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...

Bibliográfalaš dieđut
Váldodahkkit:	Munnur, D, Bartlett, E, Mikolcevic, P, Kirby, I, Rack, J, Mikoc, A, Cohen, M, Ahel, I
Materiálatiipa:	Journal article
Almmustuhtton:	Oxford University Press 2019

Geahča maid

Reversible mono-ADP-ribosylation of DNA breaks.
Dahkki: Munnur, D, et al.
Almmustuhtton: (2017)

Specificity of reversible ADP-ribosylation and regulation of cellular processes
Dahkki: Crawford, K, et al.
Almmustuhtton: (2017)

Discovery of reversing enzymes for RNA ADP-ribosylation reveals a possible defence module against toxic attack
Dahkki: Lu, Y, et al.
Almmustuhtton: (2025)

MacroD1 is a promiscuous ADP-ribosyl hydrolase localized to mitochondria
Dahkki: Agnew, T, et al.
Almmustuhtton: (2018)

Specificity of DNA ADP-Ribosylation Reversal by NADARs
Dahkki: Bara Cihlova, et al.
Almmustuhtton: (2024-04-01)

ADP-ribosylation: new facets of an ancient modification
Dahkki: Palazzo, L, et al.
Almmustuhtton: (2017)

MacroD1 Is a Promiscuous ADP-Ribosyl Hydrolase Localized to Mitochondria
Dahkki: Thomas Agnew, et al.
Almmustuhtton: (2018-01-01)

Serine ADP-ribosylation reversal by the hydrolase ARH3
Dahkki: Fontana, P, et al.
Almmustuhtton: (2017)

Streptomyces coelicolor macrodomain hydrolase SCO6735 cleaves thymidine-linked ADP-ribosylation of DNA
Dahkki: Hloušek-Kasun, A, et al.
Almmustuhtton: (2022)

Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling
Dahkki: Pietro Fontana, et al.
Almmustuhtton: (2023-06-01)

(ADP-ribosyl)hydrolases: structure, function, and biology
Dahkki: Rack, JGM, et al.
Almmustuhtton: (2020)

Serine ADP-ribosylation reversal by the hydrolase ARH3
Dahkki: Pietro Fontana, et al.
Almmustuhtton: (2017-06-01)

Streptomyces coelicolor macrodomain hydrolase SCO6735 cleaves thymidine-linked ADP-ribosylation of DNA
Dahkki: Andrea Hloušek-Kasun, et al.
Almmustuhtton: (2022-01-01)

Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal
Dahkki: Rack, JGM, et al.
Almmustuhtton: (2021)

(ADP-ribosyl)hydrolases: Structural basis for differential substrate recognition and inhibition
Dahkki: Rack, J, et al.
Almmustuhtton: (2018)

Interplay of histone marks with serine ADP-ribosylation
Dahkki: Bartlett, E, et al.
Almmustuhtton: (2018)

DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on protein substrates
Dahkki: Zhu, K, et al.
Almmustuhtton: (2022)

Viral macro domains reverse protein ADP-ribosylation.
Dahkki: Li, C, et al.
Almmustuhtton: (2016)

Reversing ADP-ribosylation
Dahkki: Giuliana Katharina Moeller, et al.
Almmustuhtton: (2017-08-01)

Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal
Dahkki: Johannes Gregor Matthias Rack, et al.
Almmustuhtton: (2021-07-01)

Studying catabolism of protein ADP-Ribosylation
Dahkki: Palazzo, L, et al.
Almmustuhtton: (2017)

Monitoring poly(ADP-ribosyl)glycohydrolase activity with a continuous fluorescent substrate
Dahkki: Drown, B, et al.
Almmustuhtton: (2018)

Serine ADP-Ribosylation Depends on HPF1
Dahkki: Bonfiglio, J, et al.
Almmustuhtton: (2017)

The Making and Breaking of Serine-ADP-Ribosylation in the DNA Damage Response
Dahkki: Kira Schützenhofer, et al.
Almmustuhtton: (2021-11-01)

Molecular tools for the study of ADP-ribosylation: a unified and versatile method to synthesise native mono-ADP-ribosylated peptides
Dahkki: Voorneveld, J, et al.
Almmustuhtton: (2021)

DarTG is a novel toxin-antitoxin system that catalyses the reversible ADP-ribosylation of DNA
Dahkki: Ariza, A, et al.
Almmustuhtton: (2017)

Reanalysis of phosphoproteomics data uncovers ADP-ribosylation sites.
Dahkki: Matic, I, et al.
Almmustuhtton: (2012)

Beyond protein modification: the rise of non-canonical ADP-ribosylation
Dahkki: Schuller, M, et al.
Almmustuhtton: (2022)

Identification of a class of protein ADP-ribosylating sirtuins in microbial pathogens
Dahkki: Rack, J, et al.
Almmustuhtton: (2015)

Serine is the major residue for ADP-ribosylation upon DNA damage
Dahkki: Palazzo, L, et al.
Almmustuhtton: (2018)

Synthetic α- and β-Ser-ADP-ribosylated peptides reveal α-Ser-ADPr as the native epimer
Dahkki: Voorneveld, J, et al.
Almmustuhtton: (2018)

HPF1/C4orf27 is a PARP-1-interacting protein that regulates PARP-1 ADP-ribosylation activity
Dahkki: Gibbs-Seymour, I, et al.
Almmustuhtton: (2016)

Suppression of ADP-ribosylation reversal triggers cell vulnerability to alkylating agents
Dahkki: Rocco Caggiano, et al.
Almmustuhtton: (2025-01-01)

Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a conserved arginine-specific macrodomain
Dahkki: Zhengrui Zhang, et al.
Almmustuhtton: (2024-03-01)

DNA ADP-ribosylation stalls replication and is reversed by RecF-mediated homologous recombination and nucleotide excision repair
Dahkki: Lawarée, E, et al.
Almmustuhtton: (2020)

Biallelic ADPRHL2 mutations in complex neuropathy affect ADP ribosylation and DNA damage response
Dahkki: Beijer, D, et al.
Almmustuhtton: (2021)

ENPP1 processes protein ADP-ribosylation in vitro.
Dahkki: Palazzo, L, et al.
Almmustuhtton: (2016)

NR4A nuclear receptors target Poly-ADP-Ribosylated DNA-PKcs protein to promote DNA repair
Dahkki: Munnur, D, et al.
Almmustuhtton: (2019)

The role of ADP-ribosylation in regulating DNA interstrand crosslink repair
Dahkki: Gunn, A, et al.
Almmustuhtton: (2016)

Deregulated DNA ADP-ribosylation impairs telomere replication
Dahkki: Wondisford, AR, et al.
Almmustuhtton: (2024)