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001-es BibID:	BIBFORM041839
Első szerző:	Boldogh István
Cím:	Activation of ras signaling pathway by 8-oxoguanine DNA glycosylase bound to its excision product, 8-oxoguanine / Istvan Boldogh, Gyorgy Hajas, Leopoldo Aguilera-Aguirre, Muralidhar L. Hegde, Zsolt Radak, Attila Bacsi, Sanjiv Sur, Tapas K. Hazra, Sankar Mitra
Dátum:	2012
ISSN:	0021-9258
Megjegyzések:	8-Oxo-7,8-dihydroguanine (8-oxoG), arguably the most abundant base lesion induced in mammalian genomes by reactive oxygen species, is repaired via the base excision repair pathway that is initiated with the excision of 8-oxoG by OGG1. Here we show that OGG1 binds the 8-oxoG base with high affinity and that the complex then interacts with canonical Ras family GTPases to catalyze replacement of GDP with GTP, thus serving as a guanine nuclear exchange factor. OGG1-mediated activation of Ras leads to phosphorylation of the mitogen-activated kinases MEK1,2/ERK1,2 and increasing downstream gene expression. These studies document for the first time that in addition to its role in repairing oxidized purines, OGG1 has an independent guanine nuclear exchange factor activity when bound to 8-oxoG.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Journal of Biological Chemistry 287 : 25 (2012), p. 20769-20773. -
További szerzők:	Hajas György (1970-) (biológus) Aguilera-Aguirre, Leopoldo Hegde, Muralidhar L. Radák Zsolt Bácsi Attila (1967-) (immunológus) Sur, Sanjiv Hazra, Tapas K. Mitra, Sankar
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM113591
035-os BibID:	(scopus)85166243364 (cikkazonosító)105028
Első szerző:	Pan, Lang
Cím:	Nei-like DNA glycosylase 2 (NEIL2) selectively antagonizes interferon-β expression upon respiratory syncytial virus infection / Pan Lang, Xue Yaoyao, Wang Ke, Zheng Xu, Islam Azharul, Tapryal Nisha, Chakraborty Anirban, Bacsi Attila, Ba Xueqing, Hazra Tapas K., Boldogh Istvan
Dátum:	2023
ISSN:	0021-9258 1083-351X
Megjegyzések:	As part of the antiviral response, cells activate the expressions of type I interferons (IFNs) and proinflammatory mediators to control viral spreading. Viral infections can impact DNA integrity, however, how DNA damage-repair coordinates antiviral response remains elusive. Here we report Nei-like DNA glycosylase 2 (NEIL2), a transcription-coupled DNA repair protein, actively recognizes the oxidative DNA substrates induced by respiratory syncytial virus (RSV) infection to set the threshold of IFN-? expression. Our results show that NEIL2 antagonizes nuclear factor ?B (NF-?B) acting on the IFN-? promoter early after infection, thus limiting gene expression amplified by type I IFNs. Mice lacking Neil2 are far more susceptible to RSV-induced illness with exuberant expression of proinflammatory genes and tissue damage, and the administration of NEIL2 protein into the airway corrected these defects. These results suggest a safeguarding function of NEIL2 in controlling IFN-? levels against RSV infection. Due to the short and long term side effects of type I IFNs applied in antiviral therapy, NEIL2 may provide an alternative not only for ensuring genome fidelity, but also for controlling immune responses.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk oxidative stress DNA damage NF-kB transcription regulation inflammation innate immunity antiviral response
Megjelenés:	Journal Of Biological Chemistry. - 299 : 8 (2023), p. 1-15. -
További szerzők:	Xue, Yaoyao Wang, Ke Zheng, Xu Islam, Azharul Tapryal, Nisha Chakraborty, Anirban Bácsi Attila (1967-) (immunológus) Ba, Xueqing Hazra, Tapas K. Boldogh István
Pályázati támogatás:	TKP2021-EGA-19 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM069722
Első szerző:	Pan, Lang
Cím:	Oxidized Guanine Base Lesions Function in 8-Oxoguanine DNA Glycosylase-1-mediated Epigenetic Regulation of Nuclear Factor ?B-driven Gene Expression / Lang Pan, Bing Zhu, Wenjing Hao, Xianlu Zeng, Spiros A. Vlahopoulos, Tapas K. Hazra, Muralidhar L. Hegde, Zsolt Radak, Attila Bacsi, Allan R. Brasier, Xueqing Ba, Istvan Boldogh
Dátum:	2016
ISSN:	0021-9258 1083-351X
Megjegyzések:	A large percentage of redox-responsive gene promoters containevolutionarily conserved guanine-rich clusters; guaninesare the bases most susceptible to oxidative modification(s). Consequently,7,8-dihydro-8-oxoguanine (8-oxoG) is one of themost abundant base lesions in promoters and is primarilyrepaired via the 8-oxoguanine DNA glycosylase-1 (OOG1)-initiatedbase excision repair pathway. In view of a prompt cellularresponse to oxidative challenge, we hypothesized that the8-oxoG lesion and the cognate repair protein OGG1 are utilizedin transcriptional gene activation. Here, we document TNF -induced enrichment of both 8-oxoG and OGG1 in promoters ofpro-inflammatory genes, which precedes interaction of NF- Bwith its DNA-binding motif. OGG1 bound to 8-oxoG upstreamfrom the NF- B motif increased its DNA occupancy by promotingan on-rate of both homodimeric and heterodimeric forms ofNF- B. OGG1 depletion decreased both NF- B binding andgene expression, whereas Nei-like glycosylase-1 and -2 had amarginal effect. These results are the first to document a novelparadigm wherein the DNA repair protein OGG1 bound to itssubstrate is coupled to DNA occupancy of NF- B and functionsin epigenetic regulation of gene expression.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban 8-oxoguanine DNA glycosylase1 8-oxoguanine NF-kappaB gene expression inflammation
Megjelenés:	Journal Of Biological Chemistry 291 : 49 (2016), p. 25553-25566. -
További szerzők:	Zhu, Bing Hao, Wenjing Zeng, Xianlu Vlahopoulos, Spiros A. Hazra, Tapas K. Hegde, Muralidhar L. Radák Zsolt Bácsi Attila (1967-) (immunológus) Brasier, Allan R. Ba, Xueqing Boldogh István
Pályázati támogatás:	United States National Institute of Environmental Health and Sciences (grant number: RO1 ES018948 to IB) Egyéb United States National Institute of Allergic and Infectious Diseases (grant number: PO1-AI062885, to ARB and IB) Egyéb United States National Institute of Environmental Health and Sciences Center Grant (grant number: P30 ES006676 to ARB, IB) Egyéb National Science Foundation of China (grant number: 31571339 to XB) Egyéb
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
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