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001-es BibID:	BIBFORM075134
035-os BibID:	(WoS)000444060600014 (Scopus)85052296237
Első szerző:	Bene László (biofizikus)
Cím:	Dual-Laser Tetra-Polarization FRET (4polFRET) for Site-Selective Control of Homo-FRET in Hetero-FRET Systems on the Cell Surface : the Homo-FRET Gate / Bene L., Bagdány M., Ungvári T., Damjanovich L.
Dátum:	2018
ISSN:	0003-2700
Megjegyzések:	The effects of donor homo-Förster resonance energy transfer (homo-FRET) taking place in hetero-FRET systems is described in the context of hetero-FRET detection via donor and acceptor fluorescence anisotropies in cell surface receptor clusters. Donor homo-FRET can influence both the efficiency of detection as well as the magnitude of the detectable hetero-FRET. A 4-fold polarized FRET detection scheme-tetrapolarization FRET (4polFRET)-is proposed not only for discriminating the effects of homo-FRET from those of hetero-FRET, but also for correlating homo-associations of the donors and acceptors at different donor-acceptor distances, even beyond the critical Förster distance for hetero-FRET ( R0). The method is based on suppressing homo-FRET at the donor side with red-edge excitation. After the anisotropy effects of physical rotation and homo-FRET were separated by site-selective spectroscopy, the magnitude of the effect of homo-FRET on hetero-FRET has been estimated. It has been found significant, offering a new sensitive technique for detecting conformational dynamics via the homo-FRET mediated component of hetero-FRET, the "homo-FRET enhanced hetero-FRET" or "homo-FRET gate". The method is realizable in flow, as well as in image cytometry equipped with polarization detecting facility.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk four-fold fluorescence anisotropy correlations dual-hetero-FRET dual-homo-FRET homo-FRET-sensitized hetero-FRET donor fluorescence anisotropy acceptor fluorescence anisotropy
Megjelenés:	Analytical Chemistry. - 90 : 17 (2018), p. 10159-10170. -
További szerzők:	Bagdány Miklós Ungvári Tamás Damjanovich László (1960-) (általános sebész)
Pályázati támogatás:	TÁMOP-4.2.2.A-11/1/KONV-2012-0045 TÁMOP Sebészet Kutatócsoport
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM083089
035-os BibID:	(WoS)000509420400074 (Scopus)85078380578
Első szerző:	Rehó Bálint
Cím:	Simultaneous Mapping of Molecular Proximity and Comobility Reveals Agonist-Enhanced Dimerization and DNA Binding of Nuclear Receptors / Rehó Bálint, Lau Lukas, Mocsár Gábor, Müller Gabriele, Fadel Lina, Brázda Péter, Nagy László, Tóth Katalin, Vámosi György
Dátum:	2020
ISSN:	0003-2700
Megjegyzések:	Single Plane Illumination Microscopy (SPIM) revolutionized time lapse imaging of live cells and organisms due to its high speed and reduced photodamage. Quantitative mapping of molecular (co)mobility by fluorescence (cross-) correlation spectroscopy (F(C)CS) in a SPIM has been introduced to reveal molecular diffusion and binding. A complementary aspect of interactions is proximity, which can be studied by Fo?rster resonance energy transfer (FRET). Here, we extend SPIM-FCCS by alternating laser excitation, which reduces false positive cross-correlation and facilitates comapping of FRET. Thus, different aspects of interacting systems can be studied simultaneously, and molecular subpopulations can be discriminated by multiparameter analysis. After demonstrating the benefits of the method on the AP-1 transcription factor, the dimerization and DNA binding behavior of retinoic acid receptor (RAR) and retinoid X receptor (RXR) is revealed, and an extension of the molecular switch model of the nuclear receptor action is proposed. Our data imply that RAR agonist enhances RAR?RXR heterodimerization, and chromatin binding/dimerization are positively correlated. We also propose a ligand induced conformational change bringing the N-termini of RAR and RXR closer together. The RXR agonist increased homodimerization of RXR suggesting that RXR may act as an autonomous transcription factor.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Analytical Chemistry. - 92 : 2 (2020), p. 2207-2215. -
További szerzők:	Lau, Lukas Mocsár Gábor (1981-) (biofizikus) Müller, Gabriele Fadel, Lina (1988-) (gyógyszerész) Brázda Péter (1980-) (biológus, angol-magyar szakfordító) Nagy László (1966-) (molekuláris sejtbiológus, biokémikus) Tóth Katalin (biofizikus) Vámosi György (1967-) (biofizikus)
Pályázati támogatás:	GINOP-2.3.2-15-2016-00026 GINOP GINOP-2.3.3-15-2016-00030 GINOP NN129371 from the National Research, Development, and Innovation Office, Hungary Egyéb German Academic Exchange Service Egyéb Tempus Public Foundation 273478 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM043016
035-os BibID:	PMID:22797718
Első szerző:	Shrestha, Dilip (biológus)
Cím:	Comparative study of the three different fluorophore antibody conjugation strategies / Dilip Shrestha, Adrienn Bagosi, János Szöllősi, Attila Jenei
Dátum:	2012
Megjegyzések:	The progression in bioconjugational chemistry has significantly contributed to the evolution and success of protein biology. Mainly, antibody chemistry has been a subject of intensive study owing to the expansion of research areas warranted by using various derivatives of conjugated antibodies. Three reactive moieties (amine, sulfhydryl and carbohydrate) in the antibodies are chiefly favored for the conjugational purpose. This feature is known for decades, nevertheless, amine based conjugation is still the most preferred strategy despite the appreciation the other two methods receive in conserving the antigen binding affinity (ABA). No single report has been published, according to our knowledge, where these three conjugation strategies were applied to the same fluorophore antibody systems. In this study, we evaluated conjugation yield, time demand and cost efficiency of these conjugation procedures. Our results showed that amine based conjugations was by far the best technique due to its simplicity, rapidity, ease of operation, higher conjugate yield, cheaper cost and potential for larger fluorophore/protein labeling ratio without having much effect in ABA. Furthermore, sulfhydryl labeling clearly excelled in terms of reduced non-specific binding and mild effect in ABA but was usually complicated by an asymmetric antibody reduction due to mercaptoethylamine while carbohydrate oxidation based strategy performed the worst during our experiment
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Antibodies Antibody conjugation article binding affinity Biophysics cell biology chemistry Comparative Study Hungary methods Research Research Support Support time egyetemen (Magyarországon) készült közlemény
Megjelenés:	Analytical and Bioanalytical Chemistry - 404 : 5 (2012), p. 1449-1463. -
További szerzők:	Bagosi Adrienn Szöllősi János (1953-) (biofizikus) Jenei Attila (1966-) (biofizikus)
Pályázati támogatás:	TÁMOP-4.2.2-08/1-2008-0019 TÁMOP TÁMOP-4.2.1/B-09/1/KONV-2010-007 TÁMOP TÁMOP-4.2.2/B-10/ 1-2010-0024 TÁMOP
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM085978
035-os BibID:	(WoS)000467642100121 (Scopus)85065467554
Első szerző:	Szendi-Szatmári Tímea (molekuláris biológus)
Cím:	Reducing the Detrimental Effects of Saturation Phenomena in FRET Microscopy / Szendi-Szatmári Tímea, Szabó Ágnes, Szöllősi János, Nagy Peter
Dátum:	2019
ISSN:	0003-2700
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Analytical Chemistry. - 91 : 9 (2019), p. 6378-6382. -
További szerzők:	Nagyné Szabó Ágnes Timea (1982-) (vegyész) Szöllősi János (1953-) (biofizikus) Nagy Péter (1971-) (biofizikus)
Pályázati támogatás:	K120302 OTKA GINOP-2.3.2-15-2016-00020 GINOP GINOP-2.3.2-15-2016-00044 GINOP
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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