Reversible ADP-ribosylation of RNA

Reversible ADP-ribosylation of RNA

<p>ADP-ribosylation is a reversible chemical modification catalysed by ADP-ribosyltransferases such as PARPs that utilize nicotinamide adenine dinucleotide (NAD<sup>+</sup>) as a cofactor to transfer monomer or polymers of ADP-ribose nucleotide onto macromolecular targets such as p...

Πλήρης περιγραφή

Λεπτομέρειες βιβλιογραφικής εγγραφής
Κύριοι συγγραφείς:	Munnur, D, Bartlett, E, Mikolcevic, P, Kirby, I, Rack, J, Mikoc, A, Cohen, M, Ahel, I
Μορφή:	Journal article
Έκδοση:	Oxford University Press 2019

Παρόμοια τεκμήρια

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Specificity of reversible ADP-ribosylation and regulation of cellular processes
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Discovery of reversing enzymes for RNA ADP-ribosylation reveals a possible defence module against toxic attack
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MacroD1 is a promiscuous ADP-ribosyl hydrolase localized to mitochondria
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Specificity of DNA ADP-Ribosylation Reversal by NADARs
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ADP-ribosylation: new facets of an ancient modification
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MacroD1 Is a Promiscuous ADP-Ribosyl Hydrolase Localized to Mitochondria
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Streptomyces coelicolor macrodomain hydrolase SCO6735 cleaves thymidine-linked ADP-ribosylation of DNA
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Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling
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Serine ADP-ribosylation reversal by the hydrolase ARH3
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Streptomyces coelicolor macrodomain hydrolase SCO6735 cleaves thymidine-linked ADP-ribosylation of DNA
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Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal
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(ADP-ribosyl)hydrolases: Structural basis for differential substrate recognition and inhibition
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DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on protein substrates
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Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal
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Studying catabolism of protein ADP-Ribosylation
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Monitoring poly(ADP-ribosyl)glycohydrolase activity with a continuous fluorescent substrate
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Serine ADP-Ribosylation Depends on HPF1
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DarTG is a novel toxin-antitoxin system that catalyses the reversible ADP-ribosylation of DNA
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Identification of a class of protein ADP-ribosylating sirtuins in microbial pathogens
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Serine is the major residue for ADP-ribosylation upon DNA damage
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Synthetic α- and β-Ser-ADP-ribosylated peptides reveal α-Ser-ADPr as the native epimer
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HPF1/C4orf27 is a PARP-1-interacting protein that regulates PARP-1 ADP-ribosylation activity
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Suppression of ADP-ribosylation reversal triggers cell vulnerability to alkylating agents
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Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a conserved arginine-specific macrodomain
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DNA ADP-ribosylation stalls replication and is reversed by RecF-mediated homologous recombination and nucleotide excision repair
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Biallelic ADPRHL2 mutations in complex neuropathy affect ADP ribosylation and DNA damage response
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ENPP1 processes protein ADP-ribosylation in vitro.
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NR4A nuclear receptors target Poly-ADP-Ribosylated DNA-PKcs protein to promote DNA repair
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The role of ADP-ribosylation in regulating DNA interstrand crosslink repair
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Deregulated DNA ADP-ribosylation impairs telomere replication
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