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UnknownIn vivo proteomic mapping through GFP-directed proximity-dependent biotin labelling in zebrafish.
Not available
S-EPMC7906605 | biostudies-literature
ProteomicsIdentification of MARCH2 E3 ligase-substrates using proximity-dependent biotin labeling method
MARCH2 is known to be involved in intracellular vesicular trafficking. To identify its substrates, we have recently developed a method based on proximity-dependent biotin labelling. In this protocol, the MARCH2 ubiquitin ligase of interest is expressed as a fusion to Escherichia coli biotin ligase ...
ORGANISM(S): Homo sapiens (Human) 
2019-06-06 | PXD013601 | Pride
March2 Secretory proteins E3 ligase 
ProteomicsMapping of the local proteome of the Arabidopsis chloroplast intermembrane space by proximity labelling
The chloroplast intermembrane space, located between the outer and inner envelope membranes, plays key roles in protein and lipid trafficking. Currently, the proteome of the intermembrane space is largely uncharacterized, with only a relatively few protein players identified, and thus limiting our u...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2026-07-08 | PXD072271 | Pride
Ims Lc-msms Chloroplast 
ProteomicsLAMP1 and LAMP2 proximity labelling
The aim of the study is to capture the endogenous protein interactomes of LAMP1 and LAMP2A in human neurons using proximity labelling. This was carried out using full-length LAMP1 or LAMP2A fused to the light-activated biotin ligase LOV-Turbo, in cortical neurons differentiated from human iPSCs (I3...
ORGANISM(S): Homo sapiens (Human) 
2026-01-21 | PXD067562 | Pride
Lov-turbo Lamp1 Turboid Lamp2a 
UnknownEfficient TurboID-based proximity labelling method for identifying terminal sialic acid glycosylation in living cells.
Not available
S-EPMC10157534 | biostudies-literature
ProteomicsFIKK4.1-FIKK4.2 protein environment in Plasmodium falciparum infected red blood cells
In this project we used proximity labelling to investigate the environment of 2 P.falciparum kinases, FIKK4.1 and FIKK4.2, exported in the infected red blood cell (iRBCs), by fusing them to a biotin ligase. Peptide-level analysis was used to obtain more information about the topography of these 2 ki...
ORGANISM(S): Homo sapiens (Human) Plasmodium falciparum NF54 
2025-05-20 | PXD048966 | Pride
Plasmodium falciparum Exported fikk kinases Peptide-level proximity labelling Lc-ms/ms 
ProteomicsIdentification of novel Kv1.3 channel-interacting proteins using proximity labelling in T-cells
Potassium channels regulate membrane potential, calcium flux, cellular activation and effector functions of adaptive and innate immune cells. The voltage-activated Kv1.3 channel is an important regulator of T cell-mediated autoimmunity and microglia-mediated neuroinflammation. Kv1.3 channels, via pr...
ORGANISM(S): Homo sapiens (Human) 
2026-03-23 | PXD059644 | Pride
Autoimmune disease T-cells Potassium channel Kv1.3 
ProteomicsOla1p trafficking indicates an interaction network between mitochondria, Lipid droplets and stress granules in times of stress
Protein aggregates arise naturally under normal physiological conditions, but their formation is accelerated by age or stress-induced protein misfolding. One of the proteins that accumulate upon stress in yeast cells is Ola1p, know as the “super aggregator” Using a proximity labelling approach based...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-01-26 | PXD045513 | Pride
Protein detoxification  protein aggregation  protein shuttling  stress response: lipid droplets  mitochondria  proximity labelling  turboid 
UnknownProximity labelling reveals VPS13C as a regulator of Salmonella-containing vacuole fission.
Not available
S-EPMC12492975 | biostudies-literature
ProteomicsTRAIP regulates DNA double-strand break-induced ATM activation
TRAIP is a functional E3 ubiquitin ligase with a RING finger domain at the N-terminal end. To find TRAIP partners and substrates we used a proximity-dependent biotinylation assay (Bio-ID) which can identify direct protein-protein interaction but also proteins building a complex without requiring di...
ORGANISM(S): Homo sapiens (Human) 
2024-05-07 | PXD006715 | Pride
Human cells Protein interactions Dna damage Orbitrap Proximity labelling Bioid Tandem ms 
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