Large-scale characterization of HeLa cell nuclear phosphoproteins.

By S. Beausoleil, Mark P. Jedrychowski, Daniel Schwartz, Joshua E. Elias, J. Villén, Jiaxu Li, M. Cohn, Lewis C. Cantley, Steven P. Gygi. Proceedings of the National Academy of Sciences of the United States of America, 2004

1,378 citations recorded by the source corpus.

Subfields: Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/936a8cc748f8978c2799d3ea919759912657d5f6

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In Molecular Biology

1. Matthias Mann
2. Steven P. Gygi
3. John R. Yates III
4. Jesper V. Olsen
5. C. Ruse
6. A. Nakorchevsky
7. Florian Gnad
8. Alexey I. Nesvizhskii

In Spectroscopy

1. Matthias Mann
2. John R. Yates III
3. Steven P. Gygi
4. Jesper V. Olsen
5. C. Ruse
6. A. Nakorchevsky
7. Florian Gnad
8. Alexey I. Nesvizhskii

Citations in the corpus

• Systematic discovery of in vivo phosphorylation networks. (2007, background): “The MS/MS fragmentation spectra (Figure S7) confirmed the phosphorylation of Rad50 at the predicted ATM substrate site, S635, in agreement with published data (Beausoleil et al., 2004).”
• Human protein reference database—2006 update (2005, methodology): “For instance, 2002 phosphorylation sites were identified using mass spectrometry from HeLa cell nuclear extract in a single experiment (5).”
• A conserved MST-FOXO signaling pathway mediates oxidative-stress responses and extends life span. (2006, positive): “MS3 scans were triggered only for doubly charged ions demonstrating an intense neutral loss of phosphoric acid (Beausoleil et al., 2004).”
• Proteomics by mass spectrometry: approaches, advances, and applications. (2009, methodology): “To account for the ubiquitous presence of phosphate neutral losses, a neutral loss–triggered MS3 data– acquisition method has been introduced for phosphoproteome analysis (213).”
• Mapping protein post-translational modifications with mass spectrometry (2007, background): “html">MS/MS/MS spectrum where the phosphorylated serine or threonine residue is replaced by a dehydrated form (−18 Da”
• Decision Tree-Driven Tandem Mass Spectrometry for Shotgun Proteomics (2008, methodology): “Previous analyses relied on information present in tandem mass spectra to trigger an MS/MS/MS event, for example, neutral loss–triggered mass spectrometr”
• Quantitative Phosphoproteomics of Early Elicitor Signaling in Arabidopsis*S (2007, background): “2c), which separates phosphopeptides from the majority of the non-phosphopeptides due to differences in solution state charge (35).”
• The SCX/IMAC enrichment approach for global phosphorylation analysis by mass spectrometry (2008, background): “7) retain an additional negative charge and can be generally separated from nonphosphorylated peptides due to their reduced retention in the stationary phas”
• Quantitative Phosphoproteomics Applied to the Yeast Pheromone Signaling Pathway*S (2005, methodology): “7, has been used before for the enrichment of phosphopeptides (19).”
• Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. (2006, methodology): “Other studies have identified large numbers of phosphorylation sites, but without a functional context (Beausoleil et al., 2004).”
• Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations (2005, methodology): “Roughly 4 mg of protein were reduced, alkylated with iodoacetamide, and separated by SDS-PAGE as describe”