Protein posttranslational modifications: phosphorylation site analysis using mass spectrometry.
Annan
Roland S
RS
Proteomics and Biological Mass Spectrometry, Department of Computational, Analytical, and Structural Sciences, GlaxoSmithKline, King of Prussia, Pennsylvania, USA.
Zappacosta
Francesca
F
D000595:Amino Acid Sequence; D002853:Chromatography, Liquid / Q000379:methods; D004268:DNA-Binding Proteins / Q000737:chemistry; D013058:Mass Spectrometry / Q000379:methods; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010748:Phosphopeptides / Q000737:chemistry; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational / Q000235:genetics / Q000502:physiology*; D020543:Proteome; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods; D014157:Transcription Factors / Q000737:chemistry
D004268:DNA-Binding Proteins; C060292:PHO4 protein, S cerevisiae; D010446:Peptide Fragments; D010748:Phosphopeptides; D010750:Phosphoproteins; D020543:Proteome; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors