Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae

Nature Biotechnology

Volumn 20, Issue 3, 2002, Pages 301-305

  Ficarro, Scott B ^a   McCleland, Mark L ^b   Stukenberg, P Todd ^b   Burke, Daniel J ^b   Ross, Mark M ^a   Shabanowitz, Jeffrey ^a   Hunt, Donald F ^a,b   White, Forest M ^a  

^a MDS Proteomics   (United States)

^b UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL ACTIVATION; GENES; MASS SPECTROMETRY; PROTEINS;

PHOSPHORYLATION;

BIOTECHNOLOGY;

MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOPROTEIN; PROTEIN KINASE; PROTEOME;

AMINO ACID SEQUENCE; ARTICLE; CELL LYSATE; CHROMATOGRAPHY; COVALENT BOND; DEPHOSPHORYLATION; GENOME; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN MODIFICATION; PROTEIN PHOSPHORYLATION; PROTEIN PURIFICATION; SACCHAROMYCES CEREVISIAE;

ALGORITHMS; BINDING SITES; BIOTECHNOLOGY; CHROMATOGRAPHY; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DATABASES; MASS SPECTROMETRY; PHOSPHORYLATION; PROTEINS; SACCHAROMYCES CEREVISIAE; TIME FACTORS;

SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 0036198435     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/nbt0302-301     Document Type: Article

References (10)

1. On target with a new mechanism for the regulation of protein phosphorylation
2. A multidimensional electrospray MS-based approach to phosphopeptide mapping
3. 3+) affinity chromatography
4. 2 termini
5. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
6. Codon selection in yeast
7. Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
8. A systematic approach to the analysis of protein phosphorylation
9. Subfemtomole MS and MS/MS peptide sequence analysis using nano-HPLC micro-ESI Fourier transform ion cyclotron resonance mass spectrometry
10. Phosphorylated peptides are naturally processed and presented by major histocompatibility complex class I molecules in vivo