Results 51 to 60 of about 188,515 (292)
ADP-ribosylation of RNA in mammalian cells is mediated by TRPT1 and multiple PARPs
Nucleic Acids Research, 2022 RNA function relies heavily on posttranscriptional modifications. Recently, it was shown that certain PARPs and TRPT1 can ADP-ribosylate RNA in vitro. Traditionally, intracellular ADP-ribosylation has been considered mainly as a protein posttranslational
L. Weixler, Karla L. H. Feijs, R. Žaja
semanticscholar +1 more source
Poly(ADP-Ribosyl) Code Functions [PDF]
Acta Naturae, 2021 Poly(ADP-ribosyl)ation plays a key role in cellular metabolism. Covalent poly(ADP-ribosyl)ation affects the activity of the proteins engaged in DNA repair, chromatin structure regulation, gene expression, RNA processing, ribosome biogenesis, and protein translation.
Maluchenko, N. V. +4 more
openaire +2 more sources
Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease
Molecules 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 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
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
ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function
Nucleic 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
Nature 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
PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
Genes & 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
Ubiquitination accomplished: E1 and E2 enzymes were not necessary [PDF]
, 2016 Qiu et al. (2016) show that a mono-ADP-ribosyltransferase, SdeA, from Legionella pneumophila catalyzes ADP-ribosylation of ubiquitin, allowing SdeA to modify substrate with ubiquitin in the absence of E1 and E2 ...
Huang, Danny T., Nakasone, Mark
core +1 more source
Sequential ADP‐ribosylation pattern of nucleosomal histones [PDF]
European Journal of Biochemistry, 1985 The pattern of nucleosomal histones poly(ADP‐ribosyl)ation is changed under conditions which affect the poly(ADP‐ribosyl)ation state of the enzyme. At low NAD concentrations the enzyme can poly(ADP‐ribosyl)ate histones H1 and H1°, H2A, A2A, and H2B. However at NAD concentrations above 10 μM the enzyme preferentially poly(ADP‐ribosyl)ates histone H1 to ...
Ann Huletsky +5 more
openalex +4 more sources