Biotin and Related Studies

This paper demonstrates that streptavidin-based imaging outperforms immunofluorescence in detecting low-abundance or inaccessible proteins and reveals dynamic protein interactions.

The paper improves TurboID-mediated proximity labeling by optimizing enrichment and analysis methods, identifying 160 SPY interactors including 100 novel ones.

The paper defines the axon initial segment proteome using immunoproximity biotinylation and identifies SCRIB as a highly enriched AIS protein.

The paper introduces ecTurboID, a method to profile extracellular protein interactions, identifying LDLR as a new EGF-dependent EGFR partner.

The paper identifies proteins that bind the FAS1 mRNA in yeast during the cell cycle and shows Tdh3p's role in regulating its translation and cell cycle progression.

This paper introduces PhoxID, a light-activated proximity labeling method to study receptor interactomes in live mice with minute-order temporal resolution.

This paper introduces LOV-Turbo, a light-regulated proximity labeling tool that enhances spatial and temporal control of proteomic mapping in living cells.

The paper introduces SPIDER, a method using pupylation and streptavidin-biotin to identify protein-biomolecule interactions, demonstrating its application in various biological contexts.

The paper uses TurboID-NES to profile proteomes of microglial and neuronal cell lines, showing it captures a significant portion of the proteome and responds to LPS treatment.

The paper introduces O-MAP, a method for discovering RNA-interacting proteins, transcripts, and genomic loci in situ with high precision and without genetic manipulation.

The paper develops ABOLISH, a method to reduce endogenous biotinylation in yeast, enabling more accurate detection of both stable and transient protein interactions using biotin ligases.

This paper develops a novel anti-KPNB1 monoclonal antibody for BAR analysis, revealing new importin β1 interactors and expanding its known functions beyond nucleocytoplasmic transport.

The paper introduces a method to identify small molecule protein targets using engineered biotin ligases and chimeric chemical probes, demonstrating its applicability with various inhibitors.

This paper introduces Cal-ID, a tool that records calcium signaling and neuronal activity by biotinylating nearby proteins, enabling high-resolution molecular mapping.

This study uses proximity labeling to monitor protein import into the endoplasmic reticulum in living cells and identifies factors influencing ER protein import.

The paper uses proximity labeling and mass spectrometry to identify proteins associated with internalized EGFR, revealing TFG's role in endosomal sorting.

The paper maps the interactome and substrates of human receptor tyrosine kinases using AP-MS, BioID, and kinase assays, revealing interactions and functions of both well-known and understudied RTKs.

The paper uses subcellular proteomics to show Parkinson's disease-linked genes are enriched in axons of dopaminergic neurons in the mouse brain.

The paper identifies CLUH interactome in mammalian cells, revealing its association with SPAG5 and proximity to mitochondrial protein translation.

This paper introduces Mandi, a novel chemical inducer of protein proximity, and demonstrates its use in cell culture and living organisms for protein manipulation.

This study introduces Halo-seq, a method for quantifying subcellular RNA populations, and finds that AU-rich elements are enriched in the nucleus and their export depends on HuR.

The paper introduces AMAPEX, a method to label proximal proteins of post-translationally modified proteins using antibody-mediated protein A-APEX2 labeling, and validates it with histone modification profiling.

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

The paper develops a method to profile cell-type specific subcellular proteomes in the mouse brain using APEX2 proximity labeling.

Profiling 192 subcellular markers by proximity-dependent biotinylation (BioID) in human HEK 293 cells maps 4,145 proteins across 32 compartments via 35,902 interactions, available with analysis tools at humancellmap.org.

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.