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001-es BibID:	BIBFORM004856
Első szerző:	Bagossi Péter (biokémikus, vegyész)
Cím:	Molecular modeling of nearly full-length ErbB2 receptor / Bagossi, P., Horvath, G., Vereb, G., Szollosi, J., Tozser, J.
Dátum:	2005
ISSN:	0006-3495
Megjegyzések:	Members of the epidermal growth factor receptor family play important roles in various cellular processes, both in physiological and in pathological conditions. Dimerization and autophosphorylation of these receptor tyrosine kinases are key events of signal transduction. Details of the molecular events of the signaling are not entirely known. To facilitate the understanding of receptor structure and function at the molecular level, a molecular model was built for the nearly full-length ErbB2 dimer. Modeling was based on the x-ray or nuclear-magnetic resonance structures of extracellular, transmembrane, and intracellular domains. The extracellular domain was positioned above the cell membrane based on the distance determined from experimentally measured fluorescence resonance energy transfer. Favorable dimerization interactions are predicted for the extracellular, transmembrane, and protein kinase domains in the model of a nearly full-length dimer of ErbB2, which may act in a coordinated fashion in ErbB2 homodimerization, and also in heterodimers of ErbB2 with other members of the ErbB family
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban analysis Cell Line, Tumor Cell Membrane chemistry Comparative Study Computer Simulation Dimerization Energy Transfer Epidermal Growth Factor Fluorescence Fluorescence Resonance Energy Transfer Humans Hungary Lipid Bilayers methods Models, Chemical Models, Molecular Neoplasms Protein Conformation Protein Structure, Tertiary Receptor, erbB-2 Research Signal Transduction Structure-Activity Relationship Support ultrastructure
Megjelenés:	Biophysical Journal. - 88 : 2 (2005), p. 1354-1363. -
További szerzők:	Horváth Gábor (1974-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Szöllősi János (1953-) (biofizikus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
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001-es BibID:	BIBFORM004943
Első szerző:	Gadella, Theodorus W. Jr.
Cím:	Microspectroscopic imaging of nodulation factor-binding sites on living Vicia sativa roots using a novel bioactive fluorescent nodulation factor / Gadella, T. W. Jr., Vereb, G. Jr., Hadri, A. E., Rohrig, H., Schmidt, J., John, M., Schell, J., Bisseling, T.
Dátum:	1997
Megjegyzések:	A novel bioactive fluorescent nodulation (Nod) factor, NodRlv-IV(BODIPY FL-C16), has been synthesized by attaching a BODIPY FL-C16 acyl chain to the primary amino group of chitotetraose deacetylated at the nonreducing terminus by recombinant NodB. The binding of the fluorescent Nod factor to root systems of Vicia sativa was investigated with fluorescence spectral imaging microscopy (FSPIM) and fluorescence ratio imaging microscopy (FRIM). Spatially resolved fluorescence spectra of living and labeled Vicia sativa root systems were measured by FSPIM. Strong autofluorescence, inherent to many plant systems when excited at 488 nm, was corrected for by utilizing the difference in fluorescence emission spectra of the autofluorescence and NodRlv- IV(BODIPY FL-C16). A methodology is presented to break down the in situ fluorescence emission spectra into spatially resolved autofluorescence and BODIPY FL fluorescence spectra. Furthermore, an FRIM method was developed for correcting autofluorescence in fluorescence micrographs for this system. After autofluorescence correction it was shown that NodRlv-IV(BODIPY FL-C16) was concentrated in the root hairs, but was also bound to other parts of the root surface.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Binding Sites chemistry Fluorescence methods Microscopy Non-U.S.Gov't Plant Proteins Spectrometry Support
Megjelenés:	Biophysical Journal 72 : 5 (1997), p. 1986-1996. -
További szerzők:	Vereb György (1965-) (biofizikus, orvos) Hadri, Azz-Eddine Röhrig, Horst Schmidt, Jürgen John, Michael Schell, Jeff Bisseling, Ton
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001-es BibID:	BIBFORM072316
035-os BibID:	(WoS)000425895600022 (Scopus)85041571964
Első szerző:	Nagyné Szabó Ágnes Timea (vegyész)
Cím:	The Effect of Fluorophore Conjugation on Antibody Affinity and the Photophysical Properties of Dyes / Szabó Ágnes, Szendi-Szatmári Tímea, Ujlaky-Nagy László, Rádi Ildikó, Vereb György, Szöllősi János, Nagy Peter
Dátum:	2018
ISSN:	0006-3495
Megjegyzések:	Because the degree of labeling (DOL) of cell-bound antibodies, often required in quantitative fluorescence measurements, is largely unknown, we investigated the effect of labeling with two different fluorophores (AlexaFluor546, AlexaFluor647) in a systematic way using antibody stock solutions with different DOLs. Here, we show that the mean DOL of the cell-bound antibody fraction is lower than that of the stock using single molecule fluorescence measurements. The effect is so pronounced that the mean DOL levels off at approximately two fluorophores/IgG for some antibodies. We developed a method for comparing the average DOL of antibody stocks to that of the isolated, cell-bound fraction based on fluorescence anisotropy measurements confirming the aforementioned conclusions. We created a model in which individual antibody species with different DOLs, present in an antibody stock solution, were assumed to have distinct affinities and quantum yields. The model calculations confirmed that a calibration curve constructed from the anisotropy of antibody stocks can be used for determining the DOL of the bound fraction. The fluorescence intensity of the cell-bound antibody fractions and of the antibody stocks exhibited distinctly different dependence on the DOL. The behavior of the two dyes was systematically different in this respect. Fitting of the model to these data revealed that labeling with each dye affects quantum yield and antibody affinity differentially. These measurements also implied that fluorophores in multiply labeled antibodies exhibit self-quenching and lead to decreased antibody affinity, conclusions directly confirmed by steady-state intensity measurements and competitive binding assays. Although the fluorescence lifetime of antibodies labeled with multiple fluorophores decreased, the magnitude of this change was not sufficient to account for self-quenching indicating that both dynamic and static quenching processes occur involving H-aggregate formation. Our results reveal multiple effects of fluorophore conjugation, which must not be overlooked in quantitative cell biological measurements.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Biophysical Journal. - 114 : 3 (2018), p. 688-700. -
További szerzők:	Szendi-Szatmári Tímea (1989-) (molekuláris biológus) Ujlaky-Nagy László (1977-) (biofizikus) Rádi Ildikó Vereb György (1965-) (biofizikus, orvos) Szöllősi János (1953-) (biofizikus) Nagy Péter (1971-) (biofizikus)
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001-es BibID:	BIBFORM004642
Első szerző:	Vereb György (biofizikus, orvos)
Cím:	Temporally and spectrally resolved imaging microscopy of lanthanide chelates / Vereb, G., Jares-Erijman, E. A., Selvin, P. R., Jovin, T. M.
Dátum:	1998
ISSN:	006-3495
Megjegyzések:	The combination of temporal and spectral resolution in fluorescence microscopy based on long-lived luminescent labels offers a dramatic increase in contrast and probe selectivity due to the suppression of scattered light and short-lived autofluorescence. We describe various configurations of a fluorescence microscope integrating spectral and microsecond temporal resolution with conventional digital imaging based on CCD cameras. The high-power, broad spectral distribution and microsecond time resolution provided by microsecond xenon flashlamps offers increased luminosity with recently developed fluorophores with lifetimes in the submicrosecond to microsecond range. On the detection side, a gated microchannel plate intensifier provides the required time resolution and amplification of the signal. Spectral resolution is achieved with a dual grating stigmatic spectrograph and has been applied to the analysis of luminescent markers of cytochemical specimens in situ and of very small volume elements in microchambers. The additional introduction of polarization optics enables the determination of emission polarization; this parameter reflects molecular orientation and rotational mobility and, consequently, the nature of the microenvironment. The dual spectral and temporal resolution modes of acquisition complemented by a posteriori image analysis gated on the spatial, spectral, and temporal dimensions lead to a very flexible and versatile tool. We have used a newly developed lanthanide chelate, Eu-DTPA-cs124, to demonstrate these capabilities. Such compounds are good labels for time-resolved imaging microscopy and for the estimation of molecular proximity in the microscope by fluorescence (luminescence) resonance energy transfer and of molecular rotation via fluorescence depolarization. We describe the spectral distribution, polarization states, and excited-state lifetimes of the lanthanide chelate crystals imaged in the microscope
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban analogs and derivatives analysis Chelating Agents chemistry Crystallization Energy Transfer Equipment Design Fluorescence instrumentation Light Luminescence Metals methods Microscopy Microscopy,Video Models,Molecular Molecular Conformation Organometallic Compounds Pentetic Acid Rotation Support,Non-U.S.Gov't Support,U.S.Gov't,P.H.S. Time Factors
Megjelenés:	Biophysical Journal 74 : 5 (1998), p. 2210-2222. -
További szerzők:	Jares-Erijman, Elizabeth A. Selvin, Paul R. Jovin, Thomas M.
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