 |
| DOI: | 10.1007/s12010-025-05333-x |