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001-es BibID:	BIBFORM004740
035-os BibID:	(WOS)000184609400011 (scopus)12444317206
Első szerző:	Szilágyi Ildikó (orvos)
Cím:	Non-random features of loop-size chromatin fragmentation / Szilagyi, I., Varga, T., Szekvolgyi, L., Hegedus, E., Goda, K., Kaczur, V., Bacso, Z., Nakayama, Y., Posafi, J., Pongor, S., Szabo, G.
Dátum:	2003
ISSN:	730-2312 (Print)
Megjegyzések:	Upon isolation of DNA from normal eukaryotic cells by standard methods involving extensive proteolytic treatment, a rather homogeneous population of loop-size, double-stranded DNA fragments is regularly obtained. These DNA molecules can be efficiently end-labeled by the DNA polymerase I Klenow fragment, as well as by a 3'- to -5'-exonuclease-free Klenow enzyme, but not by terminal transferase (TdT) unless the ends have been filled up by Klenow, suggesting that dominantly 5' protruding termini are generated upon fragmentation. The filled-up termini were used for cloning the distal parts of the approximately 50 kb fragments. BLAST analysis of the sequence of several clones allowed us to determine the sequence of the non-cloned side of the breakpoints. Comparison of 25, 600 bp-long breakpoint sequences demonstrated prevalence of repetitive elements. Consensus motives characteristic of the breakpoint sequences have been identified. Several sequences exhibit peculiar computed conformational characteristics, with sharp transition or center of symmetry located exactly at the breakpoint. Our data collectively suggest that chromatin fragmentation involves nucleolytic cleavages at fragile/hypersensitive sites delimiting loop-size fragments in a non-random manner. Interestingly, the sequence characteristics of the breakpoints are reminiscent of certain breakpoint cluster regions frequently subject to gene rearrangements.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk analysis Animals Base Sequence Biophysics Cells chemistry Chromatin Dna DNA Fragmentation DNA Nucleotidylexotransferase DNA Polymerase I Electrophoresis,Gel,Two-Dimensional Eukaryotic Cells HL-60 Cells Humans Hungary isolation and purification Jurkat Cells methods Mice Nih 3T3 Cells Prevalence Research Sequence Analysis,DNA Support egyetemen (Magyarországon) készült közlemény
Megjelenés:	Journal of Cellular Biochemistry. - 89 : 6 (2003), p. 1193-1205. -
További szerzők:	Varga Tamás (1971-) (biológus) Székvölgyi Lóránt (1977-) (biofizikus, biokémikus, sejtbiológus) Hegedűs Éva (1978-) (biofizikus) Goda Katalin (1969-) (biofizikus) Kaczur Viktória Bacsó Zsolt (1963-) (biofizikus) Nakayama, Yuji Pósafi János Pongor Sándor Szabó Gábor (1953-) (biofizikus)
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001-es BibID:	BIBFORM047042
035-os BibID:	PMID:15156565
Első szerző:	Tar Krisztina (biokémikus, molekuláris biológus)
Cím:	Phosphatase 2A is involved in endothelial cell microtubule remodeling and barrier regulation / Krisztina Tar, Anna A. Birukova, Csilla Csortos, Éva Bakó, Joe G. N. Garcia, Alexander D. Verin
Dátum:	2004
ISSN:	0730-2312
Megjegyzések:	We have recently shown that microtubule (MT) inhibitor, nocodazole (2-5 microM) significantly increases endothelial cells (EC) actomyosin contraction and permeability indicating the importance of MT in maintaining the EC barrier (Verin et al. [2001]: Cell Mol Physiol 281:L565-L574). Okadaic acid (OA, 2-5 nM), a powerful inhibitor of protein phosphatase 2A (PP2A), significantly potentiates the effect of submaximal concentrations of nocodazole (50-200 nM) on transendothelial electrical resistance (TER) suggesting the involvement of PP2A activity in the MT-mediated EC barrier regulation. Immunofluorescent staining of EC revealed that in control cells PP2A distributes in a pattern similar to MT. Consistent with these results, we demonstrated that significant amounts of PP2A were present in MT-enriched EC fractions indicating tight association of PP2A with MT in endothelium. Treatment of EC with OA leads to disappearance of MT-like PP2A staining suggesting dissociation of PP2A from the MT network. Next, we examined the effect of PP2A inhibition on phosphorylation status of MT-associated protein tau, which in its unphosphorylated form promotes MT assembly. OA caused significant increases in tau phosphorylation confirming that tau is a substrate for PP2A in endothelium. Immunofluorescent experiments demonstrated that the OA-induced increases in tau phosphorylation strongly correlated with translocation of phospho-tau to cell periphery and disassembly of peripheral MT. These results suggest the involvement of PP2A-mediated tau dephosphorylation in alteration of EC MT structure and highlight the potential importance of PP2A in the regulation of EC the MT cytoskeleton and barrier function.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Journal of Cellular Biochemistry. - 92 : 3 (2004), p. 534-546. -
További szerzők:	Birukova, Anna A. Csortos Csilla (1956-) (biokémikus) Bakó Éva (1958-) (biokémikus) Garcia, Joe G. N. Verin, Alexander
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001-es BibID:	BIBFORM003558
Első szerző:	Tar Krisztina (biokémikus, molekuláris biológus)
Cím:	Role of protein phosphatase 2A in the regulation of endothelial cell cytoskeleton structure / Krisztina Tar, Csilla Csortos, Istvan Czikora, Gabor Olah, Shwu-Fan Ma, Raj Wadgaonkar, Pal Gergely, Joe G. N. Garcia, Alexander D. Verin
Dátum:	2006
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban endothelium phosphatase 2A permeability microtubules microfilaments tau HSP27
Megjelenés:	Journal of Cellular Biochemistry. - 98 : 4 (2006), p. 931-953. -
További szerzők:	Csortos Csilla (1956-) (biokémikus) Czikora István (1979-) (vegyész, biokémikus) Oláh Gábor Ma, Shwu-Fan Wadgaonkar, Raj Gergely Pál (1947-) (biokémikus) Garcia, Joe G. N. Verin, Alexander
Internet cím:	elektronikus változat DOI
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