proximity-dependent biotinylation

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1 Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill School of Medicine, Chapel Hill, NC 27599, USA. 2 Department of Pharmacology and Cancer Biology, Duke University School of Medicine, Durham, NC 27710, USA 3 Duke Cancer Institute, Duke University School of Medicine, Durham, NC 27710, USA 4 Department of Pathology, Duke University School of Medicine, Durham, NC 27710, USA (1)
1Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill School of Medicine, Chapel Hill, NC 27599, USA 2Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill School of Medicine, Chapel Hill, NC 27599, USA 3Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA (1)
1Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA 2Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA 5Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA 8Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA (1)
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Control of TurboID-dependent biotinylation intensity in proximity ligation screens

Proximity biotinylation screens are a widely used strategy for the unbiased identification of interacting or vicinal proteins. The latest generation biotin ligase TurboID has broadened the range of potential applications, as this ligase promotes an intense and faster biotinylation, even in subcellul...

ORGANISM(S): Homo sapiens (Human)

2023-03-29 | PXD040302 | Pride

Proximity-dependent biotinylation by TurboID to identify protein-protein interaction networks in yeast

The use of proximity-dependent biotinylation assays coupled to mass spectrometry (PDB-MS) has changed the field of protein-protein interactions (PPI) studies. Yet, despite the recurrent and successful use of BioID-based PPI screening in mammalian cells, the implementation of PDB-MS in yeast has not ...

ORGANISM(S): Schizosaccharomyces pombe 927

2019-05-16 | PXD013183 | Pride

Proximity-dependent biotinylation turboid yeast s. pombe rmt3 Rna exosome

Optical Sensors and Actuators for Probing Proximity-Dependent Biotinylation in Living Cells.

Not available

S-EPMC8890125 | biostudies-literature

BIOSITe: A novel method for direct detection of site specific biotinylation

Proximity-dependent biotinylation methods, such as those mediated by BioID and APEX, are being widely adopted for studying in vivo protein-protein interaction dynamics and subcellular structures. However, these along with other biotin-based technologies are severely dependent on avidin family protei...

ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse)

2017-12-19 | PXD007862 | Pride

Bioid Proximity dependent biotinylation Bcr abl Mass spectrometry Ip Peptide Biotinylation Biosite

A Versatile Lentiviral Delivery Toolkit for Proximity-dependent Biotinylation in Diverse Cell Types.

Not available

S-EPMC6210231 | biostudies-literature

Proximity-dependent biotinylation to elucidate the interactome of TNK2 non-receptor tyrosine kinase

Non-receptor tyrosine kinases represent an important class of signaling molecules which are involved in driving diverse cellular pathways. Although the large majority have been well-studied in terms of their protein binding partners, the interactomes of some important non-receptor tyrosine kinases s...

ORGANISM(S): Homo sapiens (Human)

2021-08-25 | PXD010474 | Pride

Tnk2 Human Bioid Biosite

Screening of Proximal and Interacting Proteins in Rice Protoplasts by Proximity-Dependent Biotinylation.

Not available

S-EPMC5427108 | biostudies-literature

A Toolbox for Efficient Proximity-Dependent Biotinylation in Zebrafish Embryos.

Not available

S-EPMC8383115 | biostudies-literature

Proximity-Dependent Biotinylation to Elucidate the Interactome of TNK2 Nonreceptor Tyrosine Kinase.

Not available

S-EPMC8744476 | biostudies-literature

Proximity Dependent Biotinylation: Key Enzymes and Adaptation to Proteomics Approaches.

Not available

S-EPMC7196579 | biostudies-literature

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