Results 121 to 130 of about 214,575 (242)

Membrane-association promotes Axin degradation through Tankyrase-dependent ADP-ribosylation

open access: yes, 2016
(A) Lysates from third instar larvae expressing indicated transgenes with the C765-Gal4 driver were analyzed by immunoblotting. Myr-Axin-V5 is present at much lower levels than Axin-V5 or MyrG-A-Axin-V5. Kinesin was used as a loading control.
Yashi Ahmed (2158360)   +3 more
core   +1 more source

PARP9 and PARP14 cross-regulate macrophage activation via STAT1 ADP-ribosylation

open access: yesNature Communications, 2016
Despite the global impact of macrophage activation in vascular disease, the underlying mechanisms remain obscure. Here we show, with global proteomic analysis of macrophage cell lines treated with either IFNγ or IL-4, that PARP9 and PARP14 regulate ...
H. Iwata   +18 more
semanticscholar   +1 more source

Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases

open access: yesScience Advances, 2020
The C-terminal RING and DTC domains of mammalian Deltex proteins catalyze ADP-ribosylation at the C terminus of ubiquitin. Cellular cross-talk between ubiquitination and other posttranslational modifications contributes to the regulation of numerous ...
Chatrin Chatrin   +8 more
semanticscholar   +1 more source

Primary cilia–extracellular vesicle crosstalk in Alzheimer's disease: Emerging mechanisms and biomarker potential

open access: yesAlzheimer's &Dementia, Volume 22, Issue 7, July 2026.
Abstract Alzheimer's disease (AD) is a neurodegenerative condition marked by cognitive decline and synaptic issues. Recent studies show primary cilia (PCs), sensory organelles present on the surface of most mammalian cells, act as a critical regulators of brain homeostasis and signaling.
Vishal Singh Guleria   +1 more
wiley   +1 more source

Cell fate regulation by chromatin ADP-ribosylation

open access: yes, 2017
ADP-ribosylation is an evolutionarily conserved complex posttranslational modification that alters protein function and/or interaction. Intracellularly, it is mainly catalyzed by diphtheria toxin-like ADP-ribosyltransferases (ARTDs), which attach one or ...
Michael O. Hottiger   +3 more
core   +1 more source

Hormonal stimulation of eucaryotic cell ADP-ribosylation.

open access: yes, 1981
The effect of thyrotropin (TSH) on the ADP-ribosylation of endogenous thyroid cell acceptor proteins was examined. Cells were "permeabilized" at 4 degrees C in hypotonic medium and then exposed to [(32)P]- or [(3)H-adenine]NAD(+).
B. Rapoport   +3 more
core   +1 more source

RBOHC‐Generated ROS Tune MIZ2/GNOM‐Dependent Root Halotropism in Arabidopsis

open access: yes
Plant, Cell &Environment, EarlyView.
Amir Cohen   +4 more
wiley   +1 more source

Arginine-Specific Mono ADP-Ribosylation In Vitro of Antimicrobial Peptides by ADP-Ribosylating Toxins

open access: yesPLoS ONE, 2012
Among the several toxins used by pathogenic bacteria to target eukaryotic host cells, proteins that exert ADP-ribosylation activity represent a large and studied family of dangerous and potentially lethal toxins. These proteins alter cell physiology catalyzing the transfer of the ADP-ribose unit from NAD to cellular proteins involved in key metabolic ...
Castagnini M   +8 more
openaire   +5 more sources

Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a conserved arginine-specific macrodomain

open access: yesNature Communications
ADP-ribosylation is a reversible post-translational modification involved in various cellular activities. Removal of ADP-ribosylation requires (ADP-ribosyl)hydrolases, with macrodomain enzymes being a major family in this category.
Zhengrui Zhang   +8 more
doaj   +1 more source

The coronavirus macrodomain is required to prevent PARP-mediated inhibition of virus replication and enhancement of IFN expression.

open access: yesPLoS Pathogens, 2019
ADP-ribosylation is a ubiquitous post-translational addition of either monomers or polymers of ADP-ribose to target proteins by ADP-ribosyltransferases, usually by interferon-inducible diphtheria toxin-like enzymes known as PARPs.
Matthew E Grunewald   +9 more
doaj   +1 more source

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