Evolution of techniques and tools for replication fork proteome and protein interaction studies.
| Autor: | Jurkovic CM; Department of Immunology and Cell Biology, Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, QC, Canada., Boisvert FM; Department of Immunology and Cell Biology, Faculty of Medicine and Health Sciences, Université de Sherbrooke, Sherbrooke, QC, Canada. |
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| Jazyk: | angličtina |
| Zdroj: | Biochemistry and cell biology = Biochimie et biologie cellulaire [Biochem Cell Biol] 2024 Apr 01; Vol. 102 (2), pp. 135-144. Date of Electronic Publication: 2023 Dec 19. |
| DOI: | 10.1139/bcb-2023-0215 |
| Abstrakt: | Understanding the complex network of protein-protein interactions (PPI) that govern cellular functions is essential for unraveling the molecular basis of biological processes and diseases. Mass spectrometry (MS) has emerged as a powerful tool for studying protein dynamics, enabling comprehensive analysis of protein function, structure, post-translational modifications, interactions, and localization. This article provides an overview of MS techniques and their applications in proteomics studies, with a focus on the replication fork proteome. The replication fork is a multi-protein assembly involved in DNA replication, and its proper functioning is crucial for maintaining genomic integrity. By combining quantitative MS labeling techniques with various data acquisition methods, researchers have made significant strides in elucidating the complex processes and molecular mechanisms at the replication fork. Overall, MS has revolutionized our understanding of protein dynamics, offering valuable insights into cellular processes and potential targets for therapeutic interventions. Competing Interests: The authors declare no competing interests. |
| Databáze: | MEDLINE |
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