Mapping protein post-translational modifications with mass spectrometry
By E. Witze, W. Old, Katheryn Resing, Natalie G. Ahn. Nature Methods, 2007
765 citations recorded by the source corpus.
Subfields: Materials Chemistry, Spectroscopy
View Paper: https://www.semanticscholar.org/paper/b950c824c0a7ad64cb8b93a39a6fe2b2bb8e7474
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Materials Chemistry
In Spectroscopy
- Alexey I. Nesvizhskii
- Chunaram Choudhary
- Matthias Mann
- Kuo-Chen Chou
- Jüergen Cox
- R. Aebersold
- Shao-En Ong
- Jesper V. Olsen
Citations in the corpus
- The First Identification of Lysine Malonylation Substrates and Its Regulatory Enzyme* (2011, background): “Proteomes in eukaryotic cells consist of over a million molecular species of proteins, easily orders of magnitude more complex than the corresponding genomes (1, 2).”
- Decoding signalling networks by mass spectrometry-based proteomics (2010, background): “MS is ideal for studying PTMs because it is a highly specific but generic detection metho”
- Identification of lysine succinylation as a new post-translational modification (2010, background): “495" language="eng" relation="no"> Protein post-translational modifications are one of the most efficient biological mechanisms for expanding the genetic code and for regulating cellular physiolog”
- A survey of computational methods and error rate estimation procedures for peptide and protein identification in shotgun proteomics (2010, background): “There is a tremendous interest in a variety of biologically significant PTMs, including phosphorylation (cell signaling), acetylation, and methylation (epigenetics) [3].”
- pSuc-Lys: Predict lysine succinylation sites in proteins with PseAAC and ensemble random forest approach. (2016, background): “Keywords: Lysine succinylation; Sequence-coupling model; General PseAAC; Random downsampling; Ensemble random forest; pSuc-Lys web-server I. INTRODUCTION In vivo, one of the most efficient biological mechanisms for expanding the genetic code and for regulating cellular physiology is protein post-tra”