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001-es BibID:	BIBFORM048678
035-os BibID:	PMID:23290998
Első szerző:	Bürkle, Alexander
Cím:	Poly(ADP-ribose) : PARadigms and PARadoxes / Alexander Bürkle, László Virág
Dátum:	2013
ISSN:	0098-2997 1872-9452
Megjegyzések:	Poly(ADP-ribosyl)ation (PARylation) is a posttranslational protein modification (PTM) catalyzed by members of the poly(ADP-ribose) polymerase (PARP) enzyme family. PARPs use NAD(+) as substrate and upon cleaving off nicotinamide they transfer the ADP-ribosyl moiety covalently to suitable acceptor proteins and elongate the chain by adding further ADP-ribose units to create a branched polymer, termed poly(ADP-ribose) (PAR), which is rapidly degraded by poly(ADP-ribose) glycohydrolase (PARG) and ADP-ribosylhydrolase 3 (ARH3). In recent years several key discoveries changed the way we look at the biological roles and mode of operation of PARylation. These paradigm shifts include but are not limited to (1) a single PARP enzyme expanding to a PARP family; (2) DNA-break dependent activation extended to several other DNA dependent and independent PARP-activation mechanisms; (3) one molecular mechanism (covalent PARylation of target proteins) underlying the biological effect of PARPs is now complemented by several other mechanisms such as protein-protein interactions, PAR signaling, modulation of NAD(+) pools and (4) one principal biological role in DNA damage sensing expanded to numerous, diverse biological functions identifying PARP-1 as a real moonlighting protein. Here we review the most important paradigm shifts in PARylation research and also highlight some of the many controversial issues (or paradoxes) of the field such as (1) the mostly synergistic and not antagonistic biological effects of PARP-1 and PARG; (2) mitochondrial PARylation and PAR decomposition, (3) the cross-talk between PARylation and signaling pathways (protein kinases, phosphatases, calcium) and the (4) divergent roles of PARP/PARylation in longevity and in age-related diseases.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Apoptosis Calcium Cell death Chromatin structure DNA repair Kinase Mitochondria Necrosis Poly(ADP-ribose) glycohydrolase Poly(ADP-ribose) polymerase Signaling Transcription Molekuláris Medicina
Megjelenés:	Molecular Aspects of Medicine. - 34 : 6 (2013), p. 1046-1065. -
További szerzők:	Virág László (1965-) (biokémikus, sejtbiológus, farmakológus)
Pályázati támogatás:	TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP Oxidatív stressz és ADP-riboziláció kapcsolatának vizsgálata TÁMOP-4.2.2.A-11/1/KONV-2012-0025 TÁMOP
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001-es BibID:	BIBFORM047217
035-os BibID:	PMID:23357756
Első szerző:	Cantó, Carles
Cím:	Crosstalk between poly(ADP-ribose) polymerase and sirtuin enzymes / Carles Cantó, Anthony A. Sauve, Peter Bai
Dátum:	2013
ISSN:	0098-2997 1872-9452
Megjegyzések:	Poly(ADP-ribose) polymerases (PARPs) are NAD(+) dependent enzymes that were identified as DNA repair proteins, however, today it seems clear that PARPs are responsible for a plethora of biological functions. Sirtuins (SIRTs) are NAD(+)-dependent deacetylase enzymes involved in the same biological processes as PARPs raising the question whether PARP and SIRT enzymes may interact with each other in physiological and pathophysiological conditions. Hereby we review the current understanding of the SIRT-PARP interplay in regard to the biochemical nature of the interaction (competition for the common NAD(+) substrate, mutual posttranslational modifications and direct transcriptional effects) and the physiological or pathophysiological consequences of the interactions (metabolic events, oxidative stress response, genomic stability and aging). Finally, we give an overview of the possibilities of pharmacological intervention to modulate PARP and SIRT enzymes either directly, or through modulating NAD(+) homeostasis.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Molekuláris Medicina
Megjelenés:	Molecular Aspects of Medicine. - 34 : 6 (2013), p. 1168-1201. -
További szerzők:	Sauve, Anthony A. Bai Péter (1976-) (biokémikus)
Pályázati támogatás:	TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP Oxidatív stressz és ADP-riboziláció kapcsolatának vizsgálata TÁMOP-4.2.2/A-11/1/KONV-2012-0025 TÁMOP TÁMOP-4.2.2/B-10/1-2010-0024 TÁMOP
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001-es BibID:	BIBFORM048676
035-os BibID:	PMID:23727362
Első szerző:	Virág László (biokémikus, sejtbiológus, farmakológus)
Cím:	50Years of poly(ADP-ribosyl)ation / László Virág
Dátum:	2013
ISSN:	0098-2997 1872-9452
Megjegyzések:	The seminal paper published in 1963 by Chambon, Weil and Mandel reporting a new NAD-dependent protein modification now known as poly(ADP-ribosyl)ation (PARylation) marked the launch of a new era in both protein research and cell biology. In the coming decades, the identity, biochemical characteristics and regulation of enzymes responsible for the synthesis and degradation of protein-bound poly(ADP-ribose) have been discovered and the surprisingly multifarious biological roles of PARylation have not ceased to amaze cell and molecular biologists ever since. The review series on PARylation following this preface is comprised of ten papers written by great experts of the field and aims to provide practicing physicians and basic scientists with the state-of-the-art on the "writers, readers and erasers" of poly(ADP-ribose), some recent paradigm shifts of the field and its translational potential.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Carcinogenesis Cell death PARG PARP Poly(ADP-ribose) Poly(ADP-ribose) polymerase Transcription Molekuláris Medicina
Megjelenés:	Molecular Aspects of Medicine. - 34 : 6 (2013), p. 1043-1045. -
Pályázati támogatás:	TÁMOP-4.2.2-08/1-2008-0019 TÁMOP TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP Oxidatív stressz és ADP-riboziláció kapcsolatának vizsgálata
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001-es BibID:	BIBFORM048677
035-os BibID:	PMID:23416893
Első szerző:	Virág László (biokémikus, sejtbiológus, farmakológus)
Cím:	Poly(ADP-ribose) signaling in cell death / László Virág, Agnieszka Robaszkiewicz, Jose Manuel Rodriguez-Vargas, Francisco Javier Oliver
Dátum:	2013
ISSN:	0098-2997 1872-9452
Megjegyzések:	Poly(ADP-ribosyl)ation (PARylation) is a reversible protein modification carried out by the concerted actions of poly(ADP-ribose) polymerase (PARP) enzymes and poly(ADP-ribose) (PAR) decomposing enzymes such as PAR glycohydrolase (PARG) and ADP-ribosyl hydrolase 3 (ARH3). Reversible PARylation is a pleiotropic regulator of various cellular functions but uncontrolled PARP activation may also lead to cell death. The cellular demise pathway mediated by PARylation in oxidatively stressed cells has been described almost thirty years ago. However, the underlying molecular mechanisms have only begun to emerge relatively recently. PARylation has been implicated in necroptosis, autophagic cell death but its role in extrinsic and intrinsic apoptosis appears to be less predominant and depends largely on the cellular model used. Currently, three major pathways have been made responsible for PARP-mediated necroptotic cell death: (1) compromised cellular energetics mainly due to depletion of NAD, the substrate of PARPs; (2) PAR mediated translocation of apoptosis inducing factor (AIF) from mitochondria to nucleus (parthanatos) and (3) a mostly elusive crosstalk between PARylation and cell death/survival kinases and phosphatases. Here we review how these PARP-mediated necroptotic pathways are intertwined, how PARylation may contribute to extrinsic and intrinsic apoptosis and discuss recent developments on the role of PARylation in autophagy and autophagic cell death.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Apoptosis Autophagy Cell death Necroptosis Necrosis Oxidative stress Poly(ADP-ribose) glycohydrolase Poly(ADP-ribose) polymerase Molekuláris Medicina
Megjelenés:	Molecular Aspects of Medicine. - 34 : 6 (2013), p. 1153-1167. -
További szerzők:	Robaszkiewicz, Agnieszka (1983-) (biokémikus) Rodriguez-Vargas, Jose Manuel Oliver, Francisco Javier
Pályázati támogatás:	TÁMOP-4.2.2.A-11/1/KONV-2012-0025 TÁMOP TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP Oxidatív stressz és ADP-riboziláció kapcsolatának vizsgálata
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