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1.

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)
Internet cím:elektronikus változat
Borító:

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:BIBFORM042654
035-os BibID:(scopus)19444380683 (wos)000229353200007
Első szerző:Horváth Gábor (biofizikus)
Cím:Selecting the right fluorophores and flow cytometer for fluorescence resonance energy transfer measurements / Gábor Horváth, Miklós Petrás, Gergely Szentesi, Ákos Fábián, John W. Park, György Vereb, János Szöllősi
Dátum:2005
ISSN:1552-4922 1552-4930
Megjegyzések:BACKGROUND:Fluorescence resonance energy transfer applied in flow cytometry (FCET) is an excellent tool for determining supramolecular organization of biomolecules at the cell surface or inside the cell. Availability of new fluorophores and cytometers requires the establishment of fluorophore dye pairs most suitable for FCET measurements.METHODS:A gastric tumor cell line (N87) was labeled for major histocompatibility complex class I heavy chain and beta2-microglobulin with antibodies conjugated with fluorescein- and indocarbocyanine-like fluorophores and analyzed in FCET measurements on a cell-by-cell basis using three flow cytometers: FACSCalibur, FACSDiVa, and FACSArray.RESULTS:Normalized fluorescence intensity values were measured and normalized energy transfer efficiencies, spectral overlap integrals, and crucial dye- and instrument-dependent parameters were calculated for all matching pairs of seven fluorophores on the three commercial cytometers. The most crucial parameter in determining the applicability of the donor-acceptor pairs was the normalized fluorescence intensity and the least important one was the spectral overlap.CONCLUSIONS:On the basis of available laser lines, the optimal dye pair for all three cytometers is the Alexa546-Alexa647 pair, which produces high energy transfer efficiency values and has the best spectral characteristics with regard to laser excitation, detection of emission, and spectral overlap.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
fluorescence resonance energy transfer
flow cytometry
donor-acceptor pair
egyetemen (magyarországon) készült közlemény
Megjelenés:Cytometry. Part A. - 65A : 2 (2005), p. 148-157. -
További szerzők:Petrás Miklós (1977-) (orvos) Szentesi Gergely (1976-) (kémia-fizika tanár) Fábián Ákos István (1982-) (aneszteziológus) Park, John W. Vereb György (1965-) (biofizikus, orvos) Szöllősi János (1953-) (biofizikus)
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

4.

001-es BibID:BIBFORM004713
035-os BibID:(scopus)0037112996 (wos)000179662300005
Első szerző:Nagy Péter (biofizikus)
Cím:Lipid rafts and the local density of ErbB proteins influence the biological role of homo- and heteroassociations of ErbB2 / Nagy, P., Vereb, G., Sebestyen, Z., Horvath, G., Lockett, S. J., Damjanovich, S., Park, J. W., Jovin, T. M., Szollosi, J.
Dátum:2002
Megjegyzések:The ErbB family of transmembrane receptor tyrosine kinases plays an important role in the pathogenesis of many cancers. The four members of the family, ErbB1-4, form various homo- and heterodimers during the course of signal transduction. A second hierarchical level of molecular associations involving 10(2)-10(3) molecules, termed large-scale clustering, has also been identified, but the regulatory factors and biological consequences of such structures have not been systematically evaluated. In this report, we describe the states of association of ErbB2 and their relationship to local ErbB3 density and lipid rafts based on quantitative fluorescence microscopy of SKBR-3 breast cancer cells. Clusters of ErbB2 colocalized with lipid rafts identified by the GM1-binding B subunit of cholera toxin. Pixel-by-pixel analysis of fluorescence resonance energy transfer between labeled antibodies indicated that the homoassociation (homodimerization) of ErbB2 was proportional to the local density of ErbB2 and inversely proportional to that of ErbB3 and of the raft-specific lipid GM1. Crosslinking lipid rafts with the B subunit of cholera toxin caused dissociation of the rafts and ErbB2 clusters, an effect that was independent of the cytoskeletal anchoring of ErbB2. Crosslinking also decreased ErbB2-ErbB3 heteroassociation and the EGF- and heregulin-induced tyrosine phosphorylation of Shc. When cells were treated with the anti-ErbB2 monoclonal antibody 4D5 (parent murine version of Trastuzumab used in the immunotherapy of breast cancer), internalization of the antibody was inhibited by crosslinking of lipid rafts, but the antiproliferative activity of 4D5 was retained and even enhanced. We conclude that local densities of ErbB2 and ErbB3, as well as the lipid environment profoundly influence the association properties and biological function of ErbB2.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Adaptor Proteins,Signal Transducing
Adaptor Proteins,Vesicular Transport
analysis
Antibodies
Antibodies,Monoclonal
Antineoplastic Agents
Biophysics
Breast Neoplasms
Carcinoma
Cell Division
Cell Membrane
Cell Transformation,Neoplastic
Cells
Cholera Toxin
Cytoskeletal Proteins
Dimerization
drug effects
Energy Transfer
Eukaryotic Cells
Female
Fluorescence
Fluorescence Resonance Energy Transfer
genetics
Humans
Hungary
Macromolecular Substances
Membrane Microdomains
metabolism
Microscopy
Oncogene Proteins v-erbB
pharmacology
Phosphorylation
physiology
Protein Binding
Protein-Tyrosine Kinases
Proteins
Receptor Protein-Tyrosine Kinases
Receptor,erbB-2
Receptor,erbB-3
Receptors,Cell Surface
Research
Signal Transduction
Support
Tumor Cells,Cultured
ultrastructure
Megjelenés:Journal of Cell Science. - 115 : Pt 22 (2002), p. 4251-4262. -
További szerzők:Vereb György (1965-) (biofizikus, orvos) Sebestyén Zsolt Horváth Gábor (1974-) (biofizikus) Lockett, Steven J. Damjanovich Sándor (1936-2017) (biofizikus) Park, John W. Jovin, Thomas M. Szöllősi János (1953-) (biofizikus)
Internet cím:elektronikus változat
elektronikus változat
Borító:

5.

001-es BibID:BIBFORM004886
Első szerző:Szentesi Gergely (kémia-fizika tanár)
Cím:Computer program for analyzing donor photobleaching FRET image series / Szentesi, G., Vereb, G., Horvath, G., Bodnar, A., Fabian, A., Matko, J., Gaspar, R., Damjanovich, S., Matyus, L., Jenei, A.
Dátum:2005
ISSN:1552-4922
Megjegyzések:The photobleaching fluorescence resonance energy transfer (pbFRET) technique is a spectroscopic method to measure proximity relations between fluorescently labeled macromolecules using digital imaging microscopy. To calculate the energy transfer values one has to determine the bleaching time constants in pixel-by-pixel fashion from the image series recorded on the donor-only and donor and acceptor double-labeled samples. Because of the large number of pixels and the time-consuming calculations, this procedure should be assisted by powerful image data processing software. There is no commercially available software that is able to fulfill these requirements. METHODS: New evaluation software was developed to analyze pbFRET data for Windows platform in National Instrument LabVIEW 6.1. This development environment contains a mathematical virtual instrument package, in which the Levenberg-Marquardt routine is also included. As a reference experiment, FRET efficiency between the two chains (beta2-microglobulin and heavy chain) of major histocompatibility complex (MHC) class I glycoproteins and FRET between MHC I and MHC II molecules were determined in the plasma membrane of JY, human B lymphoma cells. RESULTS: The bleaching time constants calculated on pixel-by-pixel basis can be displayed as a color-coded map or as a histogram from raw image format. CONCLUSION: In this report we introduce a new version of pbFRET analysis and data processing software that is able to generate a full analysis pattern of donor photobleaching image series under various conditions.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Algorithms
analysis
beta 2-Microglobulin
Biophysics
Cell Line,Tumor
Cells
Energy Transfer
Fluorescence
Fluorescence Resonance Energy Transfer
Glycoproteins
Histocompatibility Antigens
Human
Humans
Hungary
Lymphoma
Major Histocompatibility Complex
metabolism
methods
Microscopy
Photobleaching
Research
Software
Support
egyetemen (Magyarországon) készült közlemény
Megjelenés:Cytometry. Part A. - 67 : 2 (2005), p. 119-128. -
További szerzők:Vereb György (1965-) (biofizikus, orvos) Horváth Gábor (1974-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Fábián Ákos István (1982-) (aneszteziológus) Matkó János (1952-) (biológus) Gáspár Rezső (1944-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Mátyus László (1956-) (biofizikus) Jenei Attila (1966-) (biofizikus)
Internet cím:elektronikus változat
DOI
Borító:

6.

001-es BibID:BIBFORM073588
Első szerző:Szöllősi János (biofizikus)
Cím:Új fluoreszcens jelzők a citometriában = Novel fluorescent markers in cytometry / Szöllősi János, Horváth Gábor, Nagy Péter, Vereb György
Dátum:2004
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
citometria
Megjelenés:Modern sejtanalitikai módszerek : a IV. Magyar Sejtanalitikai Konferencia kiadványa / Szerk. Vereb György Jr., Szöllősi János, Molnár B. - p. 57-60. -
További szerzők:Horváth Gábor (1974-) (biofizikus) Nagy Péter (1971-) (biofizikus) Vereb György (1965-) (biofizikus, orvos)
Borító:
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