(ADP-ribosyl)hydrolases: Structural basis for differential substrate recognition and inhibition

(ADP-ribosyl)hydrolases: Structural basis for differential substrate recognition and inhibition

Protein ADP-ribosylation is a highly dynamic post-translational modification. The rapid turnover is achieved, among others, by ADP-(ribosyl)hydrolases (ARHs), an ancient family of enzymes that reverses this modification. Recently ARHs came into focus due to their role as regulators of cellular stres...

Bibliográfalaš dieđut
Váldodahkkit:	Rack, J, Ariza, A, Drown, B, Henfrey, C, Bartlett, E, Shirai, T, Hergenrother, P, Ahel, I
Materiálatiipa:	Journal article
Giella:	English
Almmustuhtton:	Elsevier 2018

Geahča maid

Monitoring poly(ADP-ribosyl)glycohydrolase activity with a continuous fluorescent substrate
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Almmustuhtton: (2018)

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

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

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

Reversible ADP-ribosylation of RNA
Dahkki: Munnur, D, et al.
Almmustuhtton: (2019)

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

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

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

Structural and bioinformatic analysis of ADP-ribosylation, transcription, and splicing
Dahkki: Henfrey, CA
Almmustuhtton: (2023)

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

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

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

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

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)

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

Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal
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Almmustuhtton: (2021)

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Dahkki: Munnur, D, et al.
Almmustuhtton: (2017)

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

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

Serine ADP-Ribosylation Depends on HPF1
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Almmustuhtton: (2017)

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

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

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

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

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

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

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Dahkki: Crawford, K, et al.
Almmustuhtton: (2017)

General ADP-Ribosylation Mechanism Based on the Structure of ADP-Ribosyltransferase–Substrate Complexes
Dahkki: Hideaki Tsuge, et al.
Almmustuhtton: (2024-07-01)

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)

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

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

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

Serine is the major residue for ADP-ribosylation upon DNA damage
Dahkki: Luca Palazzo, et al.
Almmustuhtton: (2018-02-01)

HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation
Dahkki: Suskiewicz, MJ, et al.
Almmustuhtton: (2020)

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

Arginine-specific mono ADP-ribosylation in vitro of antimicrobial peptides by ADP-ribosylating toxins.
Dahkki: Marta Castagnini, et al.
Almmustuhtton: (2012-01-01)

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

Inhibiting poly(ADP-ribosylation) improves axon regeneration
Dahkki: Alexandra B Byrne, et al.
Almmustuhtton: (2016-10-01)

Poly(ADP-ribosyl)ation /
Dahkki: Burkle, Alexander
Almmustuhtton: (2006)