Results 11 to 20 of about 133,567 (215)
Structural Diversity of Ubiquitin E3 Ligase [PDF]
Molecules, 2021 The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes ...
Sachiko Toma-Fukai, Toshiyuki Shimizu
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HERC Ubiquitin Ligases in Cancer [PDF]
Cancers, 2020 HERC proteins are ubiquitin E3 ligases of the HECT family. The HERC subfamily is composed of six members classified by size into large (HERC1 and HERC2) and small (HERC3–HERC6). HERC family ubiquitin ligases regulate important cellular processes, such as neurodevelopment, DNA damage response, cell proliferation, cell migration, and immune responses ...
Joan Sala-Gaston +7 more
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Ubiquitin ligases and beyond [PDF]
BMC Biology, 2012 In a review published in 2004 [1] and that still repays reading today, Cecile Pickart traced the evolution of research on ubiquitination from its origins in the proteasomal degradation of proteins through the revelation that it has a central role in cell cycle regulation and the recognition of regulatory roles for ubiquitin in intracellular membrane ...
Đikić, Ivan, Robertson, Miranda
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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.
Philip A. Robinson, H. C. Ardley
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A Ubiquitin-like Protein Unleashes Ubiquitin Ligases [PDF]
Cell, 2008 Modification of cullin-RING ubiquitin ligases by the ubiquitin-like molecule Nedd8 promotes substrate ubiquitination. A crystal structure of a cullin modified by Nedd8 recently reported in Cell (Duda et al., 2008) and a biochemical study in Molecular Cell (Saha and Deshaies, 2008) reveal the dramatic impact on the ligase machinery by conjugation of ...
Ning Zheng +2 more
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The SCF Ubiquitin Ligase [PDF]
Molecular Cell, 2002 The SCF E3 ubiquitin ligases select specific proteins for ubiquitination (and typically destruction) by coupling variable adaptor (F box) proteins that bind protein substrates to a conserved catalytic engine containing a cullin, Cul1, and the Rbx1/Roc1 RING finger protein.
Adam G. Eldridge, Peter K. Jackson
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Inhibitors of ubiquitin E3 ligase as potential new antimalarial drug leads
BMC Pharmacology and Toxicology, 2017 Background Protein ubiquitylation is an important post-translational regulation, which has been shown to be necessary for life cycle progression and survival of Plasmodium falciparum.
Jagrati Jain +3 more
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Cell, 2016 Ubiquitination is a post-translational modification of proteins involved in a variety of cellular processes. Ubiquitination requires the sequential action of three enzymes: E1 (ubiquitin-activating enzymes), E2 (ubiquitin-conjugating enzymes), and E3 (ubiquitin ligases).
Helen Walden, Francesca E. Morreale
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PLoS Genetics, 2023 The tumor suppressor BRCA1-BARD1 complex regulates many cellular processes; of critical importance to its tumor suppressor function is its role in genome integrity.
Qianyan Li +4 more
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Frontiers in Endocrinology, 2023 E3 ubiquitin ligases are important components of the ubiquitin protease system. This family includes many proteins, which can catalyze the ubiquitination of a variety of protein substrates and promote the degradation of them by the proteasome system ...
Jun Feng +7 more
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