Results 51 to 60 of about 143,768 (336)
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
doaj +1 more source
Emerging roles of the HECT E3 ubiquitin ligases in gastric cancer
Pathology and Oncology Research, 2023 Gastric cancer (GC) is one of the most pernicious gastrointestinal tumors with extraordinarily high incidence and mortality. Ubiquitination modification of cellular signaling proteins has been shown to play important roles in GC tumorigenesis ...
Aiqin Sun +5 more
doaj +1 more source
HERC Ubiquitin Ligases in Cancer
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
Joan Sala-Gaston +7 more
semanticscholar +1 more source
Reciprocal control of viral infection and phosphoinositide dynamics
FEBS Letters, EarlyView.Phosphoinositides, although scarce, regulate key cellular processes, including membrane dynamics and signaling. Viruses exploit these lipids to support their entry, replication, assembly, and egress. The central role of phosphoinositides in infection highlights phosphoinositide metabolism as a promising antiviral target.
Marie Déborah Bancilhon, Bruno Mesmin
wiley +1 more source
Comparative analysis of the end-joining activity of several DNA ligases. [PDF]
PLoS ONE, 2017 DNA ligases catalyze the repair of phosphate backbone breaks in DNA, acting with highest activity on breaks in one strand of duplex DNA. Some DNA ligases have also been observed to ligate two DNA fragments with short complementary overhangs or blunt ...
Robert J Bauer +6 more
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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
Proceedings of the National Academy of Sciences of the United States of America, 2019 Significance Mechanisms to balance the acquisition of sufficient Fe while preventing a toxic overload differ in bacteria, fungi, animals, and plants. Identification of specific E3 ligases acting directly on a key transcription factor for Fe uptake in ...
Jorge Rodríguez-Celma +9 more
semanticscholar +1 more source
CCT4 promotes tunneling nanotube formation
FEBS Letters, EarlyView.Tunneling nanotubes (TNTs) are membranous tunnel‐like structures that transport molecules and organelles between cells. They vary in thickness, and thick nanotubes often contain microtubules in addition to actin fibers. We found that cells expressing monomeric CCT4 generate many thick TNTs with tubulin.
Miyu Enomoto +3 more
wiley +1 more source
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 +4 more
doaj +1 more source
Multiple cullin-associated E3 ligases regulate cyclin D1 protein stability
eLife, 2023 Cyclin D1 is a key regulator of cell cycle progression, which forms a complex with CDK4/6 to regulate G1/S transition during cell cycle progression.
Ke Lu +5 more
doaj +1 more source