Sort   by:  
 Page size 
ProteomicsProteomic proximity mapping by rapamycin-dependent targeting of APEX2
Enhanced ascorbate peroxidase 2 (APEX2) can be used as a genetic tag that produces short-lived yet highly reactive biotin species, allowing the modification of proteins that interact with or are in very close proximity to the tagged protein, ideally within a confined compartment. Biotinylated protei...
ORGANISM(S): Homo sapiens (Human) 
2020-04-15 | PXD009783 | Pride
Apex2 Mass spectrometry Proximity labeling Silac Apex 
Proteomics4 RABs proxymity labelling - APEX2-mediated RAB proximity labeling identifies a role for RAB21 in clathrin-independent cargo sorting
APEX2-mediated proximity labeling was performed with 4 endosomal RABs allowed an efficient and comprehensive identification of their protein neighbors. APEX2-mediated proximity labeling was performed in triplicate. Protein enrichments obtained from all RABs were compared to APEX2-nude proximity labe...
ORGANISM(S): Homo sapiens (Human) 
2019-01-07 | PXD010950 | Pride
Early endosomes Apex2 Rabs Membrane trafficking 
ProteomicsDefining proximity proteomics of Histone modifications by antibody-mediated protein A-APEX2 labeling
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 su...
ORGANISM(S): Mus musculus (Mouse) 
2023-07-12 | PXD028063 | Pride
Proximity labeling  post-translationally  amapex  modified histones 
ProteomicsAPEX2 mediated proximity labeling to investigate the proximal proteome of mitochondria tethered ULK1 in wild type and fip200 knock down cells
The object of this project is to investigate the proximal proteome of ULK1 during mitophagy and the effects of a FIP200 knock down using the APEX2-mediated proximity labeling system. APEX2-ULK1 or APEX2 was fused to 2xFKBP-myc and stably expressed in a cell line stably expressing a truncated FIS1-FR...
ORGANISM(S): Homo sapiens (Human) 
2024-10-12 | PXD047277 | Pride
Fip200 Mitophagy Autophagy Frb-rapalog-fkbp interaction Ulk1 Apex2 Er 
ProteomicsC-BERST: Defining subnuclear proteomic landscapes at genomic elements with dCas9-APEX2
Mapping proteomic composition at distinct genomic loci and subnuclear landmarks in living cells has been a long-standing challenge. Here we report that dCas9-APEX2 Biotinylation at genomic Elements by Restricted Spatial Tagging (C-BERST) allows the unbiased mapping of proteomes near defined genomic ...
ORGANISM(S): Homo sapiens (Human) 
2018-05-07 | PXD009216 | Pride
Apex2 Biotinylation Centromere Proteomes Cas9 Subnuclear Telomere 
ProteomicsAPEX2-based mapping of the host-Shigella interface
To discover novel factors that modulate S. flexneri infection, we developed a proteomic-based approach based on the biotin ligation enzyme APEX2. To target the host-Shigella interface, we coated bacteria in vitro prior to infection using anti-GFP nanobody-expressing shigella and recombinant GFP-APE...
ORGANISM(S): Shigella flexneri Homo sapiens (Human) Shigella 
2026-08-17 | PXD063609 | Pride
Shigella Apex2 Human Biotin 
ProteomicsCharecterization of RBM42 interacting proteins in HCT116 cells with and without DNA damage
RNA binding motif protein 42 (RBM42) is an understudied gene mapped to 19q13.12 region and codes for a protein that consists of 480 amino acids, containing one RNA recognition motif (RRM) at its C-terminal region. We mapped the RBM42 interactome using ascorbate peroxidase (APEX2)-based proximity lab...
ORGANISM(S): Homo sapiens (Human) 
2023-11-22 | PXD034854 | Pride
Apex2 Human Rbm42 
GenomicsIn vivo-compatible spatial multi-omics via hydrogen peroxide-independent APEX2 labeling
In vivo-compatible spatial multi-omics via hydrogen peroxide-independent APEX2 labeling
PRJNA1526277 | ENA
GenomicsDirected evolution improves the catalytic efficiency of APEX2-mediated proximity-dependent RNA labeling
Directed evolution improves the catalytic efficiency of APEX2-mediated proximity-dependent RNA labeling
PRJNA1090511 | ENA
UnknownAPEX2 proximity labeling of RNA in bacteria.
Not available
S-EPMC11429957 | biostudies-literature
Sort   by:  
 Page size