Cargando…
Electrostatic and steric effects underlie acetylation-induced changes in ubiquitin structure and function
Covalent attachment of ubiquitin (Ub) to proteins is a highly versatile posttranslational modification. Moreover, Ub is not only a modifier but itself is modified by phosphorylation and lysine acetylation. However, the functional consequences of Ub acetylation are poorly understood. By generation an...
Autores principales: | Kienle, Simon Maria, Schneider, Tobias, Stuber, Katrin, Globisch, Christoph, Jansen, Jasmin, Stengel, Florian, Peter, Christine, Marx, Andreas, Kovermann, Michael, Scheffner, Martin |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9481602/ https://www.ncbi.nlm.nih.gov/pubmed/36114200 http://dx.doi.org/10.1038/s41467-022-33087-1 |
Ejemplares similares
-
Structural and functional consequences of NEDD8 phosphorylation
por: Stuber, Katrin, et al.
Publicado: (2021) -
The Length of a Ubiquitin Chain: A General Factor for Selective Recognition by Ubiquitin‐Binding Proteins
por: Lutz, Joachim, et al.
Publicado: (2020) -
Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy
por: Zhao, Xiaohui, et al.
Publicado: (2019) -
Fluorescently Labelled ATP Analogues for Direct Monitoring of Ubiquitin Activation
por: Hammler, Daniel, et al.
Publicado: (2020) -
Chemical proteomic profiling reveals protein interactors of the alarmones diadenosine triphosphate and tetraphosphate
por: Krüger, Lena, et al.
Publicado: (2021)