Parkin function in Parkinson's disease [PDF]
, 2018 Parkinson's disease (PD) is the second most common neurodegenerative disease, and is characterized by involuntary shaking, muscle rigidity, and the progressive loss of dopaminergic neurons.
Arkinson, Connor, Walden, Helen
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The proteasome lid triggers COP9 signalosome activity during the transition of Saccharomyces cerevisiae cells into quiescence. [PDF]
, 2019 The class of Cullin–RING E3 ligases (CRLs) selectively ubiquitinate a large portion of proteins targeted for proteolysis by the 26S proteasome. Before degradation, ubiquitin molecules are removed from their conjugated proteins by deubiquitinating enzymes,
Bramasole, Lylan +8 more
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A quantitative assay to monitor HSV-1 ICP0 ubiquitin ligase activity in vitro [PDF]
, 2015 The ubiquitin–proteasome system is an essential cellular process that plays a fundamental role in the regulation of protein stability. This pathway is tightly controlled by a sequential cascade of enzymatic steps that culminates in the formation of a ...
Boutell, Chris, Davido, David J.
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Synergistic recruitment of UbcH7~Ub and phosphorylated Ubl domain triggers parkin activation [PDF]
, 2018 The E3 ligase parkin ubiquitinates outer mitochondrial membrane proteins during oxidative stress and is linked to early-onset Parkinson’s disease. Parkin is autoinhibited but is activated by the kinase PINK1 that phosphorylates ubiquitin leading to ...
Aguirre, Jacob D. +9 more
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TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions
Computational and Structural Biotechnology Journal, 2023 Protein ubiquitination is a post-translation modification mediated by E3 ubiquitin ligases. The RING domain E3 ligases are the largest family of E3 ubiquitin ligases, they act as a scaffold, bringing the E2-ubiquitin complex and its substrate together to
Xiaohua Lou +7 more
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USP15 targets ALK3/BMPR1A for deubiquitylation to enhance bone morphogenetic protein signalling [PDF]
, 2014 Protein kinase ALK3/BMPR1A mediates bone morphogenetic protein (BMP) signalling through phosphorylation and activation of SMADs 1/5/8. SMAD6, a transcriptional target of BMP, negatively regulates the BMP pathway by recruiting E3 ubiquitin ligases and ...
Al-Salihi, Mazin A. +11 more
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E3 Ubiquitin Ligases and Their Therapeutic Applications in Cancers: Narrative Review
Journal of Pharmacy and Bioallied SciencesE3 ubiquitin ligases are a class of enzymes, essential for maintaining the equilibrium of cells by binding ubiquitin molecules to substrates to mark them for destruction.
Azfar Jamal
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Biology Direct, 2009 Background Eukaryotic Nucleo-Cytoplasmic Large DNA Viruses (NCLDV) encode most if not all of the enzymes involved in their DNA replication. It has been inferred that genes for these enzymes were already present in the last common ancestor of the NCLDV ...
Koonin Eugene V, Yutin Natalya
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Bioinformatics analysis identifies several intrinsically disordered human E3 ubiquitin-protein ligases [PDF]
PeerJ, 2016 The ubiquitin-proteasome system targets misfolded proteins for degradation. Since the accumulation of such proteins is potentially harmful for the cell, their prompt removal is important.
Wouter Boomsma +4 more
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Specificity determinants for lysine incorporation in staphylococcus aureus peptidoglycan as revealed by the structure of a MurE enzyme ternary complex [PDF]
, 2013 Background: MurE controls stereo chemical incorporation of Lysine or diaminopimelate into peptidoglycan stem peptides Results: The structure of S.aureus MurE reveals an unexpected lack of specificity for Lysine within the active site.
Barreteau +72 more
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