Quantitative Phosphoproteomics Reveals Widespread Full Phosphorylation Site Occupancy During Mitosis

By Jesper V. Olsen, M. Vermeulen, A. Santamaría, Chanchal Kumar, Martin L. Miller, Lars Juhl Jensen, Florian Gnad, Jüergen Cox, T. S. Jensen, Erich A. Nigg and 2 more. Science Signaling, 2010

1,529 citations recorded by the source corpus.

Subfields: Cell Biology, Oncology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/6977b9cb8225f3235c515cd40d4201cc41c4c489

How researchers see this paper

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

In Cell Biology

1. Matthias Mann
2. Jesper V. Olsen
3. Marc Vidal
4. Celia Fontanillo
5. Patrick Aloy
6. David E. Hill
7. M. Larance
8. Lilia M. Iakoucheva

In Oncology

1. Matthias Mann
2. Chunaram Choudhary
3. J. Harper
4. Steven P. Gygi
5. Yingming Zhao

In Spectroscopy

1. Matthias Mann
2. Jüergen Cox
3. Steven P. Gygi
4. Chunaram Choudhary
5. Stefka Tyanova
6. Alexey I. Nesvizhskii
7. Jesper V. Olsen
8. J. Villén

Citations in the corpus

• Systematic and quantitative assessment of the ubiquitin modified proteome (2011, positive): “Despite theseadvances, theoverall number ofmodificationsites is small in comparison to the extent of acetylation and phosphorylation (Choudhary et al., 2009; Huttlin et al., 2010; Olsen et al., 2010), and the extent to which ubiquitin overexpression affects the occupancy and specificity of ubiquityl”
• Multidimensional proteomics for cell biology (2015, background): “These studies have provided crucial insights into the regulation of protein properties during fundamental processes, such as cell cycle progression 83,84 , and into signalling mechanisms that affect cellular pathways, such as the epidermal growth factor signalling cascade 85 .”
• Accessibility of different histone H3-binding domains of UHRF1 is allosterically regulated by phosphatidylinositol 5-phosphate. (2014, background): “Also, acetylation of two lysine residues within the SRA was found (Choudhary et al., 2009; Dephoure et al., 2008; Olsen et al., 2010; Rigbolt et al., 2011).”
• PHOSIDA 2011: the posttranslational modification database (2010, positive): “The current version of PHOSIDA contains an additional 20 000 human phosphorylation sites from kinase enriched samples (21) or of quantified dynamics during the cell cycle (5,7).”
• Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling. (2014, methodology): “Previously, we had determined site occupancies from stable isotope labeling by amino acids in cell culture (SILAC) quantitation on the level of protein, unmodified peptide, and modified peptide (Olsen et al., 2010).”
• The endoplasmic reticulum: structure, function and response to cellular signaling (2015, background): “Inspection of large-scale phospho-proteomics studies reveals that a large number of ER-shaping proteins have identified mitosis-specific phosphorylation sites [114–121].”
• SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways (2013, methodology): “To calculate the absolute stoichiometry of Lys succinylation, we modified a previously reported algorithm (Olsen et al., 2010) that used SILAC quantification ratios of modified and unmodified peptides as well as corresponding proteins.”