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1.

001-es BibID:BIBFORM005675
Első szerző:Benkő Szilvia (molekuláris biológus)
Cím:Dendritic cell subtypes as primary targets of vaccines : the emerging role and cross-talk of pattern recognition receptors / Szilvia Benko, Zoltan Magyarics, Attila Szabo, Eva Rajnavolgyi
Dátum:2008
ISSN:1437-4315
Megjegyzések:Preventive vaccination is the most successful approach against infectious diseases and has a great impact on world health. Vaccines operate through the activation of innate immunity that helps to stimulate antigen-specific T- and B-lymphocytes. These events are orchestrated by dendritic cells (DCs) that are able to sample foreign structures and concomitantly sense 'danger signals'. Thus, DCs provide a functional link between innate and acquired immunity, and due to their regulatory potential are referred to as natural adjuvants. Human conventional and plasmacytoid DCs express different sets of well-characterized Toll-like membrane receptors (TLRs) that recognize a broad range of conserved molecular patterns of pathogens. The recently discovered cytosolic Nod-like receptors (NLRs) and RIG-like helicases (RLHs) also turned out to participate in pathogen recognition and modulation of immune responses through interacting signaling pathways. As a result of their collaboration, the TLR, NLR and RLH recognition systems induce the secretion of different combinations of cytokines that play a fundamental role in T-cell activation and instruction. Ligands of the innate recognition systems emerge as new adjuvants for vaccine design, whereas manipulation of the signaling pathways mediated by these receptors offers new avenues for fine tuning immune responses and optimizing immunotherapies.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
cross-priming
cytokines
immunomodulation
innate immunity
signaling
T-cell polarization
Megjelenés:Biological Chemistry. - 389 : 5 (2008), p. 469-485. -
További szerzők:Magyarics Zoltán (1982-) (immunológus) Szabó Attila (1981-) (molekuláris biológus, immunológus, filozófus) Rajnavölgyi Éva (1950-) (immunológus)
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2.

001-es BibID:BIBFORM036713
Első szerző:Bögel Gábor
Cím:Frank-ter Haar syndrome protein Tks4 regulates EGF-dependent cell migration / Gábor Böge, Annamária Gujdár, Miklós Geiszt, Árpád Lányi, Anna Fekete, Szabolcs Sipeki, Julian Downward, László Buday
Dátum:2012
ISSN:0021-9258
Megjegyzések:Mutations in the SH3PXD2B gene coding for the Tks4 protein are responsible for the autosomal-recessive Frank-ter Haar syndrome. Tks4, a substrate of Src tyrosine kinase is implicated in the regulation of podosome formation. Here, we report a novel role for Tks4 in the EGF signalling pathway. In EGF-treated cells, Tks4 is tyrosine phosphorylated and associated with the activated EGF receptor. This association is not direct but requires the presence of Src tyrosine kinase. In addition, treatment of cells with LY294002, an inhibitor of PI 3-kinase, or mutations of the PX domain reduces tyrosine phosphorylation and membrane translocation of Tks4. Furthermore, a PX domain mutant (R43W) Tks4 carrying a reported point mutation in a Frank-ter Haar syndrome patient showed aberrant intracellular expression and reduced phosphoinositide binding. Finally, silencing of Tks4 was shown to markedly inhibit HeLa cell migration in a Boyden chamber assay in response to EGF or serum. Our results therefore reveal a new function for Tks4 in the regulation of growth factor-dependent cell migration.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
EGF receptor
Tks4
cell migration
Frank-ter Haar syndrome
PX domain
Molekuláris Medicina
Megjelenés:Journal Of Biological Chemistry. - 287 : 37 (2012), p. 31321-31329. -
További szerzők:Gujdár Annamária Geiszt Miklós Lányi Árpád (1962-) (biológus, immunológus) Fekete Anna Sipeki Szabolcs Downward, Julian Buday László
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
A HOFI/SH3PXD2B aktin citoszkeletont szabályozó új adaptor fehérje funkcionális vizsgálata
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3.

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
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4.

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
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5.

001-es BibID:BIBFORM005097
Első szerző:Szatmári István (biológus)
Cím:Peroxisome proliferator-activated receptor gamma-regulated ABCG2 expression confers cytoprotection to human dendritic cells / Szatmari, I., Vamosi, G., Brazda, P., Balint, B. L., Benko, S., Szeles, L., Jeney, V., Ozvegy-Laczka, C., Szanto, A., Barta, E., Balla, J., Sarkadi, B., Nagy, L.
Dátum:2006
ISSN:021-9258 (Print)
Megjegyzések:ABCG2, a member of the ATP-binding cassette transporters has been identified as a protective pump against endogenous and exogenous toxic agents. ABCG2 was shown to be expressed at high levels in stem cells and variably regulated during cell differentiation. Here we demonstrate that functional ABCG2 is expressed in human monocyte-derived dendritic cells by the activation of a nuclear hormone receptor, PPARgamma. We identified and characterized a 150-base pair long conserved enhancer region, containing three functional PPAR response elements (PPARE), upstream of the human ABCG2 gene. We confirmed the binding of the PPARgamma x RXR heterodimer to this enhancer region, suggesting that PPARgamma directly regulates the transcription of ABCG2. Consistent with these results, elevated expression of ABCG2 mRNA was coupled to enhanced protein production, resulting in increased xenobiotic extrusion capacity via ABCG2 in PPARgamma-activated cells. Furthermore PPARgamma instructed dendritic cells showed increased Hoechst dye extrusion and resistance to mitoxantrone. Collectively, these results uncovered a mechanism by which up-regulation of functional ABCG2 expression can be achieved via exogenous or endogenous activation of the lipid-activated transcription factor, PPARgamma. The increased expression of the promiscuous ABCG2 transporter can significantly modify the xenobiotic and drug resistance of human myeloid dendritic cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
agonists
Animals
antagonists & inhibitors
ATP-Binding Cassette Transporters
Base Sequence
biosynthesis
Cattle
Cell Differentiation
Cells
cytology
Cytoprotection
Dendritic Cells
Dogs
Drug Resistance
Drug Resistance,Neoplasm
genetics
Human
Humans
Hungary
metabolism
Mice
Molecular Sequence Data
Neoplasm Proteins
Phenotype
physiology
PPAR gamma
Proteins
Research
Support
Up-Regulation
Xenobiotics
Megjelenés:The Journal of Biological Chemistry. - 281 : 33 (2006), p. 23812-23823. -
További szerzők:Vámosi György (1967-) (biofizikus) Brázda Péter (1980-) (biológus, angol-magyar szakfordító) Bálint Bálint László (1971-) (kutató orvos) Benkő Szilvia (1973-) (molekuláris biológus) Széles Lajos (1971-) (molekuláris biológus) Jeney Viktória (1971-) (vegyész, kémia tanár) Özvegy-Laczka Csilla Szántó Attila (1976-) (orvos, biokémikus) Barta Endre (1963-) (molekuláris biológus) Balla József (1959-) (belgyógyász, nephrológus) Sarkadi Balázs Nagy László (1966-) (molekuláris sejtbiológus, biokémikus)
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