Results 21 to 30 of about 39,153 (185)
Biallelic ADPRHL2 mutations in complex neuropathy affect ADP ribosylation and DNA damage response
Life Science Alliance, 2021 This work studies known and new ADPRHL2 mutations with different disease mechanisms overall indicating that loss of nuclear ARH3 alone is pathogenic via dysregulated nuclear ADP ribosylation.
Danique Beijer +10 more
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Selective monitoring of the protein-free ADP-ribose released by ADP-ribosylation reversal enzymes.
PLoS ONE, 2021 ADP-ribosylation is a key post-translational modification that regulates a wide variety of cellular stress responses. The ADP-ribosylation cycle is maintained by writers and erasers.
Samuel Kasson +2 more
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The interplay of TARG1 and PARG protects against genomic instability
Cell Reports, 2023 Summary: The timely removal of ADP-ribosylation is crucial for efficient DNA repair. However, much remains to be discovered about ADP-ribosylhydrolases. Here, we characterize the physiological role of TARG1, an ADP-ribosylhydrolase that removes aspartate/
Joséphine Groslambert +10 more
doaj +1 more source
Reversible ADP-ribosylation of RNA [PDF]
Nucleic Acids Research, 2019 AbstractADP-ribosylation is a reversible chemical modification catalysed by ADP-ribosyltransferases such as PARPs that utilize nicotinamide adenine dinucleotide (NAD+) as a cofactor to transfer monomer or polymers of ADP-ribose nucleotide onto macromolecular targets such as proteins and DNA.
Munnur, D +7 more
openaire +3 more sources
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
The Making and Breaking of Serine-ADP-Ribosylation in the DNA Damage Response
Frontiers in Cell and Developmental Biology, 2021 ADP-ribosylation is a widespread posttranslational modification that is of particular therapeutic relevance due to its involvement in DNA repair. In response to DNA damage, PARP1 and 2 are the main enzymes that catalyze ADP-ribosylation at damage sites ...
Kira Schützenhofer +2 more
doaj +1 more source
Roles of Asp179 and Glu270 in ADP-Ribosylation of Actin by Clostridium perfringens Iota Toxin. [PDF]
PLoS ONE, 2015 Clostridium perfringens iota toxin is a binary toxin composed of the enzymatically active component Ia and receptor binding component Ib. Ia is an ADP-ribosyltransferase, which modifies Arg177 of actin.
Alexander Belyy +5 more
doaj +1 more source
Mono ADP-ribosylation and Poly ADP-ribosylation of Proteins [PDF]
, 1981 Postsynthetic modification of proteins by transfer of ADP-ribosyl groups from NAD has been shown to occur in numerous systems. Besides ADPR transferase reactions associated with the action of bacterial toxins and viruses, ADP ribosylation reactions were also observed in eukaryotic cells (cf.
H. Hilz +3 more
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Proteasome Regulation by ADP-Ribosylation [PDF]
Cell, 2013 Protein degradation by the ubiquitin-proteasome system is central to cell homeostasis and survival. Defects in this process are associated with diseases such as cancer and neurodegenerative disorders. The 26S proteasome is a large protease complex that degrades ubiquitinated proteins. Here, we show that ADP-ribosylation promotes 26S proteasome activity
Cho-Park, Park F., Steller, Hermann
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Roles of ADP-Ribosylation during Infection Establishment by Trypanosomatidae Parasites
Pathogens, 2023 ADP-ribosylation is a reversible post-translational protein modification, which is evolutionarily conserved in prokaryotic and eukaryotic organisms.
Joshua Dowling, Craig L. Doig
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