Cargando…
Identification of Human Proteins That Modify Misfolding and Proteotoxicity of Pathogenic Ataxin-1
Proteins with long, pathogenic polyglutamine (polyQ) sequences have an enhanced propensity to spontaneously misfold and self-assemble into insoluble protein aggregates. Here, we have identified 21 human proteins that influence polyQ-induced ataxin-1 misfolding and proteotoxicity in cell model system...
Autores principales: | Petrakis, Spyros, Raskó, Tamás, Russ, Jenny, Friedrich, Ralf P., Stroedicke, Martin, Riechers, Sean-Patrick, Muehlenberg, Katja, Möller, Angeli, Reinhardt, Anita, Vinayagam, Arunachalam, Schaefer, Martin H., Boutros, Michael, Tricoire, Hervé, Andrade-Navarro, Miguel A., Wanker, Erich E. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3420947/ https://www.ncbi.nlm.nih.gov/pubmed/22916034 http://dx.doi.org/10.1371/journal.pgen.1002897 |
Ejemplares similares
-
Aggregation of polyQ-extended proteins is promoted by interaction with their natural coiled-coil partners
por: Petrakis, Spyros, et al.
Publicado: (2013) -
Systematic interaction network filtering identifies CRMP1 as a novel suppressor of huntingtin misfolding and neurotoxicity
por: Stroedicke, Martin, et al.
Publicado: (2015) -
Model systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicity
por: Brehme, Marc, et al.
Publicado: (2016) -
HIPPIE: Integrating Protein Interaction Networks with Experiment Based Quality Scores
por: Schaefer, Martin H., et al.
Publicado: (2012) -
Dynamics of a Protein Interaction Network Associated to the Aggregation of polyQ-Expanded Ataxin-1
por: Vagiona, Aimilia-Christina, et al.
Publicado: (2020)