Olha Viktorivna Shkel 예브헤니아 하르키브스카 Kim, Yun Kyung Lee, Jun-Seok 2024-01-19T13:01:35Z 2024-01-19T13:01:35Z 2022-04-03 2022-01 1861-4728 https://pubs.kist.re.kr/handle/201004/115845 Proximity labeling techniques are emerging high-throughput methods for studying protein-protein, protein-RNA, and protein-DNA interactions with temporal and spatial precision. Proximity labeling methods take advantage of enzymes that can covalently label biomolecules with reactive substrates. These labeled biomolecules can be identified using mass spectrometry or next-generation sequencing. The main advantage of these methods is their ability to capture weak or transient interactions between biomolecules. Proximity labeling is indispensable for studying organelle interactomes. Additionally, it can be used to resolve spatial composition of macromolecular complexes. Many of these methods have only recently been introduced; nonetheless, they have already provided new and deep insights into the biological processes at the cellular, organ, and organism levels. In this paper, we review a broad range of proximity labeling techniques, their development, drawbacks and advantages, and implementations in recent studies. English WILEY-V C H VERLAG GMBH Proximity Labeling Techniques: A Multi-Omics Toolbox Article 10.1002/asia.202101240 1 CHEMISTRY-AN ASIAN JOURNAL, v.17, no.2 CHEMISTRY-AN ASIAN JOURNAL 17 2 N scie scopus 000728547100001 2-s2.0-85120858421 Chemistry, Multidisciplinary Chemistry Review IN-VIVO PROTEOMICS APPROACH BIOTIN LIGASE CELL-TYPE REVEALS BIOTINYLATION CHROMATIN PROTEINS BINDING ENZYME biotin ligase DamID DNA-protein interactions mass spectrometry peroxidase photosensitizer protein- protein interactions proximity labeling PUP-IT RNA-protein interactions TRIBE