Results 11 to 20 of about 4,153 (179)

Function of Deubiquitinating Enzyme USP14 as Oncogene in Different Types of Cancer [PDF]

open access: yesCellular Physiology and Biochemistry, 2016
Background/Aims: Non-small cell lung cancer (NSCLC) tissues overexpress USP14, which promotes tumor cell proliferation and is associated with shorter overall survival time. Methods: The expression of USP14 was assayed in many types of cancers.
Ying Zhu   +4 more
doaj   +4 more sources

USP14 inhibition enhances Parkin-independent mitophagy in iNeurons [PDF]

open access: yesPharmacological Research
Loss of proteostasis is well documented during physiological aging and depends on the progressive decline in the activity of two major degradative mechanisms: the ubiquitin-proteasome system (UPS) and the autophagy-lysosomal pathway.
Greta Bernardo   +10 more
doaj   +4 more sources

A kinetic model for USP14 regulated substrate degradation in 26S proteasome.

open access: yesPLoS Computational Biology
Despite high-resolution structural studies on the USP14-proteasome-substrate complexes, time-resolved cryo-electron microscopy (cryo-EM) results on USP14-regulated allostery of the 26S proteasome are still very limited and a quantitative understanding of
Di Wu   +3 more
doaj   +4 more sources

Dynamic Interaction of USP14 with the Chaperone HSC70 Mediates Crosstalk between the Proteasome, ER Signaling, and Autophagy [PDF]

open access: yesiScience, 2020
Summary: USP14 is a deubiquitinating enzyme associated with the proteasome important for protein degradation. Here we show that upon proteasome inhibition or expression of the mutant W58A-USP14, association of USP14 with the 19S regulatory particle is ...
Vignesh Srinivasan   +6 more
doaj   +2 more sources

Enhancement of proteasome activity by a small-molecule inhibitor of USP14 [PDF]

open access: yesNature, 2010
Proteasomes, the primary mediators of ubiquitin-protein conjugate degradation, are regulated through complex and poorly understood mechanisms. Here we show that USP14, a proteasome-associated deubiquitinating enzyme, can inhibit the degradation of ...
Hanna, John   +25 more
core   +3 more sources

USP14: Structure, Function, and Target Inhibition [PDF]

open access: yesFrontiers in Pharmacology, 2022
Ubiquitin-specific protease 14 (USP14), a deubiquitinating enzyme (DUB), is associated with proteasomes and exerts a dual function in regulating protein degradation.
Feng Wang   +3 more
doaj   +3 more sources

USP14 promotes colorectal cancer progression by targeting JNK for stabilization

open access: yesCell Death and Disease, 2023
MAPK/JNK signaling is pivotal in carcinogenesis. However, ubiquitin-mediated homeostasis of JNK remains to be verified. Here, with results from RNA sequencing (RNA-seq) and luciferase reporter pathway identification, we show that USP14 orchestrates MAPK ...
Xue-Hua Du   +10 more
doaj   +3 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

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

Targeted therapy for cisplatin‐resistant lung cancer via aptamer‐guided nano‐zinc carriers containing USP14 siRNA

open access: yesMedComm, 2023
Cisplatin (DDP) is a common therapeutic option for non‐small cell lung carcinoma (NSCLC). However, some patients fail to respond to the DDP chemotherapy. Therefore, identifying novel biomarkers to improve the diagnosis and treatment of NSCLC is important.
Xinmin Zhao   +4 more
doaj   +2 more sources

Home - About - Disclaimer - Privacy