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Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations
The activation/inactivation cycle of STAT transcription factors entails their transition between different dimer conformations. Unphosphorylated STATs can dimerize in an antiparallel conformation via extended interfaces of the globular N-domains, whereas STAT activation triggers a parallel dimer con...
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| 主要な著者: | , , , |
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| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
National Academy of Sciences
2008
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2453697/ https://ncbi.nlm.nih.gov/pubmed/18591661 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0802130105 |
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