CCL

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1.

001-es BibID:BIBFORM005177
Első szerző:de Bakker, Bärbel I.
Cím:Nanometer-scale organization of the alpha subunits of the receptors for IL2 and IL15 in human T lymphoma cells / de Bakker, B. I., Bodnar, A., van Dijk, E. M. H. P., Vamosi, G., Damjanovich, S., Waldmann, T. A., van Hulst, N. F., Jenei, A., Garcia-Parajo, M. F.
Dátum:2008
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Cells
Human
Lymphoma
Biophysics
Hungary
egyetemen (Magyarországon) készült közlemény
Megjelenés:Journal of Cell Science. - 121 : 5 (2008), p. 627-633. -
További szerzők:Dóczy-Bodnár Andrea (1970-) (biofizikus) Dijk, Erik M. H. P., van Vámosi György (1967-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Waldmann, Thomas A. Hulst, Niek F., van Jenei Attila (1966-) (biofizikus) Garcia-Parajo, Maria F.
Internet cím:elektronikus változat
Intézményi repozitóriumban (DEA) tárolt változat
DOI
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2.

001-es BibID:BIBFORM059573
Első szerző:Dóczy-Bodnár Andrea (biofizikus)
Cím:Non-random patterns of membrane proteins and their roles in transmembrane signaling / Andrea Bodnár, György Vámosi, Katalin Tóth, Attila Jenei, László Mátyus, Sándor Damjanovich
Dátum:2005
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
Membrane Proteins
egyetemen (Magyarországon) készült közlemény
Proteins
Biophysics
Megjelenés:Biophysical Aspects of Transmembrane Signaling / szerk. Damjanovich S. - p. 71-95
További szerzők:Vámosi György (1967-) (biofizikus) Tóth Katalin (biofizikus) Jenei Attila (1966-) (biofizikus) Mátyus László (1956-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
Pályázati támogatás:OTKA-TS40773
OTKA
OTKA-T048745
OTKA
OTKA-T423618
OTKA
OTKA-T43509
OTKA
OTKA-F46497
OTKA
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM004736
Első szerző:Panyi György (biofizikus)
Cím:Colocalization and nonrandom distribution of Kv1.3 potassium channels and CD3 molecules in the plasma membrane of human T lymphocytes / Panyi, G., Bagdany, M., Bodnar, A., Vamosi, G., Szentesi, G., Jenei, A., Matyus, L., Varga, S., Waldmann, T. A., Gaspar, R., Damjanovich, S.
Dátum:2003
ISSN:027-8424 (Print)
Megjegyzések:Distribution and lateral organization of Kv1.3 potassium channels and CD3 molecules were studied by using electron microscopy, confocal laser scanning microscopy, and fluorescence resonance energy transfer. Immunogold labeling and electron microscopy showed that the distribution of FLAG epitope-tagged Kv1.3 channels (Kv1.3/FLAG) significantly differs from the stochastic Poisson distribution in the plasma membrane of human T lymphoma cells. Confocal laser scanning microscopy images showed that Kv1.3/FLAG channels and CD3 molecules accumulated in largely overlapping membrane areas. The numerical analysis of crosscorrelation of the spatial intensity distributions yielded a high correlation coefficient (C = 0.64). A different hierarchical level of molecular proximity between Kv1.3/FLAG and CD3 proteins was reported by a high fluorescence resonance energy transfer efficiency (E = 51%). These findings implicate that reciprocal regulation of ion-channel activity, membrane potential, and the function of receptor complexes may contribute to the proper functioning of the immunological synapse.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Animals
Antigens, CD3
Biophysics
biosynthesis
Cell Membrane
Cells
chemistry
Electrophysiology
Energy Transfer
Epitopes
Fluorescence
Fluorescence Resonance Energy Transfer
Human
Humans
Hungary
Immunohistochemistry
immunology
Jurkat Cells
Kv1.3 Potassium Channel
Lymphocytes
Lymphoma
metabolism
Mice
Microscopy
Microscopy, Confocal
Microscopy, Electron
Models, Statistical
Potassium
Potassium Channels
Potassium Channels, Voltage-Gated
Proteins
Research
Support
T-Lymphocytes
Transfection
Megjelenés:Proceedings of the National Academy of Sciences of the United States of America. - 100 : 5 (2003), p. 2592-2597. -
További szerzők:Bagdány Miklós Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus) Szentesi Gergely (1976-) (kémia-fizika tanár) Jenei Attila (1966-) (biofizikus) Mátyus László (1956-) (biofizikus) Varga Sándor (1943-) (biofizikus) Waldmann, Thomas A. Gáspár Rezső (1944-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
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elektronikus változat
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4.

001-es BibID:BIBFORM004846
035-os BibID:(scopus)3242784810 (wos)000223353700003
Első szerző:Szentesi Gergely (kémia-fizika tanár)
Cím:Computer program for determining fluorescence resonance energy transfer efficiency from flow cytometric data on a cell-by-cell basis / Szentesi, G., Horvath, G., Bori, I., Vamosi, G., Szollosi, J., Gaspar, R., Damjanovich, S., Jenei, A., Matyus, L.
Dátum:2004
Megjegyzések:The determination of fluorescence resonance energy transfer (FRET) with flow cytometry (FCET) is one of the most efficient tools to study the proximity relationships of cell membrane components in cell populations on a cell-by-cell basis. Because of the high amount of data and the relatively tedious calculations, this procedure should be assisted by powerful data processing software. The currently available programs are not able to fulfill this requirement. We developed a Windows-based program to calculate fluorescence resonance energy transfer efficiency values from list mode flow cytometry standard (FCS) files. This program displays the measured data in standard plots by generating one- and two-parameter histograms on linear or logarithmic scales. A graphical gating tool allows the user to select the desired cell population according to any combination of the parameter values. The program performs several statistical calculations, including mean, S.D., percent of the gated data. We have implemented two types of data sheet for FRET calculations to aid and guide the user during the analysis: one with population-mean-based autofluorescence correction and the other with spectrum-based cell-by-cell autofluorescence correction. In this paper, we describe the gating algorithms, the file opening procedure and the rules of gating. The structure of the program and a short description of the graphical user-interface (GUI) are also presented in this article.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Algorithms
analysis
Biophysics
Cell Membrane
Computer Simulation
Energy Transfer
Flow Cytometry
Fluorescence
Fluorescence Resonance Energy Transfer
Humans
Hungary
methods
Research
Software
Support
egyetemen (Magyarországon) készült közlemény
Megjelenés:Computer Methods and Programs in Biomedicine. - 75 : 3 (2004), p. 201-211. -
További szerzők:Horváth Gábor (1974-) (biofizikus) Bori Imre (1929-2004) Vámosi György (1967-) (biofizikus) Szöllősi János (1953-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Jenei Attila (1966-) (biofizikus) Mátyus László (1956-) (biofizikus)
Internet cím:elektronikus változat
DOI
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5.

001-es BibID:BIBFORM046092
Első szerző:Vámosi György (biofizikus)
Cím:IL-2 and IL-15 receptor [alfa]-subunits are coexpressed in a supramolecular receptor cluster in lipid rafts of T cells / Vamosi G., Bodnar A., Vereb G., Jenei A., Goldman C. K., Langowski J., Toth K., Matyus L., Szollosi J., Waldmann T. A., Damjanovich S.
Dátum:2004
ISSN:0027-8424
Megjegyzések:The private alpha-chains of IL-2 and IL-15 receptors (IL-2R and IL-15R) share the signaling beta- and gamma(c)-subunits, resulting in both common and contrasting roles of IL-2 and IL-15 in T cell function. Knowledge of the cytokine-dependent subunit assembly is indispensable for understanding the paradox of distinct signaling capacities. By using fluorescence resonance energy transfer and confocal microscopy, we have shown that IL-2R alpha, IL-15R alpha, IL-2/15R beta and gamma(c)-subunits, as well as MHC class I and II glycoproteins formed supramolecular receptor clusters in lipid rafts of the T lymphoma line Kit 225 FT7.10. Fluorescence crosscorrelation microscopy demonstrated the comobility of IL-15R alpha with IL-2R alpha and MHC class I. A model was generated for subunit switching between IL-2R alpha and IL-15R alpha upon the binding of the appropriate cytokine resulting in the formation of high-affinity heterotrimeric receptors. This model suggests a direct role for the alpha-subunits, to which no definite function has been assigned so far, in tuning cellular responses to IL-2 or IL-15. In addition, both alpha-chains were at least partially homodimerized/oligomerized, which could be the basis of distinct signaling pathways by the two cytokines.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Proceedings Of The National Academy Of Sciences Of The United States Of America. - 101 : 30 (2004), p. 11082-11087. -
További szerzők:Dóczy-Bodnár Andrea (1970-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Jenei Attila (1966-) (biofizikus) Goldman, Caroline K. Langowski, Jörg Tóth Katalin (biofizikus) Mátyus László (1956-) (biofizikus) Szöllősi János (1953-) (biofizikus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:Szerző által megadott URL
DOI
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6.

001-es BibID:BIBFORM004673
Első szerző:Vereb György (biofizikus, orvos)
Cím:Cholesterol-dependent clustering of IL-2Ralpha and its colocalization with HLA and CD48 on T lymphoma cells suggest their functional association with lipid rafts / Vereb, G., Matko, J., Vamosi, G., Ibrahim, S. M., Magyar, E., Varga, S., Szollosi, J., Jenei, A., Gaspar, R., Waldmann, T. A., Damjanovich, S.
Dátum:2000
Megjegyzések:Immunogold staining and electron microscopy show that IL-2 receptor alpha-subunits exhibit nonrandom surface distribution on human T lymphoma cells. Analysis of interparticle distances reveals that this clustering on the scale of a few hundred nanometers is independent of the presence of IL-2 and of the expression of the IL-2R beta-subunit. Clustering of IL-2Ralpha is confirmed by confocal microscopy, yielding the same average cluster size, approximately 600-800 nm, as electron microscopy. HLA class I and II and CD48 molecules also form clusters of the same size. Disruption of cholesterol-rich lipid rafts with filipin or depletion of membrane cholesterol with methyl-beta-cyclodextrin results in the blurring of cluster boundaries and an apparent dispersion of clusters for all four proteins. Interestingly, the transferrin receptor, which is thought to be located outside lipid rafts, exhibits clusters that are only 300 nm in size and are less affected by modifying the membrane cholesterol content. Furthermore, transferrin receptor clusters hardly colocalize with IL-2Ralpha, HLA, and CD48 molecules (crosscorrelation coefficient is 0.05), whereas IL-2Ralpha colocalizes with both HLA and CD48 (crosscorrelation coefficient is between 0.37 and 0.46). This coclustering is confirmed by electron microscopy. The submicron clusters of IL-2Ralpha chains and their coclustering with HLA and CD48, presumably associated with lipid rafts, could underlie the efficiency of signaling in lymphoid cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
analysis
Antigens,CD
Biophysics
Cells
Cholesterol
HLA Antigens
Human
Hungary
Immunohistochemistry
Interleukin-2
Lymphoma
Lymphoma,T-Cell
Membrane Fluidity
Membrane Lipids
metabolism
Microscopy
Microscopy,Confocal
Microscopy,Immunoelectron
Neoplasm Proteins
pathology
physiology
Proteins
Receptors,Interleukin-2
Support,Non-U.S.Gov't
T-Lymphocytes
Tumor Cells,Cultured
Megjelenés:Proceedings of the National Academy of Sciences of the United States of America. - 97 : 11 (2000), p. 6013-6018. -
További szerzők:Matkó János (1952-) (biológus) Vámosi György (1967-) (biofizikus) Ibrahim, Shehu M. Magyar Erika Varga Sándor (1943-) (biofizikus) Szöllősi János (1953-) (biofizikus) Jenei Attila (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
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elektronikus változat
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