Cargando…
HIV-1 promotes ubiquitination of the amyloidogenic C-terminal fragment of APP to support viral replication
HIV-1 replication in macrophages and microglia involves intracellular assembly and budding into modified subsets of multivesicular bodies (MVBs), which support both viral persistence and spread. However, the cellular factors that regulate HIV-1’s vesicular replication remain poorly understood. Recen...
Autores principales: | Gu, Feng, Boisjoli, Marie, Naghavi, Mojgan H. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10349857/ https://www.ncbi.nlm.nih.gov/pubmed/37454116 http://dx.doi.org/10.1038/s41467-023-40000-x |
Ejemplares similares
-
C-terminal 37 residues of LRP promote the amyloidogenic processing of APP independent of FE65
por: Lakshmana, Madepalli K, et al.
Publicado: (2008) -
N-Terminal Ubiquitination of Amyloidogenic Proteins Triggers Removal of Their Oligomers by the Proteasome Holoenzyme
por: Ye, Yu, et al.
Publicado: (2020) -
"APP"reciating the complexity of HIV-induced neurodegenerative diseases
por: Naghavi, Mojgan H.
Publicado: (2018) -
The C-terminal 32-mer fragment of hemoglobin alpha is an amyloidogenic peptide with antimicrobial properties
por: Olari, Lia-Raluca, et al.
Publicado: (2023) -
The C-terminal amyloidogenic peptide contributes to self-assembly of Avibirnavirus viral protease
por: Zheng, Xiaojuan, et al.
Publicado: (2015)