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001-es BibID:BIBFORM042744
Első szerző:Góth László (analitikus)
Cím:Acatalasemia and diabetes mellitus / László Góth, Teréz Nagy
Dátum:2012
Megjegyzések:The enzyme catalase catalyzes the breakdown of hydrogen peroxide into oxygen and water. It is the mainregulator of hydrogen peroxide metabolism. Hydrogen peroxide is a highly reactive small moleculeformed as a natural byproducts of energy metabolism. Excessive concentrations may cause significantdamages to protein, DNA, RNA and lipids. Low levels in muscle cells, facilitate insulin signaling. Acatalasemiais a result of the homozygous mutations in the catalase gene, has a worldwide distribution with 12known mutations. Increased hydrogen peroxide, due to catalase deficiency, plays a role in the pathogenesisof several diseases such as diabetes mellitus. Diabetes mellitus is a disorder caused by multiplegenetic and environmental factors. Examination of Hungarian diabetic and acatalasemic patients showedthat an increased frequency of catalase gene mutations exists among diabetes patients. Inherited catalasedeficiency may increase the risk of type 2 diabetes mellitus, especially for females. Early onset of type 2diabetes occurs with inherited catalase deficiency. Low levels of SOD and glutathione peroxidase couldcontribute to complications caused by increased oxidative stress.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
acatalasemia
diabetes
reactive oxygen species
catalse
hydrogen peroxide
Megjelenés:Arcives of Biochemistry and Biophysics. - 525 : 2 (2012), p. 195-200. -
További szerzők:Nagy Teréz (1971-) (molekuláris biológus)
Pályázati támogatás:T 71902
OTKA
Internet cím:DOI
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2.

001-es BibID:BIBFORM103651
035-os BibID:(cikkazonosító)109184 (scopus)85128192258 (wos)000793580100003
Első szerző:Imre László (biológus)
Cím:Nucleosome destabilization by polyamines / Imre Laszlo, Niaki Erfaneh Firouzi, Bosire Rosevalentine, Nanasi Peter Jr., Nagy Peter, Bacso Zsolt, Hamidova Nubar, Pommier Yves, Jordan Albert, Szabo Gabor
Dátum:2022
ISSN:0003-9861
Megjegyzések:The roles and molecular interactions of polyamines (PAs) in the nucleus are not fully understood. Here their effect on nucleosome stability, a key regulatory factor in eukaryotic gene control, is reported, as measured in agarose embedded nuclei of H2B-GFP expressor HeLa cells. Nucleosome stability was assessed by quantitative microscopy [1,2] in situ, in close to native state of chromatin, preserving the nucleosome constrained topology of the genomic DNA. A robust destabilizing effect was observed in the millimolar concentration range in the case of spermine, spermidine as well as putrescine, which was strongly pH and salt concentration-dependent, and remained significant also at neutral pH. The integrity of genomic DNA was not affected by PA treatment, excluding DNA break-elicited topological relaxation as a factor in destabilization. The binding of PAs to DNA was demonstrated by the displacement of ethidium bromide, both from deproteinized nuclear halos and from plasmid DNA. The possibility that DNA methylation patterns may be influenced by PA levels is contemplated in the context of gene expression and DNA methylation correlations identified in the NCI-60 panel-based CellMiner database: methylated loci in subsets of high-ODC1 cell lines and the dependence of PER3 DNA methylation on PA metabolism.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Archives Of Biochemistry And Biophysics. - 722 (2022), p. 1-11. -
További szerzők:Niaki, Erfaneh Firouzi Bosire, Rosevalentine (1988-) (biotechnológus) Nánási Péter Pál ifj. (1987-) (sejtbiológus) Nagy Péter (1971-) (biofizikus) Bacsó Zsolt (1963-) (biofizikus) Hamidova, Nubar Pommier, Yves Jordan, Albert Szabó Gábor (1953-) (biofizikus)
Pályázati támogatás:K128770
OTKA
K138524
OTKA
COST
Egyéb
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DOI
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3.

001-es BibID:BIBFORM003560
Első szerző:Kókai Endre (biokémikus, biológus)
Cím:CG15031/PPYR1 is an intrinsically unstructured protein that interacts with protein phosphatase Y / Kókai E., Tantos Á., Vissi E., Szöőr B., Tompa P., Gausz J., Alphey L., Friedrich P., Dombrádi V.
Dátum:2006
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
protein phosphatases Y
protein-protein interaction
CG15031 gene product
heat-stable unstructured RNA-binding protein
Drosophila melanogaster
intrinsically unstructured protein
protein phosphorylation
Megjelenés:Archives of Biochemistry and Biophysics. - 451 : 1 (2006), p. 59-67. -
További szerzők:Tantos Ágnes Vissi Emese (1968-) (biokémikus, biológus) Szöőr Balázs (1966-) (biokémikus) Tompa Péter Gausz János Alphey, Luke Friedrich Péter Dombrádi Viktor (1953-) (biokémikus)
Internet cím:elektronikus változat
DOI
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4.

001-es BibID:BIBFORM045358
035-os BibID:PMID:22286031
Első szerző:Nagy Teréz (molekuláris biológus)
Cím:A simple method for examination of polymorphisms of catalase exon 9: rs769217 in Hungarian microcytic anemia and beta-thalassemia patients / Nagy T., Csordás M., Kósa Zs., Góth L.
Dátum:2012
ISSN:0003-9861
Megjegyzések:Catalase decreases the high, toxic concentrations of hydrogen peroxide but it lets the physiological, low concentrations in the cells mainly for signaling purposes. Its decreased activity may contribute to development of several pathological conditions. Catalase mutations occur frequently in exon 9, these were examined with different, complicated and costly methods. The aim of the current study was to evaluate a method for screening of polymorphisms in catalase exon 9. We used the slab gel electrophoresis of PCR amplicons without denaturation and silver staining for visualization of the DNA bands. We detected extra DNA bands in the 400-800 bp region of the catalase exon 9. Their single stranded nature was proved with nucleotide sequence analyses, comparison with the standard SSCP, staining with Sybr Green II and Sybr Green I, ethidium bromide, no digestion with RFLP (BstX I), and digestion with plant nuclease. We used this method for examination of polymorphisms of catalase exon 9 in microcytic anemia and beta-thalassemia patients. The lowest blood catalase activities were detected in microcytic anemia and beta-thalassemia patients with the TT genotypes of the C111T polymorphism. This method was sensitive for detection of G113A acatalasemia mutation, but poorly detected C37T and G5A acatalasemia mutations.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Archives of Biochemistry and Biophysics 525 : 2 (2012), p. 201-206. -
További szerzők:Csordás Melinda Kósa Zsuzsanna Góth László (1943-) (analitikus)
Internet cím:DOI
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5.

001-es BibID:BIBFORM076953
035-os BibID:(WoS)000480371000008 (Scopus)85060845864 (PubMed)30710503
Első szerző:Szekanecz Zoltán (reumatológus, belgyógyász, immunológus)
Cím:The NLRP3 inflammasome - interleukin 1 pathway as a therapeutic target in gout / Zoltán Szekanecz, Szilvia Szamosi, Gergő E. Kovács, Elek Kocsis, Szilvia Benkő
Dátum:2019
ISSN:0003-9861
Megjegyzések:The NLRP3 inflammasome is implicated in the processing of the pro-inflammatory cytokine interleukin 1β. Inflammatory disorders associated with the activation of the NLRP3 inflammasome - IL-1 axis are termed autoinflammatory diseases. Gout is an autoinflammatory disease, which is triggered by the deposition of monosodium urate crystals of precipitated uric acid. It is characterized by recurrent attacks of inflammation due to the activation of phagocytic cells that try to clear the crystals. NLRP3 inflammasome-mediated IL-1β production plays a key role in the manifestation of the disease. Currently, the best approach to treat gout is to reduce uric acid concentration by targeting xanthine oxidase or uric acid transporters, or to use non-steroidal anti-inflammatory drugs. Nevertheless, most of these treatments are not effective enough and may results in side effects. During the past decades, our knowledge has greatly improved about the molecular mechanisms of NLRP3 activation. This knowledge enables and urges scientists to discover or design drugs that target pathways of NLRP3 inflammasome activation, or more preferentially, NLRP3 inflammasome itself. In this review, we discuss the already available drugs and products, that target the diverse pathways of the NLRP3 - IL-1β axis, and the future therapeutic perspectives.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Inflammasome
NLRP3
Interleukin 1
Gout
Autoinflammatory disease
Megjelenés:Archives of Biochemistry and Biophysics. - 670 (2019), p. 82-93. -
További szerzők:Szamosi Szilvia (1975-) (belgyógyász, reumatológus) Kovács Elek Gergő Kocsis Elek Benkő Szilvia (1973-) (molekuláris biológus)
Pályázati támogatás:EFOP-3.6.2-16-2017-00006
EFOP
TAMOP-4.2.4.A/2-11/1-2012-0001
TÁMOP
GINOP-2.3.2-15-2016-00015
GINOP
GINOP-2.3.2-15-2016-00050
GINOP
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DOI
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6.

001-es BibID:BIBFORM027917
Első szerző:Vissi Emese (biokémikus, biológus)
Cím:Protein phosphatase 1 catalytic subunit isoforms from alfalfa : biochemical characterization and cDNA cloning / Emese Vissi, Éva Csordás Tóth, Izabella Kovács, Zoltán Magyar, Gábor V. Horváth, Péter Bagossi, Pál Gergely, Dénes Dudits, Viktor Dombrádi
Dátum:1998
Megjegyzések:The catalytic subunit of protein phosphatase 1 (PP1c) was purified from an alfalfa (Medicago sativa) microcallus cell culture. The preparation was inhibited by rabbit muscle inhibitor-2 and okadaic acid and had a molecular mass of 35 kDa. Five distinct cDNAs termed MsPP1alpha, -beta, -gamma, -delta, and -epsilon were cloned from a M. sativa somatic embryo library. MsPP1alpha was identical to a cDNA reported earlier [A. Páy, M. Pirck, L. Bögre, H. Hirt, and E. Heberle-Bors Mol. Gen. Genet. 244, 176-182, 1994], while the others represented novel isoforms encoded by separate genes. The predicted amino acid sequences of MsPP1alpha, -beta, -gamma, -delta, and -epsilon were highly similar to each other and to other known PP1c sequences. The GST-MsPP1ss fusion protein expressed in Escherichia coli was catalytically active and was inhibited by inhibitor-2 and okadaic acid. Affinity-purified polyclonal MsPP1antipeptide antibody detected a protein of 36 kDa in crude cell extracts. These results proved that the cDNA clone encoded an active PP1c which was very similar to the purified enzyme. The mRNA and protein concentrations of PP1c as well as the specific activity of protein phosphatase 1 did not change during the cell cycle in a synchronized alfalfa cell culture. On the other hand, the isoforms exhibited different steady-state mRNA levels in different plant organs suggesting tissue-specific functions.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
protein phosphatase1
Medicago sativa
protein purification
cDNA sequencing
cell cycle
gene expression
egyetemen (Magyarországon) készült közlemény
Megjelenés:Archives of Biochemistry and Biophysics. - 360 : 2 (1998), p. 206-214. -
További szerzők:Csordás Tóth Éva Kovács Izabella (Szeged) Magyar Zoltán Horváth Gábor V. Bagossi Péter (1966-2011) (biokémikus, vegyész) Dudits Dénes Gergely Pál (1947-) (biokémikus) Dombrádi Viktor (1953-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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