Results 11 to 20 of about 62,421 (311)
Functional Domains of the Rsp5 Ubiquitin-Protein Ligase [PDF]
Molecular and Cellular Biology, 1999 RSP5, an essential gene of Saccharomyces cerevisiae, encodes a hect domain E3 ubiquitin-protein ligase. Hect E3 proteins have been proposed to consist of two broad functional domains: a conserved catalytic carboxyl-terminal domain of approximately 350 amino acids (the hect domain) and a large, nonconserved amino-terminal domain containing determinants ...
G, Wang, J, Yang, J M, Huibregtse
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The ubiquitin–protein ligase Itch regulates p73 stability [PDF]
The EMBO Journal, 2005 p73, a member of the p53 family of transcription factors, is upregulated in response to DNA damage, inducing cell cycle arrest and apoptosis. Besides indications that this p73 response is post-transcriptional, little is known about the underlying molecular mechanisms of p73 protein degradation.
ROSSI M. +7 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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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 +4 more
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Genome-wide analysis of HECT E3 ubiquitin ligase gene family in Solanum lycopersicum
Scientific Reports, 2021 The E3 ubiquitin ligases have been known to intrigue many researchers to date, due to their heterogenicity and substrate mediation for ubiquitin transfer to the protein.
Bhaskar Sharma +2 more
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Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases. [PDF]
, 2013 Cullin-RING ligases are multisubunit E3 ubiquitin ligases that recruit substrate-specific adaptors to catalyze protein ubiquitylation. Cul3-based Cullin-RING ligases are uniquely associated with BTB adaptors that incorporate homodimerization, Cul3 ...
Bullock, AN +30 more
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Genome-Wide Identification and Expression of Xenopus F-Box Family of Proteins. [PDF]
PLoS ONE, 2015 Protein degradation via the multistep ubiquitin/26S proteasome pathway is a rapid way to alter the protein profile and drive cell processes and developmental changes.
Banu Saritas-Yildirim +3 more
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The Biological Function and Roles in Phytohormone Signaling of the F-Box Protein in Plants
Agronomy, 2021 The ubiquitin–proteasome pathway (UPP) is an important protein degradation pathway that can participate in the regulation of the physiological process of organisms by specifically removing abnormal peptides and degrading cell regulators.
Keheng Xu +5 more
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Ubiquitin-proteasome dependent mitochondrial protein quality control [PDF]
, 2014 Dysfunctional mitochondria cause many neurodegenerative disorders and with aging in general, mechanisms of mitochondrial quality control are essential for cellular function.
Benischke, Anne-Sophie
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Computational and Structural Biotechnology Journal, 2022 Protein ubiquitination plays a vital role in controlling the degradation of intracellular proteins and in regulating cell signaling pathways. Functionally, E3 ubiquitin ligases control the transfer of ubiquitin to the target substrates. As a major family
Xiaohua Lou +7 more
doaj +1 more source