N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum.
Amino-terminal acetylation is probably the most common protein modification in eukaryotes with as many as 50%-80% of proteins reportedly altered in this way. Here we report a systematic analysis of the predicted N-terminal processing of cytosolic proteins versus those destined to be sorted to the se...
Guardado en:
Autores principales: | Gabriella M A Forte, Martin R Pool, Colin J Stirling |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2011
|
Materias: | |
Acceso en línea: | https://doaj.org/article/60376e1c97c340798328344ab8afaec3 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Towards a functional understanding of protein N-terminal acetylation.
por: Thomas Arnesen
Publicado: (2011) -
An alternative pathway for membrane protein biogenesis at the endoplasmic reticulum
por: Sarah O’Keefe, et al.
Publicado: (2021) -
Identification and functional characterization of N-terminally acetylated proteins in Drosophila melanogaster.
por: Sandra Goetze, et al.
Publicado: (2009) -
Endoplasmic reticulum acetyltransferases Atase1 and Atase2 differentially regulate reticulophagy, macroautophagy and cellular acetyl-CoA metabolism
por: Michael J. Rigby, et al.
Publicado: (2021) -
Function and molecular mechanism of N-terminal acetylation in autophagy
por: Tianyun Shen, et al.
Publicado: (2021)