Cargando…
The disordered PCI‐binding human proteins CSNAP and DSS1 have diverged in structure and function
Intrinsically disordered proteins (IDPs) regularly constitute components of larger protein assemblies contributing to architectural stability. Two small, highly acidic IDPs have been linked to the so‐called PCI complexes carrying PCI‐domain subunits, including the proteasome lid and the COP9 signalo...
Autores principales: | Ruidiaz, Sarah F., Dreier, Jesper E., Hartmann‐Petersen, Rasmus, Kragelund, Birthe B. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley & Sons, Inc.
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8442969/ https://www.ncbi.nlm.nih.gov/pubmed/34272906 http://dx.doi.org/10.1002/pro.4159 |
Ejemplares similares
-
Phosphorylation of Schizosaccharomyces pombe Dss1 mediates direct binding to the ubiquitin‐ligase Dma1 in vitro
por: Jacobsen, Nina L., et al.
Publicado: (2023) -
Expanded Interactome of the Intrinsically Disordered Protein Dss1
por: Schenstrøm, Signe M., et al.
Publicado: (2018) -
The C-terminal tail of CSNAP attenuates the CSN complex
por: Füzesi-Levi, Maria G, et al.
Publicado: (2023) -
A context-dependent and disordered ubiquitin-binding motif
por: Dreier, Jesper E., et al.
Publicado: (2022) -
Structure, dynamics, and stability of the globular domain of human linker histone H1.0 and the role of positive charges
por: Martinsen, Jacob H., et al.
Publicado: (2022)