Biotinylation of proteins in vivo: a useful posttranslational modification for protein analysis.
Cronan
J E
JE
Department of Microbiology, University of Illinois, Urbana 61801, USA.
Reed
K E
KE
D000595:Amino Acid Sequence; D000818:Animals; D017360:Arabidopsis / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D019921:Biotinylation; D019731:Carbon-Nitrogen Ligases / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D029968:Escherichia coli Proteins; D006801:Humans; D007711:Klebsiella pneumoniae / Q000201:enzymology; D017017:Methanococcus / Q000201:enzymology; D008969:Molecular Sequence Data; D009876:Operon; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D012097:Repressor Proteins; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D018411:Spodoptera; D014157:Transcription Factors
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D011506:Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D019731:Carbon-Nitrogen Ligases; C023312:holocarboxylase synthetases; C058125:birA protein, E coli