Results 61 to 70 of about 27,539 (236)

Deubiquitination in virus infection

Virology, 2007
Post-translational modification of proteins and peptides by ubiquitin, a highly evolutionarily conserved 76 residue protein, and ubiquitin-like modifiers has emerged as a major regulatory mechanism in various cellular activities. Eukaryotic viruses are known to modulate protein ubiquitination to their advantage in various ways.
openaire   +2 more sources

USP10 deubiquitinates Tau, mediating its aggregation

Cell Death & Disease, 2022
AbstractNormal Tau promotes the assembly and stabilization of microtubules, thus, maintaining axon transport. In Alzheimer’s disease (AD), Tau aggregation causes it to lose these above-mentioned functions. However, the molecular mechanism leading to Tau aggregation in AD remains ambiguous.
Zhen Wei, Kuan Zeng, Jichang Hu, Xing Li, Fang Huang, Bin Zhang, Jian-Zhi Wang, Rong Liu, Hong-Lian Li, Xiaochuan Wang   +9 more
openaire   +3 more sources

Cleavage‐Resistant CYLD Protects Against Autoimmune Hepatitis

Advanced Science, EarlyView.
Proteolytic cleavage of the deubiquitinase CYLD emerges as a critical driver of autoimmune hepatitis. TNFα‐induced CYLD loss in macrophages amplifies S100A9‐triggered MAPK activation, leading to excessive chemokine production and hepatic inflammation. Pharmacological inhibition of MEK signaling effectively attenuates experimental disease, highlighting ...
Han Liu, Chen Su, Jianling Liu, Mingyan Xing, Xiaoxia Wu, Lingxia Wang, Xiaoming Zhao, Hanwen Zhang, YangYang Xie, YangYang Wang, Hong Li, Yu Li, Ming Li, Haibing Zhang   +13 more
wiley   +1 more source

Screening of DUB activity and specificity by MALDI-TOF mass spectrometry [PDF]

, 2014
Deubiquitylases (DUBs) are key regulators of the ubiquitin system which cleave ubiquitin moieties from proteins and polyubiquitin chains. Several DUBs have been implicated in various diseases and are attractive drug targets. We have developed a sensitive
A Iphofer, A Kovalenko, A van der Horst, AC Faesen, AK Al-Hakim, AM Oliveira, B Nicholson, C Kondapalli, C Reverdy, D Bungert, D Komander, D Komander, D Komander, DW Lee, E Graner, E Szajli, EW Harhaj, F Colland, F El Oualid, F Ikeda, FE Reyes-Turcu, G Nicastro, H Mistry, HB Kramer, J Chen, J Hemelaar, J Liang, J McCullough, JF McGouran, JW Pierce, K Keusekotten, K Saigoh, L Daviet, LC Dang, LV Pham, M Altun, M Colombo, M Karas, M Li, M Pulvino, MJ Clague, MJ Lee, MK Hospenthal, N Krishnan, NL Anderson, OW Huang, P Cohen, P Rufenacht, R Ekkebus, RA Horton, S Strickson, S Virdee, SD Sherrod, SJ Orcutt, SM Nijman, SM Nijman, SP Shah, TE Messick, TE Mevissen, U Hassiepen, Y Liu, Y Takano, Y Zhang   +62 more
core   +3 more sources

OTUD6A in Airway Epithelial Cells Exacerbates Allergic Asthma by Promoting Airway Inflammation and Airway Remodeling Through Deubiquitination of hResistin/mRELMα

Advanced Science, EarlyView.
This study elucidates a novel mechanistic role of the deubiquitinase OTUD6A in asthma pathogenesis, uncovering its regulatory function in airway inflammation and airway remodeling through the stabilization of hResistin/mRELMα. This study offers a novel regulatory axis (OTUD6A‐hResistin/mRELMα) in asthma pathogenesis and OTUD6A inhibition as a potential
Weiting Pan, Xinru Xi, Wei Dai, Tingfang Xiao, Yeqing Chen, Xuanyu Chen, Xiangting Ge, Chengguang Zhao, Hui Zhang, Yali Zhang, Weixi Zhang   +10 more
wiley   +1 more source

Epidermal Growth Factor‐Like Repeats and Discoidin I‐Like Domains 3 Deficiency Attenuates Dilated Cardiomyopathy by Inhibiting Ubiquitin Specific Peptidase 10 Dependent Smad4 Deubiquitination

Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease
Background Dilated cardiomyopathy (DCM) is the leading cause of heart failure with a poor prognosis. Recent studies suggest that endothelial to mesenchymal transition (EndMT) may be involved in the pathogenesis and cardiac remodeling during DCM ...
Mengmeng Zhao, Zihui Zheng, Shanshan Peng, Yao Xu, Jishou Zhang, Jianfang Liu, Wei Pan, Zheng Yin, Shuwan Xu, Cheng Wei, Menglong Wang, Jun Wan, Juan‐Juan Qin   +12 more
doaj   +1 more source

Proteasome Lid Bridges Mitochondrial Stress with Cdc53/Cullin1 NEDDylation Status [PDF]

, 2019
Cycles of Cdc53/Cullin1 rubylation (a.k.a NEDDylation) protect ubiquitin-E3 SCF (Skp1-Cullin1-F-box protein) complexes from self-destruction and play an important role in mediating the ubiquitination of key protein substrates involved in cell cycle ...
Bramasole, L., Gefen, E., Glickman, M. H., Gurevich, S., Jimenez-Morales, D., Johnson, J., Klein, Y., Krogan, N. J., Panat, N., Pick, E., Radzinski, M., Reichmann, D., Reis, N., Rinaldi, T., Sinha, A.   +14 more
core   +1 more source

Antagonistic Ubiquitin Switching by USP7 and RNF40 Orchestrates KDM6A Homeostasis to License Coronavirus Susceptibility

Advanced Science, EarlyView.
We identify an antagonistic ubiquitin circuit that controls cellular permissiveness to multiple coronaviruses. The deubiquitinase USP7 stabilizes the epigenetic regulator KDM6A to upregulate viral receptors, while the E3 ligase RNF40 degrades KDM6A by catalyzing K6/K11‐ubiquitin chains of KDM6A for autophagic degradation.
Meng‐Zhuo Huang, Zhong‐Yuan Yang, Shi Wang, Yan Ge, Lan Lin, Mia Madel Alfajaro, Renata B. Filler, Wan‐Yao Song, Ming‐Zhu Kong, Jin Wei   +9 more
wiley   +1 more source

Elucidating the role of ubiquitination and deubiquitination in osteoarthritis progression

Frontiers in Immunology, 2023
Osteoarthritis is non-inflammatory degenerative joint arthritis, which exacerbates disability in elder persons. The molecular mechanisms of osteoarthritis are elusive. Ubiquitination, one type of post-translational modifications, has been demonstrated to
Chenxiao Zheng, Jiayi Chen, Yurui Wu, Xiaochao Wang, Yongan Lin, Lilu Shu, Wenjun Liu, Peter Wang   +7 more
doaj   +1 more source

CHARACTERIZATION OF THE UBIQUITIN LIGASE, UBE4B, IN ENDOCYTIC TRAFFICKING [PDF]

, 2017
Endocytosis is a process by which cells internalize membrane proteins to remove them from the plasma membrane, allowing cells to regulate the cell surface expression of transmembrane proteins.
Sirisaengtaksin, Natalie, Sirisaengtaksin, Natalie   +1 more
core   +1 more source