Results 11 to 20 of about 188,515 (292)

Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG

open access: yesNature Communications
Ester-linked post-translational modifications, including serine and threonine ubiquitination, have gained recognition as important cellular signals. However, their detection remains a significant challenge due to the chemical lability of the ester bond ...
Edoardo José Longarini, Ivan Matić
doaj   +2 more sources

Molecular Tools for the Study of ADP‐Ribosylation: A Unified and Versatile Method to Synthesise Native Mono‐ADP‐Ribosylated Peptides [PDF]

open access: hybridChemistry, 2021
ADP‐ribosylation (ADPr), as a post‐translational modification, plays a crucial role in DNA‐repair, immunity and many other cellular and physiological processes. Serine is the main acceptor for ADPr in DNA damage response, whereas the physiological impact
Jim Voorneveld   +8 more
semanticscholar   +2 more sources

Ubiquitin pathway blockade reveals endogenous ADP-ribosylation marking PARP7 and AHR for degradation [PDF]

open access: yesThe EMBO Journal
ADP-ribosylation is an important protein post-translational modification catalysed by a family of PARP enzymes in humans and is involved in DNA damage and immunity among other processes.
Andrii Gorelik   +6 more
doaj   +2 more sources

Uncovering the Invisible: Mono-ADP-ribosylation Moved into the Spotlight

open access: yesCells, 2021
Adenosine diphosphate (ADP)-ribosylation is a nicotinamide adenine dinucleotide (NAD+)-dependent post-translational modification that is found on proteins as well as on nucleic acids.
Ann-Katrin Hopp, Michael O. Hottiger
doaj   +2 more sources

Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling

open access: yesNature Communications, 2023
In the mammalian DNA damage response, ADP-ribosylation signalling is of crucial importance to mark sites of DNA damage as well as recruit and regulate repairs factors.
Pietro Fontana   +9 more
doaj   +2 more sources

Global remodeling of ADP-ribosylation by PARP1 suppresses influenza A virus infection [PDF]

open access: yesNature Communications
ADP-ribosylation is a highly dynamic and fully reversible post-translational modification performed by PARP enzymes that modulates protein function, abundance, localization, and turnover. Here we show that PARPs mount an antiviral response to influenza A
Zhenyu Zhang   +17 more
doaj   +2 more sources

ADP-Ribosylation of Cytidine: A Novel Nucleic Acid Modification Reversed by NADAR Hydrolases [PDF]

open access: yesToxins
ADP-ribosylation of nucleic acids is a modification found in both eukaryotes and bacteria, where it contributes to genome maintenance but can also serve as a toxic mechanism used by bacterial toxins to disrupt essential cellular processes.
Petra Mikolčević   +6 more
doaj   +2 more sources

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   +2 more sources

PARP14 is regulated by the PARP9/DTX3L complex and promotes interferon γ-induced ADP-ribosylation

open access: yesThe EMBO Journal
Protein ADP-ribosylation plays important but ill-defined roles in antiviral signalling cascades such as the interferon response. Several viruses of clinical interest, including coronaviruses, express hydrolases that reverse ADP-ribosylation catalysed by ...
Victoria Chaves Ribeiro   +2 more
doaj   +2 more sources

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

open access: goldPLoS 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   +3 more sources

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