Results 51 to 60 of about 81,380 (309)

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

open access: yesBiomolecules
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   +9 more
doaj   +1 more source

Interplay between bacterial deubiquitinase and ubiquitin E3 ligase regulates ubiquitin dynamics on Legionella phagosomes

open access: yeseLife, 2020
Legionella pneumophila extensively modulates the host ubiquitin network to create the Legionella-containing vacuole (LCV) for its replication. Many of its virulence factors function as ubiquitin ligases or deubiquitinases (DUBs).
Shuxin Liu   +5 more
doaj   +1 more source

The testis-specific E3 ubiquitin ligase RNF133 is required for fecundity in mice

open access: yesBMC Biology, 2022
Background Ubiquitination is a post-translational modification required for a number of physiological functions regulating protein homeostasis, such as protein degradation.
Kaori Nozawa   +14 more
doaj   +1 more source

The San1 Ubiquitin Ligase Avidly Recognizes Misfolded Proteins through Multiple Substrate Binding Sites

open access: yesBiomolecules, 2021
Cellular homeostasis depends on robust protein quality control (PQC) pathways that discern misfolded proteins from functional ones in the cell. One major branch of PQC involves the controlled degradation of misfolded proteins by the ubiquitin-proteasome ...
Rebeca Ibarra   +4 more
doaj   +1 more source

The proteasome lid triggers COP9 signalosome activity during the transition of Saccharomyces cerevisiae cells into quiescence. [PDF]

open access: yes, 2019
The class of Cullin–RING E3 ligases (CRLs) selectively ubiquitinate a large portion of proteins targeted for proteolysis by the 26S proteasome. Before degradation, ubiquitin molecules are removed from their conjugated proteins by deubiquitinating enzymes,
Bramasole, Lylan   +8 more
core  

Tumour–host interactions in Drosophila: mechanisms in the tumour micro‐ and macroenvironment

open access: yesMolecular Oncology, EarlyView.
This review examines how tumour–host crosstalk takes place at multiple levels of biological organisation, from local cell competition and immune crosstalk to organism‐wide metabolic and physiological collapse. Here, we integrate findings from Drosophila melanogaster studies that reveal conserved mechanisms through which tumours hijack host systems to ...
José Teles‐Reis, Tor Erik Rusten
wiley   +1 more source

The roles of E3 ubiquitin ligases in cancer progression and targeted therapy

open access: yesClinical and Translational Medicine, 2023
Ubiquitination is one of the most important post‐translational modifications which plays a significant role in conserving the homeostasis of cellular proteins.
Chibuzo Sampson   +6 more
doaj   +1 more source

Genetic attenuation of ALDH1A1 increases metastatic potential and aggressiveness in colorectal cancer

open access: yesMolecular Oncology, EarlyView.
Aldehyde dehydrogenase 1A1 (ALDH1A1) is a cancer stem cell marker in several malignancies. We established a novel epithelial cell line from rectal adenocarcinoma with unique overexpression of this enzyme. Genetic attenuation of ALDH1A1 led to increased invasive capacity and metastatic potential, the inhibition of proliferation activity, and ultimately ...
Martina Poturnajova   +25 more
wiley   +1 more source

Targeting E3 ubiquitin ligases: a new frontier in idiopathic pulmonary fibrosis treatment

open access: yesFrontiers in Immunology
Ubiquitination is a modification prevalent in eukaryotic cells. Disruptions in ubiquitination processes can have detrimental effects, potentially leading to diseases that endanger life.
Kun Zhang, Hui Yuan, Lin Shi
doaj   +1 more source

The Role of the Cullin-5 E3 Ubiquitin Ligase in the Regulation of Insulin Receptor Substrate-1

open access: yesBiochemistry Research International, 2012
Background. SOCS proteins are known to negatively regulate insulin signaling by inhibiting insulin receptor substrate-1 (IRS1). IRS1 has been reported to be a substrate for ubiquitin-dependent proteasomal degradation.
Christine Zhiwen Hu   +2 more
doaj   +1 more source

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