Results 31 to 40 of about 667,209 (277)

The relationship of the ADP-ribosylating enzyme from S. solfataricus with DING proteins and its intracellular localization [PDF]

open access: yes, 2010
The PARPSso thermoprotein from Sulfolobus solfataricus has been identified as a PARP-like enzyme that cleaves -NAD+ to synthesize oligomers of ADP-ribose and cross-reacts with polyclonal anti-PARP-1 catalytic site antibodies.
Porzio, Elena
core   +1 more source

Crystallographic and biochemical analysis of the mouse poly(ADP-ribose) glycohydrolase. [PDF]

open access: yesPLoS ONE, 2014
Protein poly(ADP-ribosyl)ation (PARylation) regulates a number of important cellular processes. Poly(ADP-ribose) glycohydrolase (PARG) is the primary enzyme responsible for hydrolyzing the poly(ADP-ribose) (PAR) polymer in vivo.
Zhizhi Wang   +3 more
doaj   +1 more source

Mitochondria are devoid of poly(ADP‐ribose)polymerase‐1, but harbor its product oligo(ADP‐ribose)

open access: yes, 2021
There are conflicting data about localization of poly(ADP-ribose)polymerase-1 and its product poly(ADP-ribose) in mitochondria. To finally clarify the discussion, we investigated with biochemical and cell biological methods the potential presence of poly(
Christian Blenn   +7 more
core   +1 more source

The Ups and Downs of Tannins as Inhibitors of Poly(ADP-Ribose)glycohydrolase

open access: yesMolecules, 2011
DNA damage to cells activates nuclear poly(ADP-ribose)polymerases (PARPs) and the poly(ADP-ribose) (PAR) synthesized is rapidly cleaved into ADP-ribose (ADPR) by PAR glycohydrolase (PARG) action.
Felix R. Althaus   +2 more
doaj   +1 more source

RNA Regulation by Poly(ADP-Ribose) Polymerases [PDF]

open access: yesMolecular Cell, 2015
Posttranscriptional regulation of RNA facilitates the fine-tuning of gene expression. It occurs through multiple pathways that include the nuclear processing of mRNA and its precursors, mRNA silencing, regulation of mRNA decay, and regulation of translation. Poly(ADP-ribose) polymerases (PARPs), enzymes that modify target proteins with ADP-ribose, play
Bock, Florian J.   +2 more
openaire   +2 more sources

The Dichotomy of the Poly(ADP-Ribose) Polymerase-Like Thermozyme from Sulfolobus solfataricus

open access: yesChallenges, 2018
The first evidence of an ADP-ribosylating activity in Archaea was obtained in Sulfolobus solfataricus(strain MT-4) where a poly(ADP-ribose) polymerase (PARP)-like thermoprotein, defined with the acronymous PARPSso, was found.
Maria Rosaria Faraone Mennella
doaj   +1 more source

Complete pathological response to olaparib and bevacizumab in advanced cervical cancer following chemoradiation in a BRCA1 mutation carrier: a case report

open access: yesJournal of Medical Case Reports, 2021
Background Homologous recombination deficiency is a marker of response to poly(ADP-ribose) polymerase inhibitors in different cancer types including ovary, prostate, and pancreatic cancer.
Rosa Montero-Macias   +12 more
doaj   +1 more source

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

Structural modeling of NAD+ binding modes to PARP-1

open access: yesВавиловский журнал генетики и селекции, 2017
The nuclear protein poly (ADP-ribose) polymerase-1 (PARP-1) plays an important role in the signaling and repair of DNA. PARP-1 catalyses covalent binding of poly (ADP-ribose) polymers with itself as well as with other acceptor proteins using NAD+ as a ...
N. V. Ivanisenko   +2 more
doaj   +1 more source

Methods for Purification of Proteins Associated with Cellular Poly(ADP-Ribose) and PARP-Specific Poly(ADP-Ribose)

open access: yes, 2011
available in PMC 2012 November 09Poly(ADP-ribose) (pADPr) is a posttranslational modification that regulates protein function through two major mechanisms: covalent modification of acceptor proteins and noncovalent binding of proteins to pADPr.
Leung, Anthony   +5 more
core   +1 more source

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