Results 31 to 40 of about 7,274 (190)
Pathogens, 2023 The chemical modification of cellular macromolecules by the transfer of ADP-ribose unit(s), known as ADP-ribosylation, is an ancient homeostatic and stress response control system.
Giuliana Catara +2 more
doaj +1 more source
Mono(ADP-ribosyl)ation Enzymes and NAD+ Metabolism: A Focus on Diseases and Therapeutic Perspectives
Cells, 2021 Mono(ADP-ribose) transferases and mono(ADP-ribosyl)ating sirtuins use NAD+ to perform the mono(ADP-ribosyl)ation, a simple form of post-translational modification of proteins and, in some cases, of nucleic acids.
Palmiro Poltronieri +2 more
doaj +1 more source
The expanding field of non-canonical RNA capping: new enzymes and mechanisms
Royal Society Open Science, 2021 Recent years witnessed the discovery of ubiquitous and diverse 5′-end RNA cap-like modifications in prokaryotes as well as in eukaryotes. These non-canonical caps include metabolic cofactors, such as NAD+/NADH, FAD, cell wall precursors UDP-GlcNAc ...
Jana Wiedermannová +2 more
doaj +1 more source
Nicotinamide Riboside Vitamin B3 Mitigated C26 Adenocarcinoma–Induced Cancer Cachexia
Frontiers in Pharmacology, 2021 Nicotinamide riboside (NR), vitamin B3, is a substrate for nicotinamide adenine dinucleotide (NAD+)–consuming enzymes and is a coenzyme for hydride-transfer enzymes, including adenosine diphosphate (ADP)–ribose transferases, poly (ADP-ribose) polymerases,
Jong Min Park +5 more
doaj +1 more source
Molecular Plant-Microbe Interactions, 2021 Structural biology has the potential to illuminate the evolution of pathogen effectors and their commonalities that cannot be readily detected at the primary sequence level.
Kyungyong Seong, Ksenia V. Krasileva
doaj +1 more source
Structure, function and inhibition of poly(ADP-ribose)polymerase, member 14 (PARP14) [PDF]
, 2018 Poly(ADP-ribose)polymerase, member 14 (PARP14, alternatively named ARTD8, BAL2, and COAST6) is an intracellular mono(ADP-ribosyl) transferase. PARP14 transfers a negatively charged ADP-ribose unit from a donor NAD+ molecule onto a target protein, post ...
Levonis, Stephan M +3 more
core +1 more source
PARP-3 and APLF function together to accelerate nonhomologous end joining [PDF]
, 2010 PARP-3 is a member of the ADP-ribosyl transferase superfamily of unknown function. We show that PARP-3 is stimulated by DNA double-strand breaks (DSBs) in vitro and functions in the same pathway as the poly (ADP-ribose)-binding protein APLF to accelerate
Ahel +59 more
core +1 more source
ING1 and 5-azacytidine act synergistically to block breast cancer cell growth. [PDF]
PLoS ONE, 2012 Inhibitor of Growth (ING) proteins are epigenetic "readers" that recognize trimethylated lysine 4 of histone H3 (H3K4Me3) and target histone acetyl transferase (HAT) and histone deacetylase (HDAC) complexes to chromatin.Here we asked whether ...
Satbir Thakur +7 more
doaj +1 more source
Emerging Concepts on the Role of ADP-Ribosylation
Challenges, 2020 NAD+ has emerged as a crucial element in both bioenergetic and signaling pathways, since it acts as a key regulator of cellular and organism homeostasis.
Palmiro Poltronieri
doaj +1 more source
Poly(ADP-ribose)polymerase activity controls plant growth by promoting leaf cell number [PDF]
, 2014 A changing global environment, rising population and increasing demand for biofuels are challenging agriculture and creating a need for technologies to increase biomass production.
Claeys, Hannes +8 more
core +3 more sources