Cargando…
A spider silk-derived solubility domain inhibits nuclear and cytosolic protein aggregation in human cells
Due to the inherent toxicity of protein aggregates, the propensity of natural, functional amyloidogenic proteins to aggregate must be tightly controlled to avoid negative consequences on cellular viability. The importance of controlled aggregation in biological processes is illustrated by spidroins,...
Autores principales: | Schellhaus, Anna Katharina, Xu, Shanshan, Gierisch, Maria E., Vornberger, Julia, Johansson, Jan, Dantuma, Nico P. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9135726/ https://www.ncbi.nlm.nih.gov/pubmed/35618760 http://dx.doi.org/10.1038/s42003-022-03442-5 |
Ejemplares similares
-
Cytosolic stress granules relieve the ubiquitin‐proteasome system in the nuclear compartment
por: Xu, Shanshan, et al.
Publicado: (2022) -
Functionalization of amyloid fibrils via the Bri2 BRICHOS domain
por: Biverstål, Henrik, et al.
Publicado: (2020) -
Silk Spinning in Silkworms and Spiders
por: Andersson, Marlene, et al.
Publicado: (2016) -
Conformation and dynamics of soluble repetitive domain elucidates the initial β-sheet formation of spider silk
por: Oktaviani, Nur Alia, et al.
Publicado: (2018) -
Untangling spider silk evolution with spidroin terminal domains
por: Garb, Jessica E, et al.
Publicado: (2010)