Human proteins with target sites of multiple post-translational modification types are more prone to be involved in disease.
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Summary
It is indicated that Mtp-proteins are significantly more inclined to participate in disease than proteins carrying no known PTM sites and the energetic effects of PTMs on the stability of PPI revealed that only a small fraction of single PTM events influence the binding energy of >2 kcal/mol, whereas the bindingEnergy can change dramatically by combinations of multiple PTM types.
- Type
- article
- Published
- 2014-05-02
- Cited by
- 35
- References
- 131
- OpenAlex
- https://openalex.org/W2317393480
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:207614203
Keywords
Posttranslational modification, Disease, Computational biology, Biology, Chemistry
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- Visualizing Post‐Translational Modifications in Protein Interaction Networks Using PTMOracle
- New bacterial transglutaminase Q-tag substrate for the development of site-specific Antibody Drug Conjugates
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