Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome

By Y. Oda, T. Nagasu, Brian T. Chait. Nature Biotechnology, 2001

743 citations recorded by the source corpus.

Subfields: Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/09d6d5623a02501f6d7c51270ab4bae14bec46c6

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Matthias Mann
2. R. Aebersold
3. Alexey I. Nesvizhskii
4. Steven P. Gygi
5. John R. Yates III
6. Joshua E. Elias
7. Jimmy K. Eng
8. J. Villén

In Spectroscopy

1. Matthias Mann
2. John R. Yates III
3. R. Aebersold
4. Alexey I. Nesvizhskii
5. Steven P. Gygi
6. Joshua E. Elias
7. J. Villén
8. Jimmy K. Eng

Citations in the corpus

• MAPK cascade signalling and synaptic plasticity (2004, background): “and 'phospho-proteomics', in which high-sensitivity mass spectrometric methods are adapted to specifically identify phosphorylated protein”
• Mapping protein post-translational modifications with mass spectrometry (2007, background): “, including those containing reactive groups that can be further adapted for solid-phase captur”
• Proteomics: the first decade and beyond (2003, neutral): “Two covalent chemistries, one based on β-elimination reaction”
• Molecular Biologist's Guide to Proteomics (2002, background): “In one approach, phosphoproteins were enriched by conversion of phosphoserine residues to biotinylated residues (118).”
• A proteomics approach to understanding protein ubiquitination (2003, methodology): “To characterize protein phosphorylation several strategies have been developed to capture modified peptides and determine their identity on a large scal”
• Complementary Profiling of Gene Expression at the Transcriptome and Proteome Levels in Saccharomyces cerevisiae*S (2002, background): “Therefore, there is a need for the development of more comprehensive methodologies that characterize these modifications and interactions, and recent reports document significant progress toward these goals (57, 58 ).”
• The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry (2008, methodology): “Chemical approaches to modify the phosphoester have also been proposed, using β-elimination and Michael additio”
• Proteomic analysis of post-translational modifications (2003, methodology): “For example, the phosphate group can be converted to an affinity tag by a β-elimination–Michael addition reaction or by phosphoamidate chemistr”
• A method for the comprehensive proteomic analysis of membrane proteins (2003, background): “Most shotgun approaches focus on protein phosphorylations using chemical derivatization”
• Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry (2003, background): “Alternatively, proteins that contain common distinguishing structural features, such as phosphate ester group”