Results 71 to 80 of about 214,575 (242)

The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome

open access: yesNature Communications, 2021
ADP-ribosylation is regulated by HPF1 and ARH3, but the cellular target spectrum of these enzymes is not fully understood. Here, the authors use quantitative proteomics to define the HPF1- and ARH3-dependent ADP-ribosylome, providing evidence that mono ...
Ivo A. Hendriks   +9 more
doaj   +1 more source

The ADP-Ribosylating Toxins of Salmonella [PDF]

open access: yesToxins, 2019
A number of pathogenic bacteria utilize toxins to mediate disease in a susceptible host. The foodborne pathogen Salmonella is one of the most important and well-studied bacterial pathogens. Recently, whole genome sequence characterizations revealed the presence of multiple novel ADP-ribosylating toxins encoded by a variety of Salmonella serovars.
Rachel A. Cheng, Martin Wiedmann
openaire   +3 more sources

Poly(ADP)ribosylation of nuclear proteins in the mouse testis

open access: yes, 1984
In "Proceedings of the 7th Intern. Symp.
R.,. JONES   +22 more
core   +1 more source

ADP-ribosylation: from molecular mechanisms to human disease

open access: yes, 2020
Post-translational modification of proteins by ADP-ribosylation, catalysed by poly (ADP-ribose) polymerases (PARPs) using NAD+ as a substrate, plays central roles in DNA damage signalling and repair, modulates a range of cellular signalling cascades and ...
Nicolas C. Hoch (8141358)   +1 more
core   +1 more source

Regulation of Rad52-dependent replication fork recovery through serine ADP-ribosylation of PolD3

open access: yesNature Communications, 2023
Although Poly(ADP-ribose)-polymerases (PARPs) are key regulators of genome stability, how site-specific ADP-ribosylation regulates DNA repair is unclear.
Frederick Richards   +7 more
doaj   +1 more source

Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue

open access: yesNature Communications, 2016
ADP-ribosylation is a reversible post-translational protein modification involved in many cellular processes. Here the authors describe a sensitive approach for the analysis of ADP-ribosylation sites under physiologic conditions and identify lysine ...
Rita Martello   +7 more
doaj   +1 more source

Chemical genetics and proteome-wide site mapping reveal cysteine MARylation by PARP-7 on immune-relevant protein targets

open access: yeseLife, 2021
Poly(ADP-ribose) polymerase 7 (PARP-7) has emerged as a critically important member of a large enzyme family that catalyzes ADP-ribosylation in mammalian cells. PARP-7 is a critical regulator of the innate immune response.
Kelsie M Rodriguez   +10 more
doaj   +1 more source

ADP-Ribosylation Regulates the Signaling Function of IFN-γ

open access: yesFrontiers in Immunology, 2021
Murine T cells express the GPI-anchored ADP-ribosyltransferase 2.2 (ARTC2.2) on the cell surface. In response to T cell activation or extracellular NAD+ or ATP-mediated gating of the P2X7 ion channel ARTC2.2 is shed from the cell surface as a soluble ...
Stephan Menzel   +6 more
doaj   +1 more source

SnapShot: ADP-Ribosylation Signaling [PDF]

open access: yesMolecular Cell, 2015
Intracellular protein ADP-ribosylation is catalyzed by diphteria toxin-like ADP-ribosyltransferases (ARTDs, formerly PARPs) ("writers"), which use NAD(+) for the modification of different amino acids. While some ARTD members catalyze protein poly-ADP-ribosylation, most of them are mono-ADP-ribosyltransferases.
openaire   +4 more sources

ADP-ribosyl-N3: A Versatile Precursor for Divergent Syntheses of ADP-ribosylated Compounds [PDF]

open access: yesMolecules, 2017
Adenosine diphosphate-ribose (ADP-ribose) and its derivatives play important roles in a series of complex physiological procedures. The design and synthesis of artificial ADP-ribosylated compounds is an efficient way to develop valuable chemical biology tools and discover new drug candidates.
Lingjun Li   +6 more
openaire   +2 more sources

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