Cargando…
Clinically Relevant Dimer Interface Mutants of STAT1 Transcription Factor Exhibit Differential Gene Expression
A transition from a parallel to an antiparallel dimer configuration of the transcription factor signal transducer and activator of transcription 1 (STAT1) is required for interferon (IFN)-mediated signal transduction. However, the precise molecular mechanisms linking conformational changes to target...
Autores principales: | Staab, Julia, Herrmann-Lingen, Christoph, Meyer, Thomas |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3724676/ https://www.ncbi.nlm.nih.gov/pubmed/23922848 http://dx.doi.org/10.1371/journal.pone.0069903 |
Ejemplares similares
-
A rapid conformational rearrangement of STAT1 dimers is required for termination rather than for amplification of interferon-γ signaling
por: Staab, Julia, et al.
Publicado: (2013) -
DNA binding reduces the dissociation rate of STAT1 dimers and impairs the interdimeric exchange of protomers
por: Riebeling, Theresa, et al.
Publicado: (2014) -
CDK8 as the STAT1 serine 727 kinase?
por: Staab, Julia, et al.
Publicado: (2013) -
A Conserved Motif in the Linker Domain of STAT1 Transcription Factor Is Required for Both Recognition and Release from High-Affinity DNA-Binding Sites
por: Hüntelmann, Bettina, et al.
Publicado: (2014) -
Two glutamic acid residues in the DNA-binding domain are engaged in the release of STAT1 dimers from DNA
por: Koch, Verena, et al.
Publicado: (2012)