Results 81 to 90 of about 27,265 (285)

UAF1 deubiquitinase complexes facilitate NLRP3 inflammasome activation by promoting NLRP3 expression

Nature Communications, 2020
NOD-like receptor protein 3 (NLRP3) detects microbial infections or endogenous danger signals and activates the NLRP3 inflammasome, which has important functions in host defense and contributes to the pathogenesis of inflammatory diseases, and thereby ...
Hui Song, Chunyuan Zhao, Zhongxia Yu, Qizhao Li, Rongzhen Yan, Ying Qin, Mutian Jia, Wei Zhao   +7 more
semanticscholar   +1 more source

Meta‐analysis fails to show any correlation between protein abundance and ubiquitination changes

FEBS Open Bio, EarlyView.
We analyzed over 50 published proteomics datasets to explore the relationship between protein levels and ubiquitination changes across multiple experimental conditions and biological systems. Although ubiquitination is often associated with protein degradation, our analysis shows that changes in ubiquitination do not globally correlate with changes in ...
Nerea Osinalde, Unai Alduntzin, Gorka Prieto, Ugo Mayor   +3 more
wiley   +1 more source

Deubiquitinases and cancer: A snapshot

Critical Reviews in Oncology/Hematology, 2016
Ubiquitination is the vital system for controlling protein degradation and regulation of basic cellular processes. Deubiquitinases (DUBs) are emerging as an important regulator of several pathways related to cancer and other diseases. Their ability to detach ubiquitin from the target substrate and regulation of signaling makes it potential target to ...
Singh, Nishant, Singh, Anuradha Bharara
openaire   +2 more sources

Mechanisms of regulation and diversification of deubiquitylating enzyme function [PDF]

, 2017
Deubiquitinating enzymes (DUBs) are proteases that reverse protein ubiquitylation and therefore modulate the outcome of this posttranslational modification.
Abdul Rehman, Akhavantabasi, Atanassov, Baker, Bingol, Borodovsky, Clague, Clague, Cohn, Coornaert, Cotto-Rios, Deng, Dufner, Eguether, Elliott, Elliott, Faronato, Feng, Floor, García-Santisteban, Gomez-Ferreria, Hassink, Heideker, Herhaus, Heride, Huang, Huang, Huang, Hutti, Jahan, Jongsma, Joo, Juang, Kayagaki, Kedersha, Kee, Kee, Kim, Kobayashi, Köhler, Koutelou, Kulathu, Kupka, Lee, Lee, Lee, Lee, Legarda, Li, Liang, Lin, Liu, Liu, Long, Lund, Ma, Mashtalir, Meulmeester, Millard, Mizuno, Naik, Nakada, Nakagawa, Nakamura, Nijman, Nijman, O'Donnell, Pahl, Perrody, Piatkov, Qiu, Redman, Reincke, Sahtoe, Samara, Scaglione, Schaeffer, Schlicher, Seki, Shao, Sims, Smogorzewska, Soares, Soncini, Sowa, Sun, Sun, Takiuchi, Tasaki, Thorne, Todi, Udeshi, Urbe, VanderLinden, Vugmeyster, Wagner, Wang, Wertz, Wertz, Wiborg, Wiener, Wijnhoven, Worden, Xu, Xu, Yan, Yang, Yang, Yang, Yao, Yao, Ye, Zeqiraj, Zhang, Zheng   +114 more
core   +3 more sources

Loss of ubiquitin-specific peptidase 18 destabilizes 14-3-3ζ protein and represses lung cancer metastasis

Cancer Biology & Therapy, 2022
Cancer metastasis is a major cause of cancer-related mortality. Strategies to reduce metastases are needed especially in lung cancer, the most common cause of cancer mortality.
Zibo Chen, Lin Zheng, Yulong Chen, Xiuxia Liu, Masanori Kawakami, Lisa Maria Mustachio, Jason Roszik, Katherine V. Ferry-Galow, Ralph E. Parchment, Xin Liu, Thorkell Andresson, Gerard Duncan, Jonathan M. Kurie, Jaime Rodriguez-Canales, Xi Liu, Ethan Dmitrovsky   +15 more
doaj   +1 more source

Mechanism of Lys6 poly-ubiquitin specificity by the L. pneumophila deubiquitinase LotA

bioRxiv, 2022
The versatility of ubiquitination to impose control over vast domains of eukaryotic biology is due, in part, to diversification through differently-linked poly-ubiquitin chains.
Gus D. Warren, Tomoe Kitao, Tyler G. Franklin, Justine V. Nguyen, P. Geurink, T. Kubori, H. Nagai, J. Pruneda   +7 more
semanticscholar   +1 more source

Targeting the ARRDC3–DRP1 Axis via hUMSC‐Derived Exosomal CRYAB for Neuroprotection in Cerebral Ischemia/Reperfusion Injury

Advanced Healthcare Materials, EarlyView.
Intranasally administered hUMSC‐derived exosomes modulate the CRYAB–ARRDC3–Drp1 axis, alleviating mitochondrial dysfunction and ferroptosis, enhancing neuronal survival, reducing oxidative stress, and promoting functional recovery in ischemia‐reperfusion injury, offering a promising therapeutic strategy for ischemic stroke.
Rong ji, Zengyu Zhang, Zhuohang Liu, Kaicheng Yang, Xueyu Mao, Min Chu, Yong Wang, Jing Zhao   +7 more
wiley   +1 more source

The function and regulation of OTU deubiquitinases [PDF]

Frontiers of Medicine, 2019
AbstractPost-translational modification of cellular proteins by ubiquitin regulates numerous cellular processes, including cell division, immune responses, and apoptosis. Ubiquitin-mediated control over these processes can be reversed by deubiquitinases (DUBs), which remove ubiquitin from target proteins and depolymerize polyubiquitin chains. Recently,
Jiansen, Du, Lin, Fu, Yingli, Sui, Lingqiang, Zhang   +3 more
openaire   +2 more sources

p53 inhibits OTUD5 transcription to promote GPX4 degradation and induce ferroptosis in gastric cancer

Clinical and Translational Medicine
Background Gastric cancer is one of the most prevalent malignant tumors within the digestive system, and ferroptosis playing a crucial role in its progression.
Junjing Zhang, Tongguan Tian, Xinxing Li, Kai Xu, Yao Lu, Xia Li, Xinyu Zhao, Ziyi Cui, Zhenxiang Wang, Yuefan Zhou, Yixin Xu, Hongchen Li, Yan Zhang, Yu Du, Lei Lv, Yanping Xu   +15 more
doaj   +1 more source

Recent Developments in Cell Permeable Deubiquitinating Enzyme Activity-Based Probes

Frontiers in Chemistry, 2019
Deubiquitinating enzymes (DUBs) function to remove or cleave ubiquitin from post-translationally modified protein substrates. There are about 100 known DUBs in the proteome, and their dysregulation has been implicated a number of disease states, but the ...
Daniel Conole, Milon Mondal, Jaimeen D. Majmudar, Edward W. Tate   +3 more
doaj   +1 more source