Results 71 to 80 of about 67,820 (304)
E3 Ubiquitin Ligases in Neurological Diseases: Focus on Gigaxonin and Autophagy
Frontiers in Physiology, 2020 Ubiquitination is a dynamic post-translational modification that regulates the fate of proteins and therefore modulates a myriad of cellular functions.
Léa Lescouzères, Pascale Bomont
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Arsenite binds to the RING finger domains of RNF20-RNF40 histone E3 ubiquitin ligase and inhibits DNA double-strand break repair. [PDF]
, 2014 Arsenic is a widespread environmental contaminant. However, the exact molecular mechanisms underlying the carcinogenic effects of arsenic remain incompletely understood.
Cai, Qian +8 more
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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 +3 more
wiley +1 more source
eLife, 2019 The circadian clock relies on regulated degradation of clock proteins to maintain rhythmicity. Despite this, we know few components that mediate protein degradation.
Ann Feke +6 more
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Emerging roles of the HECT-type E3 ubiquitin ligases in hematological malignancies
Discover Oncology, 2021 Ubiquitination-mediated proteolysis or regulation of proteins, ultimately executed by E3 ubiquitin ligases, control a wide array of cellular processes, including transcription, cell cycle, autophagy and apoptotic cell death.
Vincenza Simona Delvecchio +4 more
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The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells [PDF]
, 2019 The linear ubiquitin assembly complex (LUBAC) comprises 3 components: HOIP, HOIL-1, and Sharpin, of which HOIP and HOIL-1 are both members of the RBR subfamily of E3 ubiquitin ligases. HOIP catalyses the formation of Met1-linked ubiquitin oligomers (also
Axel Knebel +7 more
core +2 more sources
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 +7 more
wiley +1 more source
Role of RING-Type E3 Ubiquitin Ligases in Inflammatory Signalling and Inflammatory Bowel Disease
Mediators of Inflammation, 2020 Ubiquitination is a three-step enzymatic cascade for posttranslational protein modification. It includes the ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3).
Liguo Zhu +7 more
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Advanced Healthcare Materials, EarlyView.Osteogenic‐angiogenic cross‐talk is a vital prerequisite for vascularized bone regeneration. In this study, we investigated the effects of siRNA‐mediated silencing of two inhibitory proteins, Chordin and WWP‐1, via CaP‐NP‐loaded gelatin microparticles in osteogenically differentiated microtissues.
Franziska Mitrach +7 more
wiley +1 more source
F1000Research, 2020 Protein ubiquitylation is essential for the maintenance of cellular homeostasis. E3 ubiquitin ligases are key components of the enzymatic machinery catalyzing the attachment of ubiquitin to substrate proteins. Consequently, enzymatic dysfunction has been
Vishnu Balaji, Thorsten Hoppe
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