Results 21 to 30 of about 3,826 (176)

USP14 as a Therapeutic Target Against Neurodegeneration: A Rat Brain Perspective [PDF]

open access: yesFrontiers in Cell and Developmental Biology, 2020
In the recent past, many of the deubiquitinases (DUB) were found to modulate mitochondrial clearance or mitophagy and thus they are currently projected as therapeutic targets against neurodegeneration.
Chayan Banerjee   +8 more
doaj   +3 more sources

USP14 is crucial for proteostasis regulation and α-synuclein degradation in human SH-SY5Y dopaminergic cells

open access: yesHeliyon
Ubiquitin specific protease-14 (USP14) is critical for controlling proteostasis disturbed in human disorders, including Parkinson's disease (PD). Here we investigated USP14 in the regulation of α-synuclein (α-syn) degradation via the proteasome and ...
Vignesh Srinivasan   +7 more
doaj   +2 more sources

Usp14 deficiency increases tau phosphorylation without altering tau degradation or causing tau-dependent deficits. [PDF]

open access: yesPLoS ONE, 2012
Regulated protein degradation by the proteasome plays an essential role in the enhancement and suppression of signaling pathways in the nervous system.
Youngnam N Jin   +11 more
doaj   +2 more sources

Inhibition of USP14 enhances the sensitivity of breast cancer to enzalutamide [PDF]

open access: yesJournal of Experimental & Clinical Cancer Research, 2019
Background Androgen receptor (AR) is expressed in approximately 70% of breast tumors. Recent studies increasingly support AR as a potential therapeutic target of AR-positive breast cancer.
Xiaohong Xia   +9 more
doaj   +3 more sources

Inactive USP14 and inactive UCHL5 cause accumulation of distinct ubiquitinated proteins in mammalian cells. [PDF]

open access: yesPLoS ONE, 2019
USP14 is a cysteine protease deubiquitinase associated with the proteasome and plays important catalytic and allosteric roles in proteasomal degradation.
Jayashree Chadchankar   +9 more
doaj   +2 more sources

Biallelic USP14 variants cause a syndromic neurodevelopmental disorder [PDF]

open access: yesGenetics in Medicine
Imbalances in protein homeostasis affect human brain development, with the ubiquitin-proteasome system (UPS) and autophagy playing crucial roles in neurodevelopmental disorders (NDD). This study explores the impact of biallelic USP14 variants on neurodevelopment, focusing on its role as a key hub connecting UPS and autophagy.Here, we identified ...
Ebstein, Frédéric   +23 more
openaire   +5 more sources

USP14 Inhibition Regulates Tumorigenesis by Inducing Autophagy in Lung Cancer In Vitro

open access: yesInternational Journal of Molecular Sciences, 2019
The ubiquitin–proteasome system is an essential regulator of several cellular pathways involving oncogenes. Deubiquitination negatively regulates target proteins or substrates linked to both hereditary and sporadic forms of cancer. The deubiquitinating enzyme ubiquitin-specific protease 14 (USP14) is associated with proteasomes where it trims the ...
Kyung Ho Han   +7 more
openaire   +3 more sources

Inactivation of USP14 Perturbs Ubiquitin Homeostasis and Delays the Cell Cycle in Mouse Embryonic Fibroblasts and in Fruit Fly Drosophila

open access: yesCellular Physiology and Biochemistry, 2018
Background/Aims: The 26S proteasome is the key proteolytic complex for recognition and degradation of polyubiquitinated target substrates in eukaryotes.
Jung Hoon Lee   +5 more
doaj   +2 more sources

Transient interdomain interactions in free USP14 shape its conformational ensemble

open access: yesProtein Science
AbstractThe deubiquitinase (DUB) ubiquitin‐specific protease 14 (USP14) is a dual domain protein that plays a regulatory role in proteasomal degradation and has been identified as a promising therapeutic target. USP14 comprises a conserved USP domain and a ubiquitin‐like (Ubl) domain separated by a 25‐residue linker.
Johannes Salomonsson   +5 more
openaire   +5 more sources

Usp14 is required for spermatogenesis and ubiquitin stress responses in Drosophila melanogaster [PDF]

open access: yesJournal of Cell Science, 2019
ABSTRACT Deubiquitylating (DUB) enzymes free covalently linked ubiquitin moieties from ubiquitin–ubiquitin and ubiquitin–protein conjugates, and thereby maintain the equilibrium between free and conjugated ubiquitin moieties and regulate ubiquitin-mediated cellular processes. Here, we performed genetic analyses of mutant phenotypes in
Kovács, Levente   +3 more
openaire   +5 more sources

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