Results 61 to 70 of about 153,107 (330)
The enigma of the RING-UIM E3 ligases: its transformative impact on cancer research
Journal of Translational MedicineRING-UIM E3 ligases, a subfamily within the RING-type E3 ligases, comprise four members: RNF114, RNF125, RNF138, and RNF166. These ligases are crucial in various biological processes, including immunity, inflammation, epigenetics, and homologous ...
Ye Wang, Yue Zhao, Qi Xin, Jihong Zhang
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SUMO-targeted ubiquitin ligases [PDF]
, 2014 Covalent posttranslational modification with SUMO (small ubiquitin-related modifier) modulates functions of a wide range of proteins in eukaryotic cells. Sumoylation affects the activity, interaction properties, subcellular localization and the stability
Dohmen, R. Jürgen +1 more
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Molecular Medicine, 2023 The homologous to the E6-AP carboxyl terminus (HECT)-type E3 ubiquitin ligases are the selective executers in the protein ubiquitination, playing a vital role in modulation of the protein function and stability. Evidence shows the regulatory role of HECT-
Rui Zhang, Shaoqing Shi
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An isoform of 14‐3‐3 protein regulates transbilayer lipid movement at the plasma membrane
FEBS Letters, EarlyView.Loss of 14‐3‐3ζ in CHO cells confers resistance to exogenous phosphatidylserine (PS) and impairs endocytosis‐independent inward flip‐flop of fluorescent PS at the plasma membrane. RNAi‐mediated knockdown reproduces this defect, while no additive effect is seen in ATP11C‐deficient cells.
Akiko Yamaji‐Hasegawa +3 more
wiley +1 more source
A Bacterial Platform for Studying Ubiquitination Cascades Anchored by SCF-Type E3 Ubiquitin Ligases
BiomoleculesUbiquitination is one of the most important post-translational modifications in eukaryotes. The ubiquitination cascade includes ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3). The E3 ligases, responsible
Zuo-Xian Pu +9 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 eChen +2 more
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Chain reactions: molecular mechanisms of RBR ubiquitin ligases
Biochemical Society Transactions, 2020 Ubiquitination is a fundamental post-translational modification that regulates almost all aspects of cellular signalling and is ultimately catalysed by the action of E3 ubiquitin ligases.
T. Cotton, B. C. Lechtenberg
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The molecular basis of CRL4 ubiquitin ligase architecture, targeting and regulation [PDF]
, 2013 Members of the CUL4-RBX1-DDB1 (CRL4) E3 ubiquitin ligase family regulate multiple cellular processes including development, transcription, and DNA repair.
Fischer, Eric Sebastian
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FEBS Letters, EarlyView.Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley +1 more source
How to Inactivate Human Ubiquitin E3 Ligases by Mutation
Frontiers in Cell and Developmental Biology, 2020 E3 ubiquitin ligases are the ultimate enzymes involved in the transfer of ubiquitin to substrate proteins, a process that determines the fate of the modified protein.
Cristina Garcia-Barcena +3 more
semanticscholar +1 more source