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ProteomicsUSP14 inhibition enhances Parkin-independent mitophagy in iNeurons
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. This decline in proteostasis is exacerbated in age-associated neur...
ORGANISM(S): Homo sapiens (Human) 
2024-12-18 | PXD056511 | Pride
Usp14 Mitophagy Autophagy Ups Parkin March5/mitol Pink1 
GenomicsRNA-seq of coding RNA from USP14 knockout human haploid (HAP1) cells
RNA-seq of coding RNA from USP14 knockout human haploid (HAP1) cells
PRJEB21723 | ENA
TranscriptomicsRNA-seq of coding RNA from USP14 knockout human haploid (HAP1) cells
We performed a genome-scale screen for suppressors of interferon stimulated gene (ISG) expression in human haploid cells (HAP1). Ubiquitin specific peptidase 14 (USP14) was a significant hit. In order to validate USP14 as a regulator of ISG expression, we created knockouts of USP14 in HAP1 cells usi...
ORGANISM(S): Homo sapiens 
2017-07-25 | E-MTAB-5865 | biostudies-arrayexpress
ProteomicsA ubiquitinome analysis to study the functional roles of the proteasome associated deubiquitinating enzymes USP14 and UCH37
The removal of (poly)ubiquitin (Ub) chains at the proteasome is a key step in the protein degradation pathway that determines which proteins are degraded and ultimately decides cell fate. Specific polyubiquitin linkages may lead to distinct cellular effects, with several linkage types associated wit...
ORGANISM(S): Homo sapiens (Human) 
2022-06-30 | PXD030714 | Pride
Ubiquitinome Ubiquitinomics Silac Quantitative mass spectrometry Usp14 Parallel reaction monitoring Proteasome Deubiquitinase (dub) Ubiquitin Uch37/uchl5 
GenomicsTargeting USP14 Enhances Immunotherapy Response by Reprogramming Tumor-Associated Macrophages in Colon Cancer
Targeting USP14 Enhances Immunotherapy Response by Reprogramming Tumor-Associated Macrophages in Colon Cancer
PRJNA1426383 | ENA
TranscriptomicsTargeting USP14 Enhances Immunotherapy Response by Reprogramming Tumor-Associated Macrophages in Colon Cancer
Combining immunotherapy with other treatments improves survival in colorectal cancer, yet some patients remain unresponsive. Tumor-associated macrophages (TAMs) are a key immune cell population driving this immunotherapy resistance and fostering an immunosuppressive microenvironment. To overcome thi...
ORGANISM(S): Mus musculus 
2026-03-05 | GSE320101 | GEO
GenomicsLoss of the proteasome deubiquitinase USP14 induces growth defects and a senescence phenotype in colorectal cancer cells.
Loss of the proteasome deubiquitinase USP14 induces growth defects and a senescence phenotype in colorectal cancer cells.
PRJNA1043116 | ENA
ProteomicsTargeting Ubiquitin-specific proteases (USP14) Reduces Metastatic Potential and Metabolic Activity in Cervical Cancer by Modulating MCT-4
Cervical cancer is the most common cancer among women worldwide, predominantly caused by human papillomavirus (HPV) subtypes, particularly HPV 16 and 18. Although it is largely preventable through vaccination and early detection, cervical cancer remains a significant health issue, particularly in lo...
ORGANISM(S): Homo sapiens (Human) 
2026-01-19 | PXD067901 | Pride
Chemoresistance Tcga Iu-1 inhibitor Lactate efflux Ubiquitin-specific proteases Mct-4 Molecular docking Metabolic reprogramming Usp14 Deubiquitinating enzymes (dubs) Proteomics Metastasis Cervical cancer 
TranscriptomicsLoss of the proteasome deubiquitinase USP14 induces growth defects and a senescence phenotype in colorectal cancer cells.
The proteasome-associated deubiquitinase USP14 has attracted significant attention in recent years due to its potential as a drug target. Here, we employ an inducible USP14 knockout system to dissect early phenotypic and gene expression alterations following USP14 loss. Transcriptomic analysis revea...
ORGANISM(S): Homo sapiens 
2024-04-25 | GSE248258 | GEO
UnknownUSP14 inhibition enhances Parkin-independent mitophagy in iNeurons.
Not available
S-EPMC12849831 | biostudies-literature
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