Biotin and Related Studies

The paper introduces APEX-PS to map RNA binding proteins in cellular compartments, identifying SYNJ2BP as a mitochondrial mRNA anchor that aids stress recovery.

CBRPP identifies RNA-associated proteins in native cells without cross-linking or RNA manipulation.

The paper develops and benchmarks in vivo TurboID and miniTurbo labeling in zebrafish embryos for proximity-dependent biotinylation, enabling protein discovery in living vertebrates.

The paper develops and evaluates a proximity labeling method to study the endolysosomal proteome in human neurons, showing improved data normalization and complementary coverage compared to overexpression approaches.

This study identifies the interactome of Protocadherin-19 using BioID and proximity-dependent biotinylation, revealing interactions with Rho GTPase regulators and microtubule proteins.

This study maps RNA-protein interactions in living cells using MS2 and Cas13-based APEX2 targeting, identifying novel interactions like hTR and ALKBH5.

The paper describes a modified BirA protein that enables biotinylation of secreted proteins in Drosophila, allowing their isolation from ovaries and embryos.

The paper introduces APEX-Seq, a proximity labeling technique to map RNA localization and interactions, revealing insights into translation initiation complexes and stress granule composition.

C-BERST uses dCas9-APEX2 to map proteomes near genomic loci, identifying telomere and centromere-associated proteins.

The paper develops an integrated approach combining AP-MS and BioID to map protein interactions and molecular contexts across the human proteome.