Biotinylation of Cell Surface Proteins [PDF]
Membrane proteins are major sensors of extracellular stimuli and initiators of intracellular signal transduction, and their abundance on the cell surface in particular is often dynamically regulated even when there are no significant changes of their ...
Guo Huang
doaj +5 more sources
Comparative Application of BioID and TurboID for Protein-Proximity Biotinylation
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
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
Revealing and mitigating the inhibitory effect of serotonin on HRP-mediated protein labelling [PDF]
Proximity-dependent biotinylation coupled with mass spectrometry enables the characterization of subcellular proteomes. This technique has significantly advanced neuroscience by revealing sub-synaptic protein networks, such as the synaptic cleft and post-
Zora Chui-Kuen Chan+4 more
doaj +2 more sources
Super-resolution proximity labeling with enhanced direct identification of biotinylation sites
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
AirID, a novel proximity biotinylation enzyme, for analysis of protein–protein interactions
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
Nonenzymatic biotinylation of histone H2A [PDF]
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
High-Throughput Biotinylation of Proteins [PDF]
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
In‐Depth Cell‐Type‐Specific Proteome Landscape of the Brain from Human Amyloid‐β Overexpression Mouse Model [PDF]
Amyloid‐β (Aβ) plays a crucial role in Alzheimer's disease pathogenesis. Understanding how Aβ overexpression alters the proteome of individual brain cell types is essential but challenging due to the nature of brain tissue, which contains intermingled ...
Taekyung Ryu+6 more
doaj +2 more sources
AgrC biotinylation inhibits Staphylococcus aureus infection. [PDF]
Staphylococcus aureus (S. aureus) is a leading cause of nosocomial infections, particularly among antibiotic-resistant strains. S. aureus virulence is governed by the accessory gene regulator (Agr) quorum sensing (QS) system, which relies on AgrC, a two ...
Lijuan Qian+9 more
doaj +2 more sources