Mapping protein post-translational modifications with mass spectrometry
Top Cited Papers
- 27 September 2007
- journal article
- review article
- Published by Springer Science and Business Media LLC in Nature Methods
- Vol. 4 (10), 798-806
- https://doi.org/10.1038/nmeth1100
Abstract
Post-translational modifications of proteins control many biological processes, and examining their diversity is critical for understanding mechanisms of cell regulation. Mass spectrometry is a fundamental tool for detecting and mapping covalent modifications and quantifying their changes. Modern approaches have made large-scale experiments possible, screening complex mixtures of proteins for alterations in chemical modifications. By profiling protein chemistries, biologists can gain deeper insight into biological control. The aim of this review is introduce biologists to current strategies in mass spectrometry-based proteomics that are used to characterize protein post-translational modifications, noting strengths and shortcomings of various approaches.Keywords
This publication has 96 references indexed in Scilit:
- Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networksProceedings of the National Academy of Sciences of the United States of America, 2007
- Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometryProceedings of the National Academy of Sciences of the United States of America, 2007
- Large-scale phosphorylation analysis of mouse liverProceedings of the National Academy of Sciences of the United States of America, 2007
- Nitric oxide synthase generates nitric oxide locally to regulate compartmentalized protein S-nitrosylation and protein traffickingProceedings of the National Academy of Sciences of the United States of America, 2006
- Identification of S-nitrosylation motifs by site-specific mapping of the S -nitrosocysteine proteome in human vascular smooth muscle cellsProceedings of the National Academy of Sciences of the United States of America, 2006
- Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sitesProceedings of the National Academy of Sciences of the United States of America, 2006
- Multiplexed Protein Quantitation in Saccharomyces cerevisiae Using Amine-reactive Isobaric Tagging ReagentsMolecular & Cellular Proteomics, 2004
- A proteomics approach to understanding protein ubiquitinationNature Biotechnology, 2003
- Mass spectrometry-based proteomicsNature, 2003
- The origins of protein phosphorylationNature, 2002