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1.

001-es BibID:BIBFORM055851
035-os BibID:(scopus)84949232854
Első szerző:Doan-Xuan, Quang-Minh (biofizikus)
Cím:FRET Imaging by Laser Scanning Cytometry on Large Populations of Adherent Cells / Quang-Minh Doan-Xuan, Nikoletta Szalóki, Katalin Tóth, János Szöllősi, Zsolt Bacso, György Vámosi
Dátum:2014
ISSN:1934-9297 1934-9300
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Current Protocols in Cytometry. - Suppl. 70. (2014), p. [1-29]. -
További szerzők:Szalóki Nikoletta (1981-) (biológus) Tóth Katalin (biofizikus) Szöllősi János (1953-) (biofizikus) Bacsó Zsolt (1963-) (biofizikus) Vámosi György (1967-) (biofizikus)
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM050042
035-os BibID:PMID:23504771
Első szerző:Fábián Ákos István (aneszteziológus)
Cím:TripleFRET measurements in flow cytometry / Ákos Fábián, Gábor Horváth, György Vámosi, György Vereb, János Szöllősi
Dátum:2013
Megjegyzések:A frequently used method for viewing protein interactions and conformation, Forster (fluorescence) resonance energy transfer (FRET), has traditionally been restricted to two fluorophores. Lately, several methods have been introduced to expand FRET methods to three species. We present a method that allows the determination of FRET efficiency in three-dye systems on a flow cytometer. TripleFRET accurately reproduces energy transfer efficiency values measured in two-dye systems, and it can indicate the presence of trimeric complexes, which is not possible with conventional FRET methods. We also discuss the interpretation of energy transfer values obtained with tripleFRET in relation to spatial distribution of labeled molecules, specifically addressing the limitations of using total energy transfer to determine molecular distance
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Antibodies
Antibodies,Monoclonal,Humanized
article
Biophysics
cell biology
Cell Line
chemistry
cytometry
Dyes
Energy Transfer
ENERGY-TRANSFER
FLOW
Flow Cytometry
Fluorescence
Fluorescence Resonance Energy Transfer
fluorescent dye
Fluorescent Dyes
FRET
Humans
Hungary
Immunoconjugates
immunology
methods
Protein Binding
PROTEIN INTERACTIONS
Research
Research Support
resonance energy transfer
Staining and Labeling
statistics & numerical data
Support
Megjelenés:Cytometry Part A. - 83 : 4 (2013), p. 375-385. -
További szerzők:Horváth Gábor (1974-) (biofizikus) Vámosi György (1967-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Szöllősi János (1953-) (biofizikus)
Pályázati támogatás:NK 101337
OTKA
K75752
OTKA
TÁMOP-4.2.2-08/1-2008-0019
TÁMOP
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Receptor tirozin kinázok mint terápiás célpontok : működésük szabályozásának, és a közöttük fellépő molekuláris kölcsönhatások vizsgálata
TÁMOP-4.2.2.A-11/1/KONV-2012-0025
TÁMOP
Baross Gábor Program REG_EA_09-1-2009-0010
Egyéb
K77600
OTKA
K103965
OTKA
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

3.

001-es BibID:BIBFORM005182
Első szerző:Gombos Imre
Cím:Some new faces of membrane microdomains : a complex confocal fluorescence, differential polarization, and FCS imaging study on live immune cells / Gombos, I., Steinbach, G., Pomozi, I., Balogh, A., Vamosi, G., Gansen, A., Laszlo, G., Garab, G., Matko, J.
Dátum:2008
ISSN:552-4930 (Electronic)
Megjegyzések:Lipid rafts are cholesterol- and glycosphingolipid-rich plasma membrane microdomains, which control signal transduction, cellular contacts, pathogen recognition, and internalization processes. Their stability/lifetime, heterogeneity remained still controversial, mostly due to the high diversity of raft markers and cellular models. The correspondence of the rafts of living cells to liquid ordered (Lo) domains of model membranes and the effect of modulating rafts on the structural dynamics of their bulk membrane environment are also yet unresolved questions. Spatial overlap of various lipid and protein raft markers on live cells was studied by confocal laser scanning microscopy, while fluorescence polarization of DiIC18(3) and Bodipy-phosphatidylcholine was imaged with differential polarization CLSM (DP-CLSM). Mobility of the diI probe under different conditions was assessed by fluorescence correlation spectroscopic (FCS). GM1 gangliosides highly colocalized with GPI-linked protein markers of rafts and a new anti-cholesterol antibody (AC8) in various immune cells. On the same cells, albeit not fully excluded from rafts, diI colocalized much less with raft markers of both lipid and protein nature, suggesting the Lo membrane regions are not equivalents to lipid rafts. The DP-CLSM technique was capable of imaging probe orientation and heterogeneity of polarization in the plasma membrane of live cells, reflecting differences in lipid order/packing. This property--in accordance with diI mobility assessed by FCS--was sensitive to modulation of rafts either through their lipids or proteins. Our complex imaging analysis demonstrated that two lipid probes--G(M1) and a new anti-cholesterol antibody--equivocally label the membrane rafts on a variety of cell types, while some raft-associated proteins (MHC-II, CD48, CD59, or CD90) do not colocalize with each other. This indicates the compositional heterogeneity of rafts. Usefulness of the DP-CLSM technique in imaging immune cell surface, in terms of lipid order/packing heterogeneities, was also shown together with its sensitivity to monitor biological modulation of lipid rafts.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Animals
Antibodies
article
Cell Line,Tumor
Cells
Cells,Cultured
chemistry
Cholesterol
Comparative Study
Confocal
Fluorescence
Fluorescence Polarization
Humans
Hungary
immunology
Lipids
Membrane Microdomains
methods
Mice
Mice, Inbred BALB C
Mice, Inbred C3H
Microscopy
Microscopy, Confocal
Microscopy, Fluorescence
Microscopy, Polarization
Proteins
Rats
Rats, Sprague-Dawley
Research
Research Support
Signal Transduction
Spectrometry, Fluorescence
Support
Megjelenés:Cytometry. Part A. - 73 : 3 (2008), p. 220-229. -
További szerzők:Steinbach Gábor Pomozi István Balogh Andrea Vámosi György (1967-) (biofizikus) Gansen, Alexander László Glória Garab Győző Matkó János (1952-) (biológus)
Internet cím:DOI
elektronikus változat
Borító:

4.

001-es BibID:BIBFORM076128
035-os BibID:(Wos)000450299400006 (Scopus)85055751019
Első szerző:Nizsalóczki Enikő
Cím:Minimum degree of overlap between IL-9R and IL-2R on human T lymphoma cells : a quantitative CLSM and FRET analysis / Nizsalóczki Enikő, Nagy Péter, Mocsár Gábor, Szabó Ágnes, Csomós István, Waldmann Thomas A., Vámosi György, Mátyus László, Bodnár Andrea
Dátum:2018
ISSN:1552-4922 1552-4930
Megjegyzések:The heterodimeric receptor complex of IL-9 consists of the cytokine-speci?c ?-subunit and the common ? -chain shared with other cytokines, including IL-2, a central regulator of T cell function. We have shown previously the bipartite spatial relationship of IL-9 and IL-2 receptors at the surface of human T lymphoma cells: in addition to common clusters, expression of the two receptor kinds could also be observed in segregated membrane areas. Here we analyzed further the mutual cell surface organization of IL-9 and IL-2 receptors. Complementing Pearson correlation data with co-occurrence analysis of confocal microscopic images revealed that a minimum degree of IL-9R/IL-2R co-localization exists at the cell surface regardless of the overall spatial correlation of the two receptor kinds. Moreover, our FRET experiments demonstrated molecular scale assemblies of the elements of the IL-9/IL-2R system. Binding of IL-9 altered the structure and/or composition of these clusters. It is hypothesized, that by sequestering receptor subunits in common membrane areas, the overlapping domains of IL-9R and IL-2R provide a platform enabling both the formation of the appropriate receptor complex as well as subunit sharing between related cytokines.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
IL-9 and -2 receptors
uorescence resonance energy transfer
Manders coef-cient
co-occurrence analysis
Pearson correlation analysis
confocal microscopy
human T lymphoma cells
co-localization of membrane proteins
Megjelenés:Cytometry Part A. - 93 : 11 (2018), p. 1106-1117. -
További szerzők:Nagy Péter (1971-) (biofizikus) Mocsár Gábor (1981-) (biofizikus) Nagyné Szabó Ágnes Timea (1982-) (vegyész) Csomós István (1983-) (molekuláris biológus) Waldmann, Thomas A. Vámosi György (1967-) (biofizikus) Mátyus László (1956-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus)
Pályázati támogatás:EFOP-3.6.3-VEKOP-16-2017-00009
EFOP
GINOP-2.3.2-15-2016-00026
GINOP
GINOP-2.3.3-15-2016-00003
GINOP
K120302
OTKA
Intramural research program of the National Cancer Institute, NIH
Egyéb
Internet cím:Szerző által megadott URL
DOI
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5.

001-es BibID:BIBFORM039658
035-os BibID:(scopus)0036628631 (wos)000176656500002
Első szerző:Sebestyén Zsolt
Cím:Long wavelength fluorophores and cell-by-cell correction for autofluorescence significantly improves the accuracy of flow cytometric energy transfer measurements on a dual-laser benchtop flow cytometer / Zsolt Sebestyén, Péter Nagy, Gábor Horváth, György Vámosi, Reno Debets, Jan W. Gratama, Denis R. Alexander, János Szöllősi
Dátum:2002
ISSN:0196-4763
Megjegyzések:Flow cytometric fluorescence resonance energy transfer (FCET) is an efficient method to map associations between biomolecules because of its high sensitivity to changes in molecular distances in the range of 1-10 nm. However, the requirement for a dual-laser instrument and the need for a relatively high signal-to-noise system (i.e., high expression level of the molecules) pose limitations to a wide application of the method.METHODS:Antibodies conjugated to cyanines 3 and 5 (Cy3 and Cy5) were used to label membrane proteins on the cell surface. FCET measurements were made on a widely used benchtop dual-laser flow cytometer, the FACSCalibur, by using cell-by-cell analysis of energy transfer efficiency.ResultsTo increase the accuracy of FCET measurements, we applied a long wavelength donor-acceptor pair, Cy3 and Cy5, which beneficially affected the signal-to-noise ratio in comparison with the classic pair of fluorescein and rhodamine. A new algorithm for cell-by-cell correction of autofluorescence further improved the sensitivity of the technique; cell subpopulations with only slightly different FCET efficiencies could be identified. The new FCET technique was tested on various direct and indirect immunofluorescent labeling strategies. The highest FCET values could be measured when applying direct labeling on both (donor and acceptor) sides. Upon increasing the complexity of the labeling scheme by introducing secondary antibodies, we detected a decrease in the energy transfer efficiency.CONCLUSIONS:We developed a new FCET protocol by applying long wavelength excitation and detection of fluorescence and by refining autofluorescence correction. The increased accuracy of the new method makes cells with low receptor expression amenable to FCET investigation, and the new approach can be implemented easily on a commercially available dual-laser flow cytometer, such as a FACSCalibur.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Algorithms
analysis
Antibodies
Biophysics
Calibration
Cell Line, Transformed
Cells
Comparative Study
Dyes
Energy Transfer
Flow Cytometry
Fluorescein
Fluorescence
Fluorescence Resonance Energy Transfer
Fluorescent Dyes
Humans
Hungary
instrumentation
Lasers
Membrane Proteins
methods
Proteins
Reproducibility of Results
Research
Spectrometry, Fluorescence
Subtraction Technique
Support
Tumor Cells, Cultured
egyetemen (Magyarországon) készült közlemény
Megjelenés:Cytometry. - 48 : 3 (2002), p. 124-135. -
További szerzők:Nagy Péter (1971-) (biofizikus) Horváth Gábor (1974-) (biofizikus) Vámosi György (1967-) (biofizikus) Debets, Reno Gratama, Jan Willem Alexander, Denis R. Szöllősi János (1953-) (biofizikus)
Internet cím:Szerző által megadott URL
DOI
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6.

001-es BibID:BIBFORM050053
Első szerző:Szalóki Nikoletta (biológus)
Cím:High throughput FRET analysis of protein-protein interactions by slide-based imaging laser scanning cytometry / Nikoletta Szalóki, Quang Minh Doan-Xuan, János Szöllősi, Katalin Tóth, György Vámosi, Zsolt Bacsó
Dátum:2013
Megjegyzések:Laser scanning cytometry (LSC) is a slide-based technique combining advantages of flow and image cytometry: automated, high-throughput detection of optical signals with subcellular resolution. Fluorescence resonance energy transfer (FRET) is a spectroscopic method often used for studying molecular interactions and molecular distances. FRET has been measured by various microscopic and flow cytometric techniques. We have developed a protocol for a commercial LSC instrument to measure FRET on a cell-by-cell or pixel-by-pixel basis on large cell populations, which adds a new modality to the use of LSC. As a reference sample for FRET, we used a fusion protein of a single donor and acceptor (ECFP-EYFP connected by a seven-amino acid linker) expressed in HeLa cells. The FRET efficiency of this sample was determined via acceptor photobleaching and used as a reference value for ratiometric FRET measurements. Using this standard allowed the precise determination of an important parameter (the alpha factor, characterizing the relative signal strengths from a single donor and acceptor molecule), which is indispensable for quantitative FRET calculations in real samples expressing donor and acceptor molecules at variable ratios. We worked out a protocol for the identification of adherent, healthy, double-positive cells based on light-loss and fluorescence parameters, and applied ratiometric FRET equations to calculate FRET efficiencies in a semi-automated fashion. To test our protocol, we measured the FRET efficiency between Fos-ECFP and Jun-EYFP transcription factors by LSC, as well as by confocal microscopy and flow cytometry, all yielding nearly identical results. Our procedure allows for accurate FRET measurements and can be applied to the fast screening of protein interactions. A pipeline exemplifying the gating and FRET analysis procedure using the CellProfiler software has been made accessible at our web site
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Acceptor molecules
analysis
article
Biophysics
cell biology
Cells
Confocal
Confocal microscopy
cytometry
Energy Transfer
ENERGY-TRANSFER
FLOW
Flow Cytometry
Fluorescence
FLUORESCENCE RESONANCE
Fluorescence Resonance Energy Transfer
FRET
Hela Cells
Hungary
Image Cytometry
Laser Scanning Cytometry
Microscopy
molecular interaction
MOLECULAR-INTERACTIONS
Photobleaching
PROTEIN INTERACTIONS
protein protein interaction
Protein-protein interactions
Research
Research Support
resonance energy transfer
Software
Support
Megjelenés:Cytometry. Part A. - 83 : 9 (2013), p. 818-829. -
További szerzők:Doan-Xuan, Quang-Minh (1986-) (biofizikus) Szöllősi János (1953-) (biofizikus) Tóth Katalin (biofizikus) Vámosi György (1967-) (biofizikus) Bacsó Zsolt (1963-) (biofizikus)
Pályázati támogatás:K 77600
OTKA
K 103965
OTKA
NK 101337
OTKA
K 75752
OTKA
CK78179
OTKA
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
TÁMOP-4.2.2.A-11/1/KONV-2012-0023-"VÉD-ELEM"
TÁMOP
TÁMOP-4.2.2.A-11/1/KONV-2012-0025
TÁMOP
Internet cím:DOI
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7.

001-es BibID:BIBFORM004640
Első szerző:Szűcs Sándor (biokémikus, vegyész)
Cím:Single-cell measurement of superoxide anion and hydrogen peroxide production by human neutrophils with digital imaging fluorescence microscopy / Sándor Szűcs, György Vámosi, Róbert Póka, Attila Sárváry, Helga Bárdos, Margit Balázs, János Kappelmayer, László Tóth, János Szöllősi, Róza Ádány
Dátum:1998
ISSN:0196-4763
Megjegyzések:Besides flow cytometry, fluorescence microscopy combined with computerized image analysis offers an alternative tool for assessing phagocyte oxidant generation at the single-cell level. This technique provides an opportunity for the direct visualization of cells and simultaneous measurement of cellular fluorescence intensity. Thus, we developed a simple method for the quantitative evaluation of intracellular superoxide anion and hydrogen peroxide production with image cytometry by using hydroethidine and dihydrorhodamine 123 dyes, respectively. Human neutrophils stimulated with phorbol dibutyrate and labeled by these fluorogenic substrates showed intense, well recognizable red or green fluorescence. The intensity of signals from individual granulocytes of cytospin preparations were quantitatively measured in digitized images. There was a great heterogeneity in response to the stimulus within the granulocyte population as shown by the integrated fluorescence intensity values. In agreement with the results of parallel flow cytometric experiments, this simple image analysis performed on cells of cytospin preparations was able to detect the defects in the oxidative metabolism of neutrophils from patients with cervix carcinoma. We demonstrated that even minor alterations in superoxide anion/hydrogen peroxide generation can be detected by image cytometry as efficiently as by flow cytometry. This result validates imaging microscopy as an alternative to flow cytometry in such experiments. In addition, the image cytometric technique allows the observation of the kinetics of free radical production in individual cell under adherent conditions. Therefore, we carried out image analysis of the oxidative burst of neutrophils adherent to uncoated glass and fibronectin- and type IV collagen-coated surfaces in response to stimulation with phorbol dibutyrate or N-formyl-methionyl-leucyl-phenylalanine. We elaborated a calibration technique for the quantitative measurement of the ethidium bromide generation mediated by superoxide anion within individual adherent granulocytes. The ethidium bromide production varied between 0.48 and 1.17 amol/cell/min.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Anions
Carcinoma
Dyes
epidemiology
Ethidium
Flow Cytometry
Fluorescence
Human
Hungary
Hydrogen Peroxide
Image Cytometry
Image Processing
Computer-Assisted
Kinetics
metabolism
methods
Microscopy
Microscopy
Fluorescence
Neutrophils
Superoxides
Support
Non-U.S.Gov't
egyetemen (Magyarországon) készült közlemény
Megjelenés:Cytometry. - 33 : 1 (1998), p. 19-31. -
További szerzők:Vámosi György (1967-) (biofizikus) Póka Róbert (1960-) (szülész-nőgyógyász, klinikai onkológus) Sárváry Attila (1971-) (népegészségtan szakorvos) Bárdos Helga (1969-) (megelőző orvostan és népegészségtan szakorvos) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Kappelmayer János (1960-) (laboratóriumi szakorvos) Tóth László (orvos) Szöllősi János (1953-) (biofizikus) Ádány Róza (1952-) (megelőző orvostan és népegészségtan szakorvos)
Internet cím:DOI
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Borító:

8.

001-es BibID:BIBFORM075132
035-os BibID:(WoS)000430916400003 (Scopus)85045892766
Első szerző:Vámosi György (biofizikus)
Cím:Turning Noise into Order on the Cell Surface : resonant Activation of Molecular Highlighters / György Vámosi, László Damjanovich, László Bene
Dátum:2018
ISSN:1552-4922 1552-4930
Megjegyzések:MOLECULAR biology has been revolutionized by the discoveryof a new family of fluorophores termed fluorescent proteins(FPs). The value of this kind of fluorophores rests in thepossibility to genetically attach it to virtually all kinds of proteinsand detect it relatively easily via fluorescence spectroscopynot interfering with life processes (1,2). Besides the moreconventional, simple type of FPs with fixed absorption andemission characteristics?that is, with constant absorptionand emission wavelength ranges, and constant absorptioncoefficient and quantum efficiency?there are also those whosephotophysical properties can be modulated by light. This FPsubfamily is called molecular highlighters.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
photoactivation
fluorescent protein
single molecule counting
super-resolution microscopy
light induced rotation
FRETforce
Megjelenés:Cytometry Part A. - 93A (2018), p. 397-401. -
További szerzők:Damjanovich László (1960-) (általános sebész) Bene László (1963-) (biofizikus)
Pályázati támogatás:TÁMOP-4.2.2.A-11/1/KONV-2012-0045
TÁMOP
Sebészet Kutatócsoport
GINOP-2.3.2-15-2016-00026
GINOP
GINOP-2.3.3-15-2016-00003
GINOP
K103965
OTKA
TAMOP-4.2.4.A/2-11/1-2012-0001
TÁMOP
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

9.

001-es BibID:BIBFORM003899
035-os BibID:(scopus)48849084338 (wos)000258123600002
Első szerző:Vámosi György (biofizikus)
Cím:Dissecting interacting molecular populations by FRET / Vamosi, G., Damjanovich, S., Szollosi, J.
Dátum:2008
Tárgyszavak:Orvostudományok Elméleti orvostudományok kutatási jelentés
folyóiratcikk
FRET
Megjelenés:Cytometry. Part A. - 73A : 8 (2008), p. 681-684. -
További szerzők:Damjanovich Sándor (1936-2017) (biofizikus) Szöllősi János (1953-) (biofizikus)
Internet cím:elektronikus változat
DOI
Borító:
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