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204 results
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Page 1
BioID: A Screen for Protein-Protein Interactions.
Roux KJ, et al. Curr Protoc Protein Sci 2018. PMID 29516480 Free PMC article.
The ligase is fused to a protein of interest and expressed in cells, where it biotinylates proximal endogenous proteins. Because it is a rare protein modification in nature, biotinylation of these endogenous proteins by BioID fusion proteins enables their selective isolation and identification with standard biotin-affinity capture. Proteins identified by BioID are candidate interactors for the protein of interest. BioID can be applied to insoluble proteins, can identify weak and/or transient interactions, and is amenable to temporal regulation. ...
The ligase is fused to a protein of interest and expressed in cells, where it biotinylates proximal endogenous proteins. Becau …
Expression and purification of E. coli BirA biotin ligase for in vitro biotinylation.
Li Y and Sousa R. Protein Expr Purif 2012. PMID 22227598 Free PMC article.
As a complementary approach to in vivo biotinylation of Avi-tag-bearing proteins, we developed a protocol for producing recombinant BirA ligase for in vitro biotinylation. The target protein was expressed as both thioredoxin and MBP fusions, and was released from the corresponding fusion by TEV protease. ...
As a complementary approach to in vivo biotinylation of Avi-tag-bearing proteins, we developed a protocol for producing recombinant …
RNA-protein interaction detection in living cells.
Ramanathan M, et al. Nat Methods 2018. PMID 29400715 Free PMC article.
RNA-protein interactions play numerous roles in cellular function and disease. Here we describe RNA-protein interaction detection (RaPID), which uses proximity-dependent protein labeling, based on the BirA* biotin ligase, to rapidly identify the proteins that bind RNA sequences of interest in living cells. ...To improve the BirA*-labeling component of RaPID, moreover, a new mutant BirA* was engineered from Bacillus subtilis, termed BASU, that enables >1,000-fold faster kinetics and >30-fold increased signal-to-noise ratio over the prior standard Escherichia coli BirA*, thereby enabling direct study of RNA-protein interactions in living cells on a timescale as short as 1 min....
RNA-protein interactions play numerous roles in cellular function and disease. Here we describe RNA-protein interaction detect …
An improved smaller biotin ligase for BioID proximity labeling
Kim DI, et al. Mol Biol Cell 2016. PMID 26912792 Free PMC article.
The BioID method uses a promiscuous biotin ligase to detect protein-protein associations as well as proximate proteins in living cells. ...BioID2 enables more-selective targeting of fusion proteins, requires less biotin supplementation, and exhibits enhanced labeling of proximate proteins. ...
The BioID method uses a promiscuous biotin ligase to detect protein-protein associations as well as proximate proteins
A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells.
Roux KJ, et al. J Cell Biol 2012. PMID 22412018 Free PMC article.
We have developed a new technique for proximity-dependent labeling of proteins in eukaryotic cells. Named BioID for proximity-dependent biotin identification, this approach is based on fusion of a promiscuous Escherichia coli biotin protein ligase to a targeting protein. BioID features proximity-dependent biotinylation of proteins that are near-neighbors of the fusion protein. Biotinylated proteins may be isolated by affinity capture and identified by mass spectrometry. ...
We have developed a new technique for proximity-dependent labeling of proteins in eukaryotic cells. Named BioID for proximity-depende …
Site-specific biotinylation of purified proteins using BirA.
Fairhead M and Howarth M. Methods Mol Biol 2015. PMID 25560075 Free PMC article.
Therefore labeling of purified proteins by biotin is a powerful way to achieve protein capture, immobilization, and functionalization, as well as multimerizing or bridging molecules. ...AviTag can conveniently be added genetically at the N-terminus, C-terminus, or in exposed loops of a target protein. We describe here procedures for AviTag insertion by inverse PCR, purification of BirA fused to glutathione-S-transferase (GST-BirA) from E. coli, BirA biotinylation of purified protein, and gel-shift analysis by SDS-PAGE to quantify the extent of biotinylation....
Therefore labeling of purified proteins by biotin is a powerful way to achieve protein capture, immobilization, and functional …
Towards improving proximity labeling by the biotin ligase BirA.
Oostdyk LT, et al. Methods 2019. PMID 30419333
The most widely used proximity labeling method is BioID, which features a mutant biotin ligase BirA(Arg118Gly), termed BirA(*), fused to a protein of interest. ...BioID using a BirA(Arg118Lys)-Lamin A fusion enabled identification of PCNA as a lamina-proximal protein in HEK293T cells, a finding that was validated by immunofluorescence microscopy. ...
The most widely used proximity labeling method is BioID, which features a mutant biotin ligase BirA(Arg118Gly), termed BirA(*) …
In Vivo Biotinylation of Antigens in E. coli
Gräslund S, et al. Methods Mol Biol 2017. PMID 28470616
Site-specific biotinylation of proteins is often the method of choice to enable efficient immobilization of a protein on a surface without interfering with protein folding. ...Here we describe a method of in vivo biotinylation of proteins during expression in E. coli, by tagging the protein with the short biotin acceptor peptide sequence, Avi tag, and co-expression of the E. coli biotin ligase (BirA) resulting in precise biotinylation of a specific lysine residue in the tag....
Site-specific biotinylation of proteins is often the method of choice to enable efficient immobilization of a protein on a sur …
Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor.
Weaver LH, et al. Protein Sci 2001. PMID 11714930 Free PMC article.
A model is suggested for the complex between the biotin repressor of Escherichia coli, BirA, and BCCP, the biotin carboxyl carrier protein to which BirA transfers biotin. ...The unique feature of the proposed interaction between BirA and BCCP is that it uses the same beta-sheet region on the surface of BirA that the protein uses for homodimerization into a form competent to bind DNA. ...
A model is suggested for the complex between the biotin repressor of Escherichia coli, BirA, and BCCP, the biotin carboxyl carrier …
E-cadherin interactome complexity and robustness resolved by quantitative proteomics.
Guo Z, et al. Sci Signal 2014. PMID 25468996 Free PMC article.
Moreover, by tagging identified proteins with GFP (green fluorescent protein), we determined the subcellular localization of 83 putative E-cadherin-proximal proteins and identified 24 proteins that were previously uncharacterized as part of adherens junctions. We constructed and characterized a comprehensive E-cadherin interaction network of 79 published and 394 previously uncharacterized proteins using a structure-informed database of protein-protein interactions. ...
Moreover, by tagging identified proteins with GFP (green fluorescent protein), we determined the subcellular localization of 8 …
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