Results 211 to 220 of about 129,362 (255)
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Protein homeostasis and aging: Role of ubiquitin protein ligases
Neurochemistry International, 2012Protein homeostasis is fundamental in normal cellular function and cell survival. The ubiquitin-proteasome system (UPS) plays a central role in maintaining the protein homeostasis network through selective elimination of misfolded and damaged proteins.
N. Jana
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Ubiquitin-protein ligases in muscle wasting.
The International Journal of Biochemistry & Cell Biology, 2005Muscle wasting occurs when rates of protein degradation outstrip rates of protein synthesis. Accelerated rates of protein degradation develop in atrophying muscle largely through activation of the ubiquitin-proteasome pathway. The complexity of the ubiquitination process, however, has hampered our understanding of how this pathway is activated in ...
Pei-rang Cao, Hannah J Kim, S. Lecker
semanticscholar +4 more sources
Ubiquitin-protein ligases--novel therapeutic targets?
Current Protein and Peptide Science, 2004Intracellular protein degradation is a tightly regulated process that in many cases is controlled by protein ubiquitylation. The ubiquitin pathway is a major route by which cells not only remove normal proteins at the appropriate time but also abnormally
P. Robinson, H. Ardley
semanticscholar +3 more sources
Ubiquitin Ligases: Structure, Function, and Regulation
Annual Review of Biochemistry, 2017Ubiquitin E3 ligases control every aspect of eukaryotic biology by promoting protein ubiquitination and degradation. At the end of a three-enzyme cascade, ubiquitin ligases mediate the transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to ...
Ning Zheng, Nitzan Shabek
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Ubiquitin‐protein ligases in muscle wasting: multiple parallel pathways?
Current Opinion in Clinical Nutrition & Metabolic Care, 2003Studies in a wide variety of animal models of muscle wasting have led to the concept that increased protein breakdown via the ubiquitin-proteasome pathway is responsible for the loss of muscle mass seen as muscle atrophy. The complexity of the ubiquitination apparatus has hampered our understanding of how this pathway is activated in atrophying muscles
S. Lecker
semanticscholar +4 more sources
Adenovirus protein involved in virus internalization recruits ubiquitin-protein ligases.
Biochemistry, 2002Adenovirus penton base protein is involved in virus internalization. Searching for the cellular partners of this protein, we used dodecahedra, adenovirus subviral particles composed of 12 bases, for screening a human lung expression library.
R. Galinier +4 more
semanticscholar +7 more sources
E3 Ubiquitin Ligases Neurobiological Mechanisms: Development to Degeneration
Frontiers in Molecular Neuroscience, 2017 Cells regularly synthesize new proteins to replace old or damaged proteins. Deposition of various aberrant proteins in specific brain regions leads to neurodegeneration and aging.
Arun Upadhyay +2 more
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Cullin 3 Ubiquitin Ligases in Cancer Biology: Functions and Therapeutic Implications
Frontiers in Oncology, 2016 Cullin-RING ubiquitin ligases are the largest E3 ligase family in eukaryotes and are multi-protein complexes. In these complexes, the Cullin protein serves as a scaffold to connect two functional modules of the ligases, the catalytic subunit and ...
Hsin-yi Chen, Ruey-hwa Chen
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Small Molecule Modulators of RING-Type E3 Ligases: MDM and Cullin Families as Targets
Frontiers in Pharmacology, 2018 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 +2 more
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E3 ubiquitin ligases in cancer and implications for therapies
Cancer and Metastasis Reviews, 2017Bin Wang, Jia Liu, Jianping Guo
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