Results 11 to 20 of about 33,953 (257)

Comparative Application of BioID and TurboID for Protein-Proximity Biotinylation

open access: yesCells, 2020
BioID is a well-established method for identifying protein–protein interactions and has been utilized within live cells and several animal models. However, the conventional labeling period requires 15–18 h for robust biotinylation which may not be ideal ...
Danielle G. May   +3 more
doaj   +2 more sources

Off-the-shelf proximity biotinylation for interaction proteomics

open access: yesNature Communications, 2021
Proximity biotinylation is a powerful tool to profile interactomes, but it requires genetic engineering of the target protein. Here, the authors develop a proximity biotinylation enzyme that can be directed to the target using antibodies, enabling ...
Irene Santos-Barriopedro   +2 more
doaj   +2 more sources

AirID, a novel proximity biotinylation enzyme, for analysis of protein–protein interactions

open access: yeseLife, 2020
Proximity biotinylation based on Escherichia coli BirA enzymes such as BioID (BirA*) and TurboID is a key technology for identifying proteins that interact with a target protein in a cell or organism.
Kohki Kido   +8 more
doaj   +2 more sources

Super-resolution proximity labeling with enhanced direct identification of biotinylation sites

open access: yesCommunications Biology
Promiscuous labeling enzymes, such as APEX2 or TurboID, are commonly used in in situ biotinylation studies of subcellular proteomes or protein–protein interactions.
Sanghee Shin   +6 more
doaj   +2 more sources

Streptavidin Coverage on Biotinylated Surfaces [PDF]

open access: yesACS Applied Materials & Interfaces, 2021
Biosensors and other biological platform technologies require the functionalization of their surface with receptors to enhance affinity and selectivity. Control over the functionalization density is required to tune the platform's properties. Streptavidin (SAv) monolayers are widely used to immobilize biotinylated proteins, receptors, and DNA.
P. H. Erik Hamming, Jurriaan Huskens
openaire   +4 more sources

High-Throughput Biotinylation of Proteins [PDF]

open access: green, 2008
One of the more useful tags for a protein in biochemical experiments is biotin, because of its femtomolar dissociation constant with streptavidin or avidin. Robust methodologies have been developed for other the in vivo addition of a single biotin to recombinant protein or the in vitro enzymatic or chemical addition of biotin to a protein.
Brian K. Kay   +2 more
openalex   +4 more sources

Nonenzymatic biotinylation of histone H2A [PDF]

open access: bronzeProtein Science, 2009
AbstractHolocarboxylase synthetase (HCS, eukaryotic enzyme) and BirA (prokaryotic) are biotin protein ligases that catalyze the ATP‐dependent attachment of biotin to apocarboxylases via the reactive intermediate, bio‐5′‐AMP. In this study, we examined the in vitro mechanism of biotin attachment to histone H2A in the presence of HCS and BirA.
Shannon Healy   +4 more
openalex   +4 more sources

An unexpected strategy to alleviate hypoxia limitation of photodynamic therapy by biotinylation of photosensitizers

open access: yesNature Communications, 2022
The most common working mechanism of photodynamic therapy is based on high-toxicity singlet oxygen, which is called Type II photodynamic therapy. But it is highly dependent on oxygen consumption.
Jing An   +9 more
semanticscholar   +1 more source

Immunoproximity biotinylation reveals the axon initial segment proteome

open access: yesbioRxiv, 2023
The axon initial segment (AIS) is a specialized neuronal compartment required for action potential generation and neuronal polarity. However, understanding the mechanisms regulating AIS structure and function has been hindered by an incomplete knowledge ...
Wei Zhang   +9 more
semanticscholar   +1 more source

Engineering of ultraID, a compact and hyperactive enzyme for proximity-dependent biotinylation in living cells

open access: yesCommunications Biology, 2022
Proximity-dependent biotinylation (PDB) combined with mass spectrometry analysis has established itself as a key technology to study protein-protein interactions in living cells. A widespread approach, BioID, uses an abortive variant of the E.
Lea Kubitz   +9 more
semanticscholar   +1 more source

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