Results 31 to 40 of about 86,842 (296)

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

A Bacterial Platform for Studying Ubiquitination Cascades Anchored by SCF-Type E3 Ubiquitin Ligases

Biomolecules
Ubiquitination 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, Jun-Li Wang, Yu-Yang Li, Luo-Yu Liang, Yi-Ting Tan, Ze-Hui Wang, Bao-Lin Li, Guang-Qin Guo, Li Wang, Lei Wu   +9 more
doaj   +1 more source

Semantic clustering analysis of E3-ubiquitin ligases in gastrointestinal tract defines genes ontology clusters with tissue expression patterns

BMC Gastroenterology, 2022
Background Ubiquitin ligases (Ub-ligases) are essential intracellular enzymes responsible for the regulation of proteome homeostasis, signaling pathway crosstalk, cell differentiation and stress responses.
Veronika Iatsiuk, Frantisek Malinka, Marketa Pickova, Jolana Tureckova, Jiri Klema, Frantisek Spoutil, Vendula Novosadova, Jan Prochazka, Radislav Sedlacek   +8 more
doaj   +1 more source

Exploration of Aberrant E3 Ligases Implicated in Alzheimer’s Disease and Development of Chemical Tools to Modulate Their Function

Frontiers in Cellular Neuroscience, 2021
The Ubiquitin Proteasome System (UPS) is responsible for the degradation of misfolded or aggregated proteins via a multistep ATP-dependent proteolytic mechanism. This process involves a cascade of ubiquitin (Ub) transfer steps from E1 to E2 to E3 ligase.
Frances M. Potjewyd, Alison D. Axtman
doaj   +1 more source

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

FEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes, Guilherme M. Azevedo, Amanda P. Barcellos, Diana Bahia   +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, Almaz Zagidullin, Aygul Valiullina, Regina Sayarova, Albert Rizvanov   +4 more
doaj   +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, Alexander Zhelkovsky, Katharina Bilotti, Laura E Crowell, Thomas C Evans, Larry A McReynolds, Gregory J S Lohman   +6 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, Aiqin Sun, Xianyan Tian, Yifei Chen, Wannian Yang, Qiong Lin   +5 more
doaj   +1 more source

Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10

FEBS Letters, EarlyView.
Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang, Satoshi Hashimoto, Sota Ito, Chisato Kikuguchi, Miho Hoshi, Kiyoshi Yamaguchi, Yoichi Furukawa, Toru Suzuki, Toshifumi Inada   +8 more
wiley   +1 more source

E3 ubiquitin ligases: structural diversity, dysregulation in disease, and their emerging role in targeted therapeutic strategies

Frontiers in Molecular Biosciences
The Ubiquitin-Proteasome System (UPS) is a key mechanism of cellular homeostasis. A central part of this mechanism is E3 ubiquitin ligases, which selectively direct proteins to be ubiquitinated for degradation via the UPS.
Srineevas Sriram, Prahalad Krishnakumar, C. Sudandiradoss   +2 more
doaj   +1 more source