Acylpeptide Hydrolase Inhibition as Targeted Strategy to Induce Proteasomal Down-Regulation

Acylpeptide hydrolase (APEH), one of the four members of the prolyl oligopeptidase class, catalyses the removal of N-acylated amino acids from acetylated peptides and it has been postulated to play a key role in protein degradation machinery. Disruption of protein turnover has been established as an...

Full description

Bibliographic Details
Main Authors: Palmieri, Gianna, Bergamo, Paolo, Luini, Alberto, Ruvo, Menotti, Gogliettino, Marta, Langella, Emma, Saviano, Michele, Hegde, Ramanath N., Sandomenico, Annamaria, Rossi, Mose
Format: Online
Language:English
Published: Public Library of Science 2011
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3189933/
id pubmed-3189933
recordtype oai_dc
spelling pubmed-31899332011-10-20 Acylpeptide Hydrolase Inhibition as Targeted Strategy to Induce Proteasomal Down-Regulation Palmieri, Gianna Bergamo, Paolo Luini, Alberto Ruvo, Menotti Gogliettino, Marta Langella, Emma Saviano, Michele Hegde, Ramanath N. Sandomenico, Annamaria Rossi, Mose Research Article Acylpeptide hydrolase (APEH), one of the four members of the prolyl oligopeptidase class, catalyses the removal of N-acylated amino acids from acetylated peptides and it has been postulated to play a key role in protein degradation machinery. Disruption of protein turnover has been established as an effective strategy to down-regulate the ubiquitin-proteasome system (UPS) and as a promising approach in anticancer therapy. Public Library of Science 2011-10-10 /pmc/articles/PMC3189933/ /pubmed/22016782 http://dx.doi.org/10.1371/journal.pone.0025888 Text en Palmieri et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Palmieri, Gianna
Bergamo, Paolo
Luini, Alberto
Ruvo, Menotti
Gogliettino, Marta
Langella, Emma
Saviano, Michele
Hegde, Ramanath N.
Sandomenico, Annamaria
Rossi, Mose
spellingShingle Palmieri, Gianna
Bergamo, Paolo
Luini, Alberto
Ruvo, Menotti
Gogliettino, Marta
Langella, Emma
Saviano, Michele
Hegde, Ramanath N.
Sandomenico, Annamaria
Rossi, Mose
Acylpeptide Hydrolase Inhibition as Targeted Strategy to Induce Proteasomal Down-Regulation
author_facet Palmieri, Gianna
Bergamo, Paolo
Luini, Alberto
Ruvo, Menotti
Gogliettino, Marta
Langella, Emma
Saviano, Michele
Hegde, Ramanath N.
Sandomenico, Annamaria
Rossi, Mose
author_sort Palmieri, Gianna
title Acylpeptide Hydrolase Inhibition as Targeted Strategy to Induce Proteasomal Down-Regulation
title_short Acylpeptide Hydrolase Inhibition as Targeted Strategy to Induce Proteasomal Down-Regulation
title_full Acylpeptide Hydrolase Inhibition as Targeted Strategy to Induce Proteasomal Down-Regulation
title_fullStr Acylpeptide Hydrolase Inhibition as Targeted Strategy to Induce Proteasomal Down-Regulation
title_full_unstemmed Acylpeptide Hydrolase Inhibition as Targeted Strategy to Induce Proteasomal Down-Regulation
title_sort acylpeptide hydrolase inhibition as targeted strategy to induce proteasomal down-regulation
description Acylpeptide hydrolase (APEH), one of the four members of the prolyl oligopeptidase class, catalyses the removal of N-acylated amino acids from acetylated peptides and it has been postulated to play a key role in protein degradation machinery. Disruption of protein turnover has been established as an effective strategy to down-regulate the ubiquitin-proteasome system (UPS) and as a promising approach in anticancer therapy.
publisher Public Library of Science
publishDate 2011
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3189933/
_version_ 1611479835873378304