Results 31 to 40 of about 77,829 (292)

ARH Family of ADP-Ribose-Acceptor Hydrolases

open access: yesCells, 2022
The ARH family of ADP-ribose-acceptor hydrolases consists of three 39-kDa members (ARH1-3), with similarities in amino acid sequence. ARH1 was identified based on its ability to cleave ADP-ribosyl-arginine synthesized by cholera toxin.
Hiroko Ishiwata-Endo   +6 more
doaj   +1 more source

The PARP1/ARTD1-Mediated Poly-ADP-Ribosylation and DNA Damage Repair in B Cell Diversification

open access: yesAntibodies, 2014
ADP-ribosylation is an essential post-translational modification, mediated by a family of proteins named poly-ADP-ribose polymerases/Diphtheria toxin-like ADP-ribosyltransferases (PARPs/ARTDs), that functions to assist in cellular homeostasis through an ...
Jackline J.M. Lasola   +3 more
doaj   +1 more source

ADP-Ribosylation Factor 6 Regulates a Novel Plasma Membrane Recycling Pathway

open access: yesJournal of Cell Biology, 1997
ADP-ribosylation factor (ARF) 6 localizes to the plasma membrane (PM) in its GTP state and to a tubulovesicular compartment in its GDP state in HeLa cells that express wild-type or mutant forms of this GTPase.
H. Radhakrishna, J. Donaldson
semanticscholar   +1 more source

PARP-3 and APLF function together to accelerate nonhomologous end joining [PDF]

open access: yes, 2010
PARP-3 is a member of the ADP-ribosyl transferase superfamily of unknown function. We show that PARP-3 is stimulated by DNA double-strand breaks (DSBs) in vitro and functions in the same pathway as the poly (ADP-ribose)-binding protein APLF to accelerate
Ahel   +59 more
core   +1 more source

Partial (13)C isotopic enrichment of nucleoside monophosphates: useful reporters for NMR structural studies [PDF]

open access: yes, 2005
Analysis of the (13)C isotopic labeling patterns of nucleoside monophosphates (NMPs) extracted from Escherichia coli grown in a mixture of C-1 and C-2 glucose is presented. By comparing our results to previous observations on amino acids grown in similar
Kishore, Anita I.   +2 more
core   +2 more sources

APLF (C2orf13) is a novel component of poly(ADP-ribose) signaling in mammalian cells [PDF]

open access: yes, 2008
APLF is a novel protein of unknown function that accumulates at sites of chromosomal DNA strand breakage via forkhead-associated (FHA) domain-mediated interactions with XRCC1 and XRCC4.
Caldecott, Keith W   +4 more
core   +3 more sources

Altered cytoplasmic and nuclear ADP‐ribosylation levels analyzed with an improved ADP‐ribose binder are a prognostic factor in renal cell carcinoma

open access: yesThe Journal of Pathology: Clinical Research, 2023
ADP‐ribosylation (ADPR) of proteins is catalyzed by ADP‐ribosyltransferases, which are targeted by inhibitors (i.e. poly(ADP‐ribose) polymerase inhibitors [PARPi]). Although renal cell carcinoma (RCC) cells are sensitive in vitro to PARPi, studies on the
Peter Schraml   +6 more
doaj   +1 more source

To translate, or not to translate: viral and host mRNA regulation by interferon-stimulated genes. [PDF]

open access: yes, 2015
Type I interferon (IFN) is one of the first lines of cellular defense against viral pathogens. As a result of IFN signaling, a wide array of IFN-stimulated gene (ISG) products is upregulated to target different stages of the viral life cycle.
Li, Melody MH   +2 more
core   +1 more source

Regulation of Transcription Factor NFAT by ADP-Ribosylation [PDF]

open access: yesMolecular and Cellular Biology, 2008
ADP-ribosylation is a reversible posttranslational modification mediated by poly-ADP-ribose polymerase (PARP). The results of recent studies demonstrate that ADP-ribosylation contributes to transcription regulation. Here, we report that transcription factor NFAT binds to and is ADP-ribosylated by PARP-1 in an activation-dependent manner ...
Opeyemi A, Olabisi   +8 more
openaire   +2 more sources

Inhibition of Cell Migration by PITENINs: The Role of ARF6 [PDF]

open access: yes, 2012
We have previously reported the development of small molecule phosphatidylinositol-3,4,5-trisphosphate (PIP3) antagonists (PITs) that block pleckstrin homology (PH) domain interaction, including activation of Akt, and show anti-tumor potential.
Degterev, Alexei   +9 more
core   +1 more source

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