Results 261 to 270 of about 231,680 (303)
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The Role of Ubiquitin E3 Ligase in Atherosclerosis
Current Medicinal Chemistry, 2020Atherosclerosis is a chronic inflammatory vascular disease. Atherosclerotic cardiovascular disease is the main cause of death in both developed and developing countries. Many pathophysiological factors, including abnormal cholesterol metabolism, vascular inflammatory response, endothelial dysfunction and vascular smooth muscle cell proliferation and ...
Zhi-Xiang Zhou +8 more
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Inhibitors for E3 Ubiquitin Ligases
Nature Biotechnology, 2010Two studies show that specific cullin-RING E3 ubiquitin ligases can be targeted with small molecules.
Jeffrey W. Harper
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E3 ubiquitin ligases for MHC molecules
Current Opinion in Immunology, 2009Recently, novel E3 ubiquitin ligases that target MHC molecules for lysosomal degradation have been discovered by several groups. All these E3s are membrane-bound and possess a variant type RING domain, termed the RING-CH or RING variant (RINGv) domain. They belong to a new E3 family designated Modulator of Immune Recognition (MIR), based on the name of
Satoshi, Ishido +3 more
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Structure of the human UBR5 E3 ubiquitin ligase
Structure, 2022ABSTRACT The human UBR5 (also known as EDD) is a single polypeptide chain HECT-type E3 ubiquitin ligase essential for embryonic development in mammals. Although widely expressed, UBR5 is markedly amplified and overexpressed in breast, ovarian, prostate, gastric and pancreatic ...
Feng Wang +7 more
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Autoantigen Ro52 is an E3 ubiquitin ligase
Biochemical and Biophysical Research Communications, 2006Anti-Ro/SSA antibodies are classic autoantibodies commonly found in patients with Sjögren's syndrome, a chronic autoimmune disease characterized by dryness of the eyes and mouth. The autoantibodies recognize a RING-finger protein, Ro52, whose function is still unknown.
Keiji, Wada, Tetsu, Kamitani
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Ubiquitination on Nonlysine Residues by a Viral E3 Ubiquitin Ligase
Science, 2005Ubiquitination controls a broad range of cellular functions. The last step of the ubiquitination pathway is regulated by enzyme type 3 (E3) ubiquitin ligases. E3 enzymes are responsible for substrate specificity and catalyze the formation of an isopeptide bond between a lysine residue of the substrate (or the N terminus of the ...
Ken, Cadwell, Laurent, Coscoy
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RNF220, an E3 ubiquitin ligase that targets Sin3B for ubiquitination
Biochemical and Biophysical Research Communications, 2010Modification of proteins by ubiquitination plays important roles in various cellular processes. During this process, the target specificity is determined by ubiquitin ligases. Here we identify RNF220 (RING finger protein 220) as a novel ubiquitin ligase for Sin3B. As a conserved RING protein, RNF220 can bind E2 and mediate auto-ubiquitination of itself.
Qinghua, Kong +5 more
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HECT-Type E3 Ubiquitin Ligases in Cancer
Trends in Biochemical Sciences, 2019Ubiquitination, a post-translational modification that involves a covalent attachment of ubiquitin to a protein substrate, is essential for cellular homeostatic maintenance. At the end of a three-enzyme cascade, E3 ubiquitin ligases (E3s) recruit substrates and promote or directly catalyze ubiquitin transfer to targets.
Francesca Bernassola +2 more
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The HECT family of E3 ubiquitin ligases and PTEN
Seminars in Cancer Biology, 2022Members of the HECT family of E3 ubiquitin ligases have emerged as prominent regulators of PTEN function, subcellular localization and levels. In turn this unfolding regulatory network is allowing for the identification of genes directly involved in both tumorigenesis at large and cancer susceptibility syndromes. While the complexity of this regulatory
Song, Min Sup, Pandolfi, Pier Paolo
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E3 ubiquitin ligases in cancer and implications for therapies
Cancer and Metastasis Reviews, 2017E3 ligases are a class of enzymes that can transfer ubiquitin to substrates for their degradation, which are of importance in cellular homeostasis. Since many oncogenic or tumor-suppressive proteins are reported to be regulated by the ubiquitin-proteasome system (UPS), E3 ligases, which function as substrate interacting modules, have been attracting ...
Dong, Wang +4 more
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