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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Ubiquitin specific peptidase 22

Top mentioned proteins: Ubiquitin, Histone, V1a, c-Myc, POLYMERASE
Papers on USP22
Expression of USP22 and Survivin is an indicator of malignant behavior in hepatocellular carcinoma.
Qi et al., Guilin, China. In Int J Oncol, Dec 2015
Ubiquitin-specific protease 22 (USP22) is a newly discovered deubiquitinating enzyme and is a cancer stem cell marker that plays a role in tumorigenesis, therapy resistance and cell cycle progression.
Usp22 deficiency impairs intestinal epithelial lineage specification in vivo.
Johnsen et al., Göttingen, Germany. In Oncotarget, Dec 2015
The Ubiquitin-specific Protease 22 (USP22) is the ubiquitin hydrolase component of the human SAGA complex which deubiquitinates histone H2B during transcription.
The deubiquitinating enzyme activity of USP22 is necessary for regulating HeLa cell growth.
Tian et al., Shijiazhuang, China. In Gene, Dec 2015
Ubiquitin-specific protease 22 (USP22) can regulate the cell cycle and apoptosis in many cancer cell types, while it is still unclear whether the deubiquitinating enzyme activity of USP22 is necessary for these processes.
Aggregation of Polyglutamine-expanded Ataxin 7 Protein Specifically Sequesters Ubiquitin-specific Protease 22 and Deteriorates Its Deubiquitinating Function in the Spt-Ada-Gcn5-Acetyltransferase (SAGA) Complex.
Hu et al., Shanghai, China. In J Biol Chem, Oct 2015
We investigated the effects of polyQ-expanded Atx7 on ubiquitin-specific protease (USP22), an interacting partner of Atx7 functioning in deubiquitination of histone H2B.
p38 mitogen-activated protein kinase inhibits USP22 transcription in HeLa cells.
Li et al., Jiujiang, China. In Biomed Rep, Jul 2015
UNASSIGNED: Elevated expression of ubiquitin-specific processing enzyme 22 (USP22) was identified in multiple types of human cancers, and was correlated with tumorigenesis and progression.
Decreased H2B monoubiquitination and overexpression of ubiquitin-specific protease enzyme 22 in malignant colon carcinoma.
Yang et al., Chengdu, China. In Hum Pathol, Jul 2015
This study aimed to evaluate the expression of H2B monoubiquitination enzyme (uH2B) and ubiquitin-specific protease enzyme 22 (USP22) in colon carcinoma and establish a correlation between the expression of these enzymes and clinicopathological parameters.
USP22 promotes tumor progression and induces epithelial-mesenchymal transition in lung adenocarcinoma.
Cai et al., Harbin, China. In Lung Cancer, Jun 2015
OBJECTIVES: Our previous study showed that USP22 as an oncogene may mediate cancer development and progression in NSCLC, but the underlying molecular mechanism remains uncharacterized.
High USP22 expression indicates poor prognosis in hepatocellular carcinoma.
He et al., Guilin, China. In Oncotarget, Jun 2015
Ubiquitin-specific protease 22 (USP22) removes ubiquitin from histones, thus regulating gene transcription.
Histone H2B monoubiquitination: roles to play in human malignancy.
Marsh et al., Sydney, Australia. In Endocr Relat Cancer, Feb 2015
The H2Bub1 enzymatic cascade involves E3 RING finger ubiquitin ligases, with the main E3 generally accepted to be the RNF20-RNF40 complex, and deubiquitinases including ubiquitin-specific protease 7 (USP7), USP22 and USP44.
Deubiquitinases and the new therapeutic opportunities offered to cancer.
Saridakis et al., Toronto, Canada. In Endocr Relat Cancer, Feb 2015
In this review, we recapitulate structure-function studies of the most studied DUBs including USP7, USP22, CYLD, UCHL1, BAP1, A20, as well as ataxin 3 and connect them to regulatory mechanisms and their growing protein interaction networks.
The Cellular Protein Complex Associated with a Transforming Region of E1A Contains c-MYC.
Chinnadurai et al., Saint Louis, United States. In J Virol, 2014
The same E1A region additionally interacted with the constituents of a deubiquitinase complex consisting of USP22, ATXN7, and ATXN7L3 via TRRAP.
Differential Genes Expression between Fertile and Infertile Spermatozoa Revealed by Transcriptome Analysis.
Rajender et al., Lucknow, India. In Plos One, 2014
Some transcripts were specific to the normozoospermic group (up-regulated: CAPNS1, FAM153C, ARF1, CFL1, RPL19, USP22; down-regulated: ZNF90, SMNDC1, c14orf126, HNRNPK), while some were specific to the asthenozoospermic group (up-regulated: RPL24, HNRNPM, RPL4, PRPF8, HTN3, RPL11, RPL28, RPS16, SLC25A3, C2orf24, RHOA, GDI2, NONO, PARK7; down-regulated: HNRNPC, SMARCAD1, RPS24, RPS24, RPS27A, KIFAP3).
SIRT1 activation by a c-MYC oncogenic network promotes the maintenance and drug resistance of human FLT3-ITD acute myeloid leukemia stem cells.
Bhatia et al., Duarte, United States. In Cell Stem Cell, 2014
This SIRT1 overexpression is related to enhanced expression of the USP22 deubiquitinase induced by c-MYC, leading to reduced SIRT1 ubiquitination and enhanced stability.
Functions of SAGA in development and disease.
Dent et al., Anderson, United States. In Epigenomics, 2014
Although the transcriptional programs regulated by SAGA in embryos are not well defined, deletion of either Gcn5 or USP22, the catalytic subunit of a deubiquitinase module in SAGA, leads to early embryonic lethality.
USP22 nuclear expression is significantly associated with progression and unfavorable clinical outcome in human esophageal squamous cell carcinoma.
Li et al., Jinan, China. In J Cancer Res Clin Oncol, 2012
Data show that USP22 protein plays an essential role in esophageal squamous cell carcinoma (ESCC) progression and has clinical potentials as a biomarker and as an attractively therapeutic target for ESCC.
The ubiquitin hydrolase USP22 contributes to 3'-end processing of JAK-STAT-inducible genes.
Henriksen et al., Charlottesville, United States. In Faseb J, 2012
RNAi-mediated knockdown of the ubiquitin hydrolase, USP22, results in 2-fold higher ubH2B, and 2-fold lower transcriptional elongation at IRF1. USP22 depletion also diminishes 3'-end cleavage/polyadenylation by 2- to 3-fold.
Knock-down of ubiquitin-specific protease 22 by micro-RNA interference inhibits colorectal cancer growth.
Dong et al., Harbin, China. In Int J Colorectal Dis, 2012
USP22 plays a crucial role in tumor formation and growth by regulating cell proliferation with USP22-dependent signaling pathway.
USP22 acts as an oncogene by the activation of BMI-1-mediated INK4a/ARF pathway and Akt pathway.
Wang et al., Harbin, China. In Cell Biochem Biophys, 2012
USP22 may act as an oncogene in CRC as it positively regulates cell cycle via both BMI-1-mediated INK4a/ARF pathway and Akt signaling pathway.
USP22 regulates cell proliferation by deubiquitinating the transcriptional regulator FBP1.
Dent et al., Anderson, United States. In Embo Rep, 2011
show that USP22 affects the expression of p21 by altering far upstream element (FUSE)-binding protein 1 (FBP1) ubiquitination
Genomic models of metastatic cancer: functional analysis of death-from-cancer signature genes reveals aneuploid, anoikis-resistant, metastasis-enabling phenotype with altered cell cycle control and activated Polycomb Group (PcG) protein chromatin silencing pathway.
Glinsky, Albany, United States. In Cell Cycle, 2006
This analysis predicts that cancer cells manifesting a stem cell-like expression profile of a death-from-cancer signature would exhibit the following features: a concomitantly increased expression of certain members of inhibitor of apoptosis protein (IAP) family (Survivin and XIAP); activation of mitotic spindle check point proteins (BUB1, BUB3, KNTC2, Mad2, PLK1, PLK4, STK6/Aurora A); and elevated levels of certain cell cycle control/marker proteins (CCNB1, CCNB2, CCND1, CCNA2, CDC2, CDC25, Ki67, USP22).
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