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001-es BibID:	BIBFORM003553
Első szerző:	Kakuk Annamária (molekuláris biológus)
Cím:	Nuclear and nucleolar localization signals and their targeting function in phosphatidylinositol 4-kinase PI4K230 / Kakuk A., Friedlander E., Vereb Gy. Jr., Lisboa, D., Bagossi P., Tóth G., Gergely P., Vereb Gy.
Dátum:	2008
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban phosphatidylinositol 4-kinase PI4K230 nuclear localization signal NLS nucleolar targeting NTS importins permeabilized HeLa cells import assay
Megjelenés:	Experimental Cell Research. - 314 : 13 (2008), p. 2376-2388. -
További szerzők:	Friedländer Elza (1980-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Lisboa, Duarte (1982-) (biotechnológus) Bagossi Péter (1966-2011) (biokémikus, vegyész) Tóth Gábor Gergely Pál (1947-) (biokémikus) Vereb György (1938-) (biokémikus, sejtbiológus)
Internet cím:	elektronikus változat DOI
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001-es BibID:	BIBFORM010361
035-os BibID:	(scopus)68849090496 (wos)000269333400005
Első szerző:	Roszik János (biofizikus)
Cím:	Evaluation of intensity-based ratiometric FRET in image cytometry-approaches and a software solution / Roszik, J., Lisboa, D., Szollosi, J., Vereb, G.
Dátum:	2009
ISSN:	1552-4922 (Print)
Megjegyzések:	The intensity-based ratiometric FRET (fluorescence resonance energy transfer) method is a powerful technique for following molecular interactions in living cells. Since it is not based on irreversibly destroying the donor or the acceptor fluorophores, the time course of changes in FRET efficiency values can be monitored by this method. ImageJ, a sophisticated software tool for many types of image processing allows users to extend it with programs for various purposes. Implementing intensity-based ratiometric FRET with ImageJ vastly enhances the applicability of the FRET method. We developed an efficient ImageJ plugin, RiFRET, which calculates FRET efficiency on a pixel-by-pixel basis from ratiometric FRET images. It allows the user to correct for channel cross-talk (bleed-through) and to calculate FRET from image stacks, i.e., from 3D data sets. Semiautomatic processing for larger datasets is also included in the program. Furthermore, several options for calibrating FRET efficiency calculations were tested and their applicability to various expression systems is discussed. Although the ratiometric FRET method is widely applied, our plugin is the first freely available software for evaluating such FRET data. The program is user friendly and provides reliable, standardized results.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Cells cytometry Energy Transfer Fluorescence Fluorescence Resonance Energy Transfer FRET Image Processing Software time
Megjelenés:	Cytometry. Part A. - 75A : 9 (2009), p. 761-767. -
További szerzők:	Lisboa, Duarte (1982-) (biotechnológus) Szöllősi János (1953-) (biofizikus) Vereb György (1965-) (biofizikus, orvos)
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM022510
Első szerző:	Váradi Tímea (okleveles vegyész)
Cím:	ErbB protein modifications are secondary to severe cell membrane alterations induced by elisidepsin treatment / Váradi T., Roszik J., Lisboa D., Vereb G., Molina-Guijarro J. M., Galmarini C. M., Szöllosi J., Nagy P.
Dátum:	2011
Megjegyzések:	Elisidepsin is a marine-derived anti-tumor agent with unique mechanism of action. It has been suggested to induce necrosis associated with severe membrane damage. Since indirect evidence points to the involvement of ErbB receptor tyrosine kinases and lipid rafts in the mechanism of action of elisidepsin, we investigated the effect of the drug on the distribution of ErbB proteins and systematically compared the elisidepsin sensitivity of cell lines overexpressing ErbB receptors. Stable expression of a single member of the ErbB family (ErbB1-3) or co-transfection of ErbB2 and ErbB3 did not modify the elisidepsin sensitivity of CHO and A431 cells. However, elisidepsin induced the redistribution of ErbB3 and two GPI-anchored proteins (transfected GPI-anchored eGFP and placental alkaline phosphatase) from the plasma membrane to intracellular vesicles without comparable effects on ErbB1 and ErbB2. Elisidepsin increased the binding of a conformational sensitive anti-ErbB3 antibody without modifying the binding of other ErbB2 or ErbB3 antibodies, and it decreased the homoassociation of both ErbB2 and ErbB3. We also found that elisidepsin decreased the fluorescence anisotropy of a membrane specific fluorescent probe and induced a blue shift in the emission spectrum of Laurdan pointing to significant changes in the order of the plasma membrane possibly associated with the formation of liquid ordered domains. Although the distribution of ErbB proteins is preferentially altered by elisidepsin, our data question their role in determining sensitivity to the drug. We assume that induction of liquid ordered domains is the primary action of elisidepsin leading to all the other observed changes.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Elisidepsin ErbB proteins Liquid ordered domain FRET
Megjelenés:	European Journal of Pharmacology 667 : 1-3 (2011), p. 91-99. -
További szerzők:	Roszik János (1979-) (biofizikus) Lisboa, Duarte (1982-) (biotechnológus) Vereb György (1965-) (biofizikus, orvos) Molina-Guijarro, J. M. Galmarini, Carlos M. Szöllősi János (1953-) (biofizikus) Nagy Péter (1971-) (biofizikus)
Internet cím:	Szerző által megadott URL Intézményi repozitóriumban (DEA) tárolt változat DOI
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