Phospho.ELM: a database of phosphorylation sites—update 2011

By Holger Dinkel, Claudia Chica, Allegra Via, Cathryn M. Gould, Lars Juhl Jensen, Toby J. Gibson, Francesca Diella. Nucleic Acids Res., 2010

543 citations recorded by the source corpus.

The Phospho.ELM resource (http://phospho.elm.eu.org) is a relational database designed to store in vivo and in vitro phosphorylation data extracted from the scientific literature and phosphoproteomic analyses. The resource has been actively developed for more than 7 years and currently comprises 42 574 serine, threonine and tyrosine non-redundant phosphorylation sites. Several new features have been implemented, such as structural disorder/order and accessibility information and a conservation score. Additionally, the conservation of the phosphosites can now be visualized directly on the multiple sequence alignment used for the score calculation. Finally, special emphasis has been put on linking to external resources such as interaction networks and other databases.

Subfields: Materials Chemistry, Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/de1f8c27ecadc8ab6304f18b5f6797fb75bfe402

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

1. Desmond G. Higgins
2. Zsuzsanna Dosztányi
3. Vladimir N Uversky
4. Lukasz Kurgan
5. Fanchi Meng

In Molecular Biology

1. Zsuzsanna Dosztányi
2. Desmond G. Higgins
3. Vladimir N Uversky
4. Lukasz Kurgan
5. Gábor Erdös
6. Kazutaka Katoh
7. Zhenling Peng
8. Bálint Mészáros

In Spectroscopy

1. Desmond G. Higgins
2. Zsuzsanna Dosztányi
3. Vladimir N Uversky
4. Lukasz Kurgan

Citations in the corpus

• Prediction of protein disorder based on IUPred (2018, methodology): “61 Various other motif-centric tools, such as SLiMPrints or SLiM-Search, also rely on IUPred.”
• PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse (2011, background): “The overlap of LTP with MS sites in PSP is 48% (5229 out of 10 727 LTP sites), considerably higher than the 17% (846 out of 5095 LTP sites) previously reported (20).”
• ProViz—a web-based visualization tool to investigate the functional and evolutionary features of protein sequences (2016, background): “These modules are regularly modulated by post-translational modifications (PTMs) (10,11) and can be added or removed by alternative transcription or alternative splicing to produce protein isoforms with unique functional properties (12,13).”