Cargando…
Solution structure of the HOIL-1L NZF domain reveals a conformational switch regulating linear ubiquitin affinity
Attachment of polyubiquitin (poly-Ub) chains to proteins is a major posttranslational modification in eukaryotes. Linear ubiquitin chain assembly complex, consisting of HOIP (HOIL-1-interacting protein), HOIL-1L (heme-oxidized IRP2 Ub ligase 1), and SHARPIN (Shank-associated RH domain–interacting pr...
Autores principales: | Walinda, Erik, Sugase, Kenji, Ishii, Naoki, Shirakawa, Masahiro, Iwai, Kazuhiro, Morimoto, Daichi |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10511788/ https://www.ncbi.nlm.nih.gov/pubmed/37595872 http://dx.doi.org/10.1016/j.jbc.2023.105165 |
Ejemplares similares
-
Biological and Physicochemical Functions of Ubiquitylation Revealed by Synthetic Chemistry Approaches
por: Morimoto, Daichi, et al.
Publicado: (2017) -
Ubiquitylation Directly Induces Fold Destabilization of Proteins
por: Morimoto, Daichi, et al.
Publicado: (2016) -
Isolation and characterization of a minimal building block of polyubiquitin fibrils
por: Morimoto, Daichi, et al.
Publicado: (2018) -
Real-Time Observation of the Interaction between Thioflavin T and an Amyloid Protein by Using High-Sensitivity Rheo-NMR
por: Iwakawa, Naoto, et al.
Publicado: (2017) -
Hydrogen-Deuterium Exchange Profiles of Polyubiquitin Fibrils
por: Morimoto, Daichi, et al.
Publicado: (2018)