Results 71 to 80 of about 188,515 (292)

RhoA GTPase switch controls Cx43-hemichannel activity through the contractile system [PDF]

open access: yes, 2012
ATP-dependent paracrine signaling, mediated via the release of ATP through plasma membrane-embedded hemichannels of the connexin family, coordinates a synchronized response between neighboring cells.
Bultynck, Geert   +7 more
core   +13 more sources

HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation

open access: yesNature, 2020
The anti-cancer drug target poly(ADP-ribose) polymerase 1 (PARP1) and its close homologue, PARP2, are early responders to DNA damage in human cells 1 , 2 .
M. Suskiewicz   +11 more
semanticscholar   +1 more source

The potential role and application of PARP inhibitors in cancer treatment [PDF]

open access: yes, 2009
Background: Since many anti-cancer agents act by inflicting DNA damage on tumour cells, there is increasing interest in the use of inhibitors of DNA repair to increase the cytotoxicity of these agents.
Chalmers, Anthony J
core   +2 more sources

Role of APD-Ribosylation in Bone Health and Disease

open access: yesCells, 2019
The transfer of adenosine diphosphate (ADP)-ribose unit(s) from nicotinamide adenine dinucleotide (NAD+) to acceptor proteins is known as ADP-ribosylation.
Chun Wang, Gabriel Mbalaviele
doaj   +1 more source

Streptomyces coelicolor macrodomain hydrolase SCO6735 cleaves thymidine-linked ADP-ribosylation of DNA

open access: yesComputational and Structural Biotechnology Journal, 2022
ADP-ribosylation is an ancient, highly conserved, and reversible covalent modification critical for a variety of endogenous processes in both prokaryotes and eukaryotes.
Andrea Hloušek-Kasun   +9 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

A novel physiological role for ARF1 in the formation of bidirectional tubules from the Golgi. [PDF]

open access: yes, 2017
Capitalizing on CRISPR/Cas9 gene-editing techniques and super-resolution nanoscopy, we explore the role of the small GTPase ARF1 in mediating transport steps at the Golgi.
Baddeley, David   +12 more
core   +2 more sources

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

Mono ADP-ribosylation and Poly ADP-ribosylation of Proteins [PDF]

open access: yes, 1981
Postsynthetic modification of proteins by transfer of ADP-ribosyl groups from NAD has been shown to occur in numerous systems. Besides ADPR transferase reactions associated with the action of bacterial toxins and viruses, ADP ribosylation reactions were also observed in eukaryotic cells (cf.
H. Hilz   +3 more
openaire   +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

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