Results 71 to 80 of about 68,518 (300)
E3-ubiquitin ligases and recent progress in osteoimmunology
Ubiquitin-mediated proteasomal degradation is a post-transcriptional protein modification that is comprised of various components including the 76-amino acid protein ubiquitin (Ub), Ub-activating enzyme (E1), Ub-conjugating enzyme (E2), ubiquitin ligase (
Yosuke Asano +8 more
doaj +1 more source
Meta‐analysis fails to show any correlation between protein abundance and ubiquitination changes
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
Small Molecule Modulators of RING-Type E3 Ligases: MDM and Cullin Families as Targets
Ubiquitin–proteasome system (UPS) is a primary signaling pathway for regulation of intracellular protein levels. E3 ubiquitin ligases, substrate-specific members of the UPS, represent highly attractive protein targets for drug discovery.
Emil Bulatov +4 more
doaj +1 more source
E3 Ubiquitin Ligases in Neurological Diseases: Focus on Gigaxonin and Autophagy
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
doaj +1 more source
UBP12 and UBP13 negatively regulate the activity of the ubiquitin-dependent peptidases DA1, DAR1 and DAR2 [PDF]
Protein ubiquitination is a very diverse post-translational modification leading to protein degradation or delocalization, or altering protein activity. In Arabidopsis thaliana, two E3 ligases, BIG BROTHER (BB) and DA2, activate the latent peptidases DA1,
Chen, Ying +10 more
core +1 more source
Nanotherapies for Atherosclerosis: Targeting, Catalysis, and Energy Transduction
Atherosclerosis management is hindered by poor drug targeting and plaque heterogeneity. Nanotechnology overcomes these barriers via three core strategies: (1) target‐engineered nanocarriers that achieve lesion‐specific precision via ligand modification, biomimetic camouflage, stimuli‐responsive release, and self‐propelling nanomotors; (2) catalytic ...
Yuqi Yang +4 more
wiley +1 more source
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
doaj +1 more source
Emerging roles of the HECT-type E3 ubiquitin ligases in hematological malignancies
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
doaj +1 more source
RNF213 is characterized as a dual‐functional antiviral effector. It directly mediates the degradation of the influenza A virus nucleoprotein (NP) while simultaneously activating the MDA5‐mediated innate immune signaling pathway. This coordinated response establishes a powerful host defense system against viral infection. ABSTRACT Influenza A virus (IAV)
Haoning Li +5 more
wiley +1 more source
Role of RING-Type E3 Ubiquitin Ligases in Inflammatory Signalling and Inflammatory Bowel Disease
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
doaj +1 more source

