Results 51 to 60 of about 214,575 (242)

Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease

open access: yesMolecules and Cells, 2021
SUMMARY ARH3/ADPRHL2 and PARG are the primary enzymes reversing ADP-ribosylation in vertebrates, yet their functions in vivo remain unclear. ARH3 is the only hydrolase able to remove serine-linked mono(ADP-ribose) (MAR) but is much less efficient than ...
Evgeniia A. Prokhorova   +19 more
semanticscholar   +1 more source

The DarT/DarG Toxin–Antitoxin ADP-Ribosylation System as a Novel Target for a Rational Design of Innovative Antimicrobial Strategies

open access: yesPathogens, 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

PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes

open access: yesGenes & Development, 2017
In this review, Gupte et al. discuss new findings on the diverse roles of PARPs in chromatin regulation, transcription, RNA biology, and DNA repair as well as recent advances that link ADP-ribosylation to stress responses, metabolism, viral infections ...
Rebecca Gupte, Ziying Liu, W. Kraus
semanticscholar   +1 more source

The Making and Breaking of Serine-ADP-Ribosylation in the DNA Damage Response

open access: yesFrontiers 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

ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function

open access: yesNucleic Acids Research, 2021
The functionality of DNA, RNA and proteins is altered dynamically in response to physiological and pathological cues, partly achieved by their modification. While the modification of proteins with ADP-ribose has been well studied, nucleic acids were only
L. Weixler   +5 more
semanticscholar   +1 more source

HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones

open access: yesNature Communications, 2021
Upon binding to DNA breaks, poly(ADP-ribose) polymerase 1 (PARP1) ADP-ribosylates itself and other factors to initiate DNA repair. Serine is the major residue for ADP-ribosylation upon DNA damage, which strictly depends on HPF1.
F. Sun   +5 more
semanticscholar   +1 more source

A Protein Semisynthesis-Based Strategy to Investigate the Functional Impact of Linker Histone Serine ADP-Ribosylation

open access: yes, 2022
Recently developed chemical and enzyme-based technologies to install serine ADP-ribosylation onto synthetic peptides have enabled new approaches to study poly­(ADP-ribose) polymerase (PARP) biology.
Chad A. Brautigam (242609)   +7 more
core   +1 more source

Roles of Asp179 and Glu270 in ADP-Ribosylation of Actin by Clostridium perfringens Iota Toxin. [PDF]

open access: yesPLoS 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

Protein and RNA ADP-ribosylation detection is influenced by sample preparation and reagents used

open access: yesLife Science Alliance, 2022
Mono(ADP-ribosyl)ation is an emerging modification, for which recently detection reagents were generated. We cross-validated all reagents and observe remarkable differences in efficiency, depending on the substrate investigated and on the methods that ...
L. Weixler   +11 more
semanticscholar   +1 more source

Proteasome Regulation by ADP-Ribosylation [PDF]

open access: yesCell, 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
openaire   +2 more sources

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