Results 71 to 80 of about 47,588 (257)
Role of E3 ubiquitin ligases in lung cancer
E3 ubiquitin ligases are a large family of proteins that catalyze the ubiquitination of many protein substrates for targeted degradation by the 26S proteasome. Therefore, E3 ubiquitin ligases play an essential role in a variety of biological processes including cell cycle regulation, proliferation and apoptosis.
Snoek, B.C. +3 more
openaire +2 more sources
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
The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity
Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav +4 more
wiley +1 more source
Functional Dissection of a HECT Ubiquitin E3 Ligase
Ubiquitination is one of the most prevalent protein post-translational modifications in eukaryotes, and its malfunction is associated with a variety of human diseases. Despite the significance of this process, the molecular mechanisms that govern the regulation of ubiquitination remain largely unknown.
Jin-Ying, Lu +6 more
openaire +2 more sources
This study reveals that NF‐κB1‐driven TRAIP upregulation in ALD correlates with disease severity. Mechanistically, TRAIP directly binds β‐catenin via its CC domain and promotes its K48‐linked ubiquitination and degradation, which is independent of the GSK3β/β‐TrCP pathway.
Zhan Wu +13 more
wiley +1 more source
Ubiquitination is a crucial post-translational modification of proteins that mediates the degradation or functional regulation of specific proteins. This process participates in various biological processes such as cell growth, development, and signal ...
Heng-Rui Zhang +10 more
doaj +1 more source
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
doaj +1 more source
. ABSTRACT Neuroinflammation driven by microglial activation is a defining feature of Alzheimer's disease (AD), yet the molecular mechanisms sustaining this proinflammatory state remain unclear. Here, we identify the deubiquitinase OTUD7B as a critical regulator of microglial activation and AD pathology.
Luyao Li +15 more
wiley +1 more source
Role and therapeutic potential of E3s in the tumor microenvironment of hepatocellular carcinoma
Hepatocellular carcinoma (HCC) is a high-incidence, poor-prognosis malignancy worldwide, requiring new strategies for treatment. Ubiquitination, especially ubiquitination through E3 ubiquitin ligases, plays an indispensable role in the development and ...
Hailin Wang +10 more
doaj +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

