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1.

001-es BibID:BIBFORM004644
Első szerző:Brock Roland
Cím:Rapid characterization of green fluorescent protein fusion proteins on the molecular and cellular level by fluorescence correlation microscopy / Brock, R., Vamosi, G., Vereb, G., Jovin, T. M.
Dátum:1999
Megjegyzések:Fluorescence correlation microscopy (FCM) was applied to characterize fusion proteins of the green fluorescent protein (GFP) on the cellular as well as molecular level within seconds in an integrated instrument. FCM combines the inherent sensitivity and high spatial resolution of fluorescence correlation spectroscopy with fluorescence imaging and micropositioning, thereby providing a spectrum of molecular information in the cellular context. Signatures of characteristic parameters derived from the autocorrelation functions served to distinguish a GFP fusion protein of the epidermal growth factor receptor from GFP fluorescence in the endoplasmic reticulum and cytoplasm. Diffusion constants measured for free transiently expressed GFP reproduced values reported previously with other techniques. The accessible concentration range extends from millions to only a few thousand molecules per cell, with single molecule detectability in the femtoliter detection volume. The detailed molecular characterization offered by FCM is fully compatible with automation in sample identification and detection, offering new possibilities for highly integrated high-throughput screening
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Animal
Automation
chemistry
Cho Cells
Cytoplasm
Diffusion
Endoplasmic Reticulum
Epidermal Growth Factor
Fluorescence
Hamsters
instrumentation
Luminescent Proteins
methods
Microscopy
Microscopy, Fluorescence
Proteins
Receptor, Epidermal Growth Factor
Recombinant Fusion Proteins
Sensitivity and Specificity
Support, Non-U.S.Gov't
Transfection
ultrastructure
Megjelenés:Proceedings of the National Academy of Sciences of the United States of America. - 96 : 18 (1999), p. 10123-10128. -
További szerzők:Vámosi György (1967-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Jovin, Thomas M.
Internet cím:elektronikus változat
elektronikus változat
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2.

001-es BibID:BIBFORM004925
Első szerző:Damjanovich Sándor (biofizikus)
Cím:Structural hierarchy in the clustering of HLA class I molecules in the plasma membrane of human lymphoblastoid cells / Damjanovich, S., Vereb, G., Schaper, A., Jenei, A., Matko, J., Starink, J. P., Fox, G. Q., Arndt-Jovin, D. J., Jovin, T. M.
Dátum:1995
Megjegyzések:Major histocompatibility complex (MHC) class I antigens in the plasma membranes of human T (HUT-102B2) and B (JY) lymphoma cells were probed by immunochemical reagents using fluorescence, transmission electron, and scanning force microscopies. Fluorescent labels were attached to monoclonal antibodies W6/32 or KE-2 directed against the heavy chain of HLA class I (A, B, C) and L368 or HB28 against the beta 2-microglobulin light chain. The topological distribution in the nanometer range was studied by photobleaching fluorescence resonance energy transfer (pbFRET) on single cells. A nonrandom codistribution pattern of MHC class I molecules was observed over distances of 2-10 nm. A second, nonrandom, and larger-scale topological organization of the MHC class I antigens was detected by indirect immunogold labeling and imaging by transmission electron microscopy (TEM) and scanning force microscopy (SFM). Although some differences in antigen distribution between the B- and T-cell lines were detected by pbFRET, both cell lines exhibited similar clustering patterns by TEM and SFM. Such defined molecular distributions on the surfaces of cells of the immune system may reflect an underlying specialization of membrane lipid domains and fulfill important functional roles in cell-cell contacts and signal transduction.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Adult
analysis
beta 2-Microglobulin
Cell Line
Cell Membrane
chemistry
Energy Transfer
Fluorescence
Gold Colloid
Histocompatibility Antigens Class I
Human
Immunohistochemistry
immunology
Light
Lymphocytes
Major Histocompatibility Complex
methods
Microscopy
Microscopy,Electron
Signal Transduction
Support,Non-U.S.Gov't
Tumor Cells,Cultured
ultrastructure
egyetemen (Magyarországon) készült közlemény
Megjelenés:Proceedings of the National Academy of Sciences of the United States of America. - 92 : 4 (1995), p. 1122-1126. -
További szerzők:Vereb György (1965-) (biofizikus, orvos) Schaper, Achim Jenei Attila (1966-) (biofizikus) Matkó János (1952-) (biológus) Starink, J. Pascual Fox, Geoffrey Q. Arndt-Jovin, Donna J. Jovin, Thomas M.
Internet cím:elektronikus változat
elektronikus változat
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3.

001-es BibID:BIBFORM004864
035-os BibID:(scopus)26444452209 (wos)000232299300016
Első szerző:Friedländer Elza (biofizikus)
Cím:Signal transduction of erbB receptors in trastuzumab (Herceptin) sensitive and resistant cell lines : local stimulation using magnetic microspheres as assessed by quantitative digital microscopy / Friedlander, E., Arndt-Jovin, D. J., Nagy, P., Jovin, T. M., Szollosi, J., Vereb, G.
Dátum:2005
ISSN:1552-4922
Megjegyzések:ErbB2 (HER-2), a member of the epidermal growth factor (EGF) receptor family, is a class I transmembrane receptor tyrosine kinase. Although erbB2 has no known physiologic ligand, it can form complexes with other members of the family and undergo transactivation of its very potent kinase activity, thereby initiating downstream signaling and cell proliferation. ErbB2 is a frequent pathologic marker in ductal invasive breast carcinomas and is targeted by using a specific humanized monoclonal antibody, trastuzumab (Herceptin). The antibody is effective in only 20% to 50% of erbB2-positive tumors, and this resistance, as yet poorly understood, constitutes a major therapeutic challenge. METHODS: Magnetic microspheres coated with ligands or antibodies are widely used for separation of proteins and cells and allow localized, high intensity, and precisely timed stimulation of cells. We used EGF- and trastuzumab-covered paramagnetic microspheres, quantitative confocal laser scanning microscopy, and digital image processing to investigate the (trans)activation of and local signal propagation from erbB1 and erbB2 on trastuzumab sensitive and resistant carcinoma cell lines expressing these receptors at high levels. RESULTS: On A431 cells expressing high levels of endogenous erbB1 and transfected erbB2-mYFP (A4-erbB2-mYFP F4 cell line), EGF-coupled-microspheres activated erbB1 and transactivated erbB2-mYFP. In two other cell lines with comparable erbB2 expression but lower levels of erbB1, EGF microspheres transactivated erbB2 less efficiently. Trastuzumab in solution activated erbB2 on A4-erbB2-mYFP and the trastuzumab sensitive SKBR-3 cells, but only negligibly on the resistant JIMT-1 cells that showed a 10 times higher K(d) for the antibody. Nevertheless, pronounced erbB2 activation and tyrosine phosphorylation could be detected after stimulation with trastuzumab-coupled microspheres in all cell lines, although transactivation of erbB1 was negligible. Receptor phosphorylation was restricted to the immediate proximity of the microspheres, i.e., receptor clusters external to these locations remained inactive. CONCLUSION: ErbB1 ligand and erbB2 specific antibody attached to magnetic microspheres are efficient tools in assessing erbB activation, localized signal propagation, and erbB heterodimer formation. Trastuzumab coupled to microspheres is more efficient at accessing erbB2 and activating it than trastuzumab in solution
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Animals
Antibodies
Antibodies,Monoclonal
Biophysics
Carcinoma
Cell Line
Cell Line,Tumor
Cell Proliferation
Cells
chemistry
drug effects
Drug Resistance,Neoplasm
Epidermal Growth Factor
genetics
Humans
Hungary
Ligands
Magnetics
metabolism
methods
Microscopy
Microspheres
pharmacology
Phosphorylation
Proteins
Receptor,erbB-2
Research
Signal Transduction
Solubility
Support
Trans-Activation (Genetics)
Megjelenés:Cytometry. Part A. - 67 : 2 (2005), p. 161-171. -
További szerzők:Arndt-Jovin, Donna J. Nagy Péter (1971-) (biofizikus) Jovin, Thomas M. Szöllősi János (1953-) (biofizikus) Vereb György (1965-) (biofizikus, orvos)
Internet cím:elektronikus változat
DOI
Borító:

4.

001-es BibID:bibEBI7047
Első szerző:Fritzsche, Wolfgang
Cím:Combination of fluorescence in situ hybridization and scanning force microscopy for the ultrastructural characterization of defined chromatin regions / Fritzsche, W., Takács L., Vereb G., Schlammadinger, J., Jovin, T. M.
Dátum:1996
ISSN:1071-1023
Tárgyszavak:idegen nyelvű folyóiratközlemény külföldi lapban
Cells
Chromatin
Chromosomes
Dna
Fluorescence
Hybridization
Insitu hybridization.Human-chromosomes
Interphase
methods
Microscopy
ultrastructure
Megjelenés:Journal of Vacuum Science and Technology. B. - 14 : 2 (1996), p. 1399-1404. -
További szerzők:Takács Lili (1969-) (szemész) Vereb György (1965-) (biofizikus, orvos) Schlammadinger József (1938-) (kutató orvos) Jovin, Thomas M.
Internet cím:DOI
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5.

001-es BibID:BIBFORM004632
Első szerző:Hirschberg, J. G.
Cím:Interferometric measurment of fluorescence excitation spectra / Hirschberg, J. G., Vereb, G. Jr., Meyer, C. K., Kirsch, A. K., Kohen, E., Jovin, T. M.
Dátum:1998
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Fluorescence
Megjelenés:Applied Optics 37 : 10 (1998), p. 1953-1957. -
További szerzők:Vereb György (1965-) (biofizikus, orvos) Meyer, Christoph K. Kirsch, Achim K. Kohen, E. Jovin, Thomas M.
Borító:

6.

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
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7.

001-es BibID:BIBFORM073667
Első szerző:Vereb György (biofizikus, orvos)
Cím:Novel microscope-based approaches for the investigation of protein-protein interactions in signal transduction / György Vereb, Christoph K. Meyer, Thomas M. Jovin
Dátum:1997
ISBN:978 364 264 583 9
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
Megjelenés:Interacting Protein Domains. NATO ASI Series / ed. L. Heilmeyer. - p. 49-52. -
További szerzők:Meyer, Christoph K. Jovin, Thomas M.
Pályázati támogatás:F013335
OTKA
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

8.

001-es BibID:BIBFORM004936
Első szerző:Vereb György (biofizikus, orvos)
Cím:Immobilization of molecules, membranes and cells for modern optical and non-optical microscopy by photo-cross-linking / Vereb, G. Jr., Damjanovich, S., Jovin, T. M.
Dátum:1995
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Atomic force microscope.Adhesion.Surface
Cells
Microscopy
Megjelenés:Journal of Photochemistry and Photobiology. B, Biology. - 27 : 3 (1995), p. 275-277. -
További szerzők:Damjanovich Sándor (1936-2017) (biofizikus) Jovin, Thomas M.
Internet cím:elektronikus változat
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9.

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.
Internet cím:elektronikus változat
elektronikus változat
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