Cargando…
TDP-43 aggregation inside micronuclei reveals a potential mechanism for protein inclusion formation in ALS
Amyotrophic lateral sclerosis (ALS) is a devastating progressive neurodegenerative disease with no known etiology. The formation of pathological protein inclusions, including RNA-binding proteins such as TDP-43 and rho guanine nucleotide exchange factor (RGNEF) are a hallmark of ALS. Despite intensi...
Autores principales: | Droppelmann, Cristian A., Campos-Melo, Danae, Moszczynski, Alexander J., Amzil, Hind, Strong, Michael J. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6934605/ https://www.ncbi.nlm.nih.gov/pubmed/31882736 http://dx.doi.org/10.1038/s41598-019-56483-y |
Ejemplares similares
-
Which TDP-43 aggregates are toxic in ALS?
por: Valle, Cristiana, et al.
Publicado: (2016) -
The emerging role of guanine nucleotide exchange factors in ALS and other neurodegenerative diseases
por: Droppelmann, Cristian A., et al.
Publicado: (2014) -
DCTN1 Binds to TDP-43 and Regulates TDP-43 Aggregation
por: Deshimaru, Manami, et al.
Publicado: (2021) -
Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation
por: Gruijs da Silva, Lara A, et al.
Publicado: (2022) -
The Integral Role of RNA in Stress Granule Formation and Function
por: Campos-Melo, Danae, et al.
Publicado: (2021)