A minimal peptide substrate in biotin holoenzyme synthetase‐catalyzed biotinylation
By D. Beckett, E. Kovaleva, P. Schatz. Protein Science, 2008
757 citations recorded by the source corpus.
Subfields: Cell Biology, Organic Chemistry
View Paper: https://www.semanticscholar.org/paper/3a64ae21599d9b77746a8d705a2c50e1a2d381e7
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In Cell Biology
Citations in the corpus
- Real-Time DNA Sequencing from Single Polymerase Molecules (2009, background): “Incubate DNA polymerase carrying an N-terminal biotin-tag (Beckett et al., 1999) with 1.”
- Ribosome profiling reveals pervasive translation outside of annotated protein-coding genes. (2014, methodology): “Ribosome Affinity Purification The ribosome affinity tag construct comprised human ribosomal protein L1 fused to the biotin acceptor peptide (Beckett et al., 1999; de Boer et al., 2003), coexpressed with a biotin ligase using a 2A peptide (de Felipe et al.”
- Naive CD4(+) T cell frequency varies for different epitopes and predicts repertoire diversity and response magnitude. (2007, methodology): “The Fc domain on the alpha chain was replaced with a BirA biotinylation signal sequence (Beckett et al., 1999) generated by oligonucleotide synthesis.”
- Real-time DNA sequencing from single polymerase molecules. (2010, methodology): “For a surface derivatization providing selectively biotinylated ZMW floors (described in Section 3.2), they include nonspecific biotinylation of the enzyme (Hermanson, 1996), introduction of specific biotin tags (Beckett et al., 1999), or fusion proteins (Nilsson et al., 1997).”
- Site-specific biotinylation of purified proteins using BirA (2015, background): “BLRP (Biotin ligase recognition peptide) contains a core of AviTag and is 23 residues: (MAGGLNDIFEAQKIEWHEDTGGS) (5,49).”