Cargando…
Characterization of distinct molecular interactions responsible for IRF3 and IRF7 phosphorylation and subsequent dimerization
IRF3 and IRF7 are critical transcription factors in the innate immune response. Their activation is controlled by phosphorylation events, leading to the formation of homodimers that are transcriptionally active. Phosphorylation occurs when IRF3 is recruited to adaptor proteins via a positively charg...
Autores principales: | Dalskov, Louise, Narita, Ryo, Andersen, Line L, Jensen, Nanna, Assil, Sonia, Kristensen, Kennith H, Mikkelsen, Jacob G, Fujita, Takashi, Mogensen, Trine H, Paludan, Søren R, Hartmann, Rune |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7672473/ https://www.ncbi.nlm.nih.gov/pubmed/33205822 http://dx.doi.org/10.1093/nar/gkaa873 |
Ejemplares similares
-
GSK3β-SCF(FBXW7α) mediated phosphorylation and ubiquitination of IRF1 are required for its transcription-dependent turnover
por: Garvin, Alexander J, et al.
Publicado: (2019) -
A ChIP–chip approach reveals a novel role for transcription factor IRF1 in the DNA damage response
por: Frontini, Mattia, et al.
Publicado: (2009) -
SPIB and BATF provide alternate determinants of IRF4 occupancy in diffuse large B-cell lymphoma linked to disease heterogeneity
por: Care, Matthew A., et al.
Publicado: (2014) -
Functional IRF3 deficiency in a patient with herpes simplex encephalitis
por: Andersen, Line Lykke, et al.
Publicado: (2015) -
Nucleosome accessibility governed by the dimer/tetramer interface
por: Böhm, Vera, et al.
Publicado: (2011)