{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Li X"],"funding":["the Major Program of National Natural Science Foundation of China","Guangdong Province Fund for Distinguished Young Scholars","National Key R&D Program of China","the General Program of National Natural Science Foundation of China","Natural Science Foundation of Guangdong Province","National Natural Science Foundation of China","Guangdong Provincial Key Laboratory of Synthetic Genomics"],"pagination":["87-100"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9510856"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["20(1)"],"pubmed_abstract":["Proximity labeling catalyzed by promiscuous enzymes, such as APEX2, has emerged as a powerful approach to characterize multiprotein complexes and protein-protein interactions. However, current methods depend on the expression of exogenous fusion proteins and cannot be applied to identify proteins surrounding post-translationally modified proteins. To address this limitation, we developed a new method to label proximal proteins of interest by antibody-mediated protein A-ascorbate peroxidase 2 (pA-APEX2) labeling (AMAPEX). In this method, a modified protein is bound in situ by a specific antibody, which then tethers a pA-APEX2 fusion protein. Activation of APEX2 labels the nearby proteins with biotin; the biotinylated proteins are then purified using streptavidin beads and identified by mass"],"journal":["Genomics, proteomics & bioinformatics"],"pubmed_title":["Defining Proximity Proteome of Histone Modifications by Antibody-mediated Protein A-APEX2 Labeling."],"pmcid":["PMC9510856"],"funding_grant_id":["31971354","32070610","2021B1515020109","32090031","2019YFA0903803","32000580","2020B1515120034","2019B030301006"],"pubmed_authors":["Bouchonville KJ","Chan K","Zhao W","Wen Q","Gan H","Li N","Peng H","Li X","Offer SM","Gao Y","Wang W","Wang Z","Zhou J"],"additional_accession":[]},"is_claimable":false,"name":"Defining Proximity Proteome of Histone Modifications by Antibody-mediated Protein A-APEX2 Labeling.","description":"Proximity labeling catalyzed by promiscuous enzymes, such as APEX2, has emerged as a powerful approach to characterize multiprotein complexes and protein-protein interactions. However, current methods depend on the expression of exogenous fusion proteins and cannot be applied to identify proteins surrounding post-translationally modified proteins. To address this limitation, we developed a new method to label proximal proteins of interest by antibody-mediated protein A-ascorbate peroxidase 2 (pA-APEX2) labeling (AMAPEX). In this method, a modified protein is bound in situ by a specific antibody, which then tethers a pA-APEX2 fusion protein. Activation of APEX2 labels the nearby proteins with biotin; the biotinylated proteins are then purified using streptavidin beads and identified by mass","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Feb","modification":"2026-05-27T22:53:37.873Z","creation":"2025-04-06T12:12:58.717Z"},"accession":"S-EPMC9510856","cross_references":{"pubmed":["34555496"],"doi":["10.1016/j.gpb.2021.09.003"]}}