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The Role of NEDD4 E3 Ubiquitin-Protein Ligases in Parkinson's Disease. [PDF]
Genes (Basel), 2022 Parkinson’s disease (PD) is a debilitating neurodegenerative disease that causes a great clinical burden. However, its exact molecular pathologies are not fully understood.
Conway JA, Kinsman G, Kramer ER.
europepmc +4 more sources
NEDD4: The founding member of a family of ubiquitin-protein ligases. [PDF]
Gene, 2015 Ubiquitination plays a crucial role in regulating proteins post-translationally. The focus of this review is on NEDD4, the founding member of the NEDD4 family of ubiquitin ligases that is evolutionarily conserved in eukaryotes. Many potential substrates of NEDD4 have been identified and NEDD4 has been shown to play a critical role in the regulation of ...
Boase NA, Kumar S.
europepmc +8 more sources
E3 ubiquitin ligases: styles, structures and functions
Molecular Biomedicine, 2021 E3 ubiquitin ligases are a large family of enzymes that join in a three-enzyme ubiquitination cascade together with ubiquitin activating enzyme E1 and ubiquitin conjugating enzyme E2.
Yang Wang
exaly +3 more sources
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.
Boomsma W +4 more
europepmc +2 more sources
Antibody targeting of E3 ubiquitin ligases for receptor degradation
Nature, 2022 Most current therapies that target plasma membrane receptors function by antagonizing ligand binding or enzymatic activities. However, typical mammalian proteins comprise multiple domains that execute discrete but coordinated activities. Thus, inhibition
Yvonne T Kschonsak +2 more
exaly +2 more sources
Mammalian HECT ubiquitin-protein ligases: biological and pathophysiological aspects.
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2014 Members of the HECT family of E3 ubiquitin-protein ligases are characterized by a C-terminal HECT domain that catalyzes the covalent attachment of ubiquitin to substrate proteins and by N-terminal extensions of variable length and domain architecture that determine the substrate spectrum of a respective HECT E3.
M. Scheffner, Sharad Kumar
semanticscholar +7 more sources
Ubiquitin-protein ligases [PDF]
Journal of Cell Science, 2004 Post-translational covalent tagging of proteins with the 76-residue protein ubiquitin (Ub) serves many functions. Polyubiquitylated proteins are directed to the large multi-component, multi-catalytic protease the 26S proteasome.
P. Robinson, H. Ardley
semanticscholar +4 more sources
Physical and Functional Interaction of the HECT Ubiquitin-protein Ligases E6AP and HERC2* [PDF]
Journal of Biological Chemistry, 2011 Deregulation of the ubiquitin-protein ligase E6AP contributes to the development of the Angelman syndrome and to cervical carcinogenesis suggesting that the activity of E6AP needs to be under tight control.
Simone Kühnle +6 more
semanticscholar +5 more sources
E3Miner: a text mining tool for ubiquitin-protein ligases [PDF]
Nucleic Acids Research, 2008 Ubiquitination is a regulatory process critically involved in the degradation of >80% of cellular proteins, where such proteins are specifically recognized by a key enzyme, or a ubiquitin-protein ligase (E3).
Hodong Lee, G. Yi, Jong-Chan Park
semanticscholar +5 more sources
The Role of Ubiquitin-Protein Ligases in Neurodegenerative Disease [PDF]
Neurodegenerative Diseases, 2004 Alzheimer’s disease and Parkinson’s disease are the most common neurodegenerative conditions associated with the ageing process. The pathology of these and other neurodegenerative disorders, including polyglutamine diseases, is characterised by the presence of inclusion bodies in brain tissue of affected patients.
H. Ardley, P. Robinson
semanticscholar +4 more sources