Results 51 to 60 of about 98,022 (279)

The Histone Methyltransferase SMYD2 Methylates PARP1 and Promotes Poly(ADP-ribosyl)ation Activity in Cancer Cells

open access: yesNeoplasia: An International Journal for Oncology Research, 2014
Poly(ADP-ribose) polymerase-1 (PARP1) catalyzes the poly(ADP-ribosyl)ation of protein acceptors using NAD+ as the substrate is now considered as an important target for development of anticancer therapy. PARP1 is known to be post-translationally modified
Lianhua Piao   +6 more
doaj   +1 more source

Poly ADP-ribose polymerase-1 and health

open access: yesExperimental Biology and Medicine, 2010
Niacin (vitamin B3) is required to form nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP), which are involved in scores of anabolic and catabolic redox reactions throughout metabolism. It is now understood that NAD+ is also a substrate for several families of ADP-ribosylation reactions, which control ...
openaire   +2 more sources

PARP-1 regulates DNA repair factor availability. [PDF]

open access: yes, 2018
PARP-1 holds major functions on chromatin, DNA damage repair and transcriptional regulation, both of which are relevant in the context of cancer. Here, unbiased transcriptional profiling revealed the downstream transcriptional profile of PARP-1 enzymatic
Birbe, Ruth   +31 more
core   +2 more sources

A ribose-functionalized NAD+ with unexpected high activity and selectivity for protein poly-ADP-ribosylation. [PDF]

open access: yes, 2019
Nicotinamide adenine dinucleotide (NAD+)-dependent ADP-ribosylation plays important roles in physiology and pathophysiology. It has been challenging to study this key type of enzymatic post-translational modification in particular for protein poly-ADP ...
Chen, Jingwen   +9 more
core   +1 more source

Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation

open access: yesFEBS Letters, EarlyView.
Sorbitol‐induced hyperosmotic stress rapidly induces reversible mono(ADP‐ribosyl)ation (MARylation) on PARP1 without the signs of genotoxic signaling. We show that PARP1 autoMARylation is HPF1 dependent and forms hydroxylamine‐resistant O‐glycosidic linkages.
Anna Georgina Kopasz   +11 more
wiley   +1 more source

Inhibiting poly(ADP-ribosylation) improves axon regeneration

open access: yeseLife, 2016
The ability of a neuron to regenerate its axon after injury depends in part on its intrinsic regenerative potential. Here, we identify novel intrinsic regulators of axon regeneration: poly(ADP-ribose) glycohodrolases (PARGs) and poly(ADP-ribose ...
Alexandra B Byrne   +5 more
doaj   +1 more source

Poly(ADP-ribose)glycohydrolase is an upstream regulator of Ca2+ fluxes in oxidative cell death [PDF]

open access: yes, 2018
Oxidative DNA damage to cells activates poly(ADP-ribose)polymerase-1 (PARP-1) and the poly(ADP-ribose) formed is rapidly degraded to ADP-ribose by poly(ADP-ribose)glycohydrolase (PARG).
Althaus, Felix   +4 more
core  

Inflammation-induced DNA damage and damage-induced inflammation: a vicious cycle [PDF]

open access: yes, 2014
Inflammation is the ultimate response to the constant challenges of the immune system by microbes, irritants or injury. The inflammatory cascade initiates with the recognition of microorganism-derived pathogen associated molecular patterns (PAMPs) and ...
Abe   +100 more
core   +1 more source

PARP inhibition and pharmacological ascorbate demonstrate synergy in castration‐resistant prostate cancer

open access: yesMolecular Oncology, EarlyView.
Pharmacologic ascorbate (vitamin C) increases ROS, disrupts cellular metabolism, and induces DNA damage in CRPC cells. These effects sensitize tumors to PARP inhibition, producing synergistic growth suppression with olaparib in vitro and significantly delayed tumor progression in vivo. Pyruvate rescue confirms ROS‐dependent activity.
Nicolas Gordon   +13 more
wiley   +1 more source

The Role of PARPs in Inflammation—And Metabolic—Related Diseases: Molecular Mechanisms and Beyond

open access: yesCells, 2019
Poly(ADP-ribosyl)ation (PARylation) is an essential post-translational modification catalyzed by poly(ADP-ribose) polymerase (PARP) enzymes. Poly(ADP-ribose) polymerase 1 (PARP1) is a well-characterized member of the PARP family.
Yueshuang Ke   +6 more
doaj   +1 more source

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