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Hidden dynamic signatures drive substrate selectivity in the disordered phosphoproteome
Phosphorylation sites are hyperabundant in the eukaryotic disordered proteome, suggesting that conformational fluctuations play a major role in determining to what extent a kinase interacts with a particular substrate. In biophysical terms, substrate selectivity may be determined not just by the str...
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| Publicado no: | Proc Natl Acad Sci U S A |
|---|---|
| Main Authors: | , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
2020
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7519349/ https://ncbi.nlm.nih.gov/pubmed/32900925 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1921473117 |
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