An extract of Artemisia dracunculus L. inhibits ubiquitin-proteasome activity and preserves skeletal muscle mass in a murine model of diabetes. [PDF]
PLoS ONE, 2013 Impaired insulin signaling is a key feature of type 2 diabetes and is associated with increased ubiquitin-proteasome-dependent protein degradation in skeletal muscle. An extract of Artemisia dracunculus L.
Heather Kirk-Ballard +8 more
doaj +1 more source
The degradation of p53 and its major E3 ligase Mdm2 is differentially dependent on the proteasomal ubiquitin receptor S5a. [PDF]
, 2013 p53 and its major E3 ligase Mdm2 are both ubiquitinated and targeted to the proteasome for degradation. Despite the importance of this in regulating the p53 pathway, little is known about the mechanisms of proteasomal recognition of ubiquitinated p53 and
A Arlt +93 more
core +3 more sources
Characterization of the ubiquitylating components of the human malaria parasite's protein degradation pathway. [PDF]
PLoS ONE, 2012 Ubiquitin-dependent protein degradation within malarial parasites is a burgeoning field of interest due to several encouraging reports of proteasome inhibitors that were able to confer antimalarial activity. Despite the growing interest in the Plasmodium
Duk-Won D Chung +4 more
doaj +1 more source
Proteasome Inhibitors: Harnessing Proteostasis to Combat Disease [PDF]
, 2020 The proteasome is the central component of the main cellular protein degradation pathway. During the past four decades, the critical function of the proteasome in numerous physiological processes has been revealed, and proteasome activity has been linked
Li, Jing, Sherman, David J.
core
Chemical proteasome inhibition as a novel animal model of inner retinal degeneration in rats.
PLoS ONE, 2019 Chemical proteasome inhibition has been a valuable animal model of neurodegeneration to uncover roles for the ubiquitin-proteasome system in the central nervous system.
Masaaki Kageyama +4 more
doaj +1 more source
A Novel Peptide-Based SILAC Method to Identify the Posttranslational Modifications Provides Evidence for Unconventional Ubiquitination in the ER-Associated Degradation Pathway. [PDF]
, 2013 The endoplasmic reticulum-associated degradation (ERAD) pathway is responsible for disposing misfolded proteins from the endoplasmic reticulum by inducing their ubiquitination and degradation.
Anania, Veronica +4 more
core +3 more sources
Molecular Oncology, EarlyView.Aldehyde dehydrogenase 1A1 (ALDH1A1) is a cancer stem cell marker in several malignancies. We established a novel epithelial cell line from rectal adenocarcinoma with unique overexpression of this enzyme. Genetic attenuation of ALDH1A1 led to increased invasive capacity and metastatic potential, the inhibition of proliferation activity, and ultimately ...
Martina Poturnajova +25 more
wiley +1 more source
Nature Communications, 2017 Targeting the ubiquitin proteasome system to modulate protein homeostasis using small molecules has promising therapeutic potential. Here the authors describe Homo-PROTACS: small molecules that can induce the homo-dimerization of E3 ubiquitin ligases and
Chiara Maniaci +8 more
doaj +1 more source
Microbial Cell, 2018 Pathogenic microorganisms employ specialized virulence factors to cause disease. Biofilm formation and the production of a polysaccharide capsule are two important virulence factors in Cryptococcus neoformans, the fungal pathogen that causes ...
François L. Mayer +2 more
doaj +1 more source
Ubiquitin-Dependent and Independent Proteasomal Degradation in Host-Pathogen Interactions
Molecules, 2023 Ubiquitin, a small protein, is well known for tagging target proteins through a cascade of enzymatic reactions that lead to protein degradation. The ubiquitin tag, apart from its signaling role, is paramount in destabilizing the modified protein.
Wojciech Bialek +2 more
doaj +1 more source