CCL

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1.

001-es BibID:BIBFORM004633
035-os BibID:(scopus)0344447088 (wos)000074651400008
Első szerző:Nagy Péter (biofizikus)
Cím:Intensity-based energy transfer measurements in digital imaging microscopy / Nagy P., Vamosi G., Bodnar A., Lockett S. J., Szollosi J.
Dátum:1998
ISSN:175-7571
Megjegyzések:Investigation of protein-protein associations is important in understanding structure and function relationships in living cells. Using Forster-type resonance energy transfer between donor and acceptor labeled monoclonal antibodies we can assess the cell surface topology of membrane proteins against which the antibodies were raised. In our current work we elaborated a quantitative image microscopic technique based on the measurement of fluorescence intensities to calculate the energy transfer efficiency on a pixel-by-pixel basis. We made use of the broad excitation and emission spectrum of cellular autofluorescence for background correction of images. In addition to the reference autofluorescence images (UV background) we recorded three fluorescent images (donor, acceptor and energy transfer signal) of donor-acceptor double labeled samples, and corrected for spectral spillage of the directly excited donor and acceptor fluorescence into the energy transfer image. After careful image registration we were able to calculate the energy transfer efficiency on a pixel-by -pixel basis. In this paper, we also present a critical comparison between results obtained with this method and other approaches (photobleaching and flow cytometric energy transfer measurements)
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Antibodies
Antibodies, Monoclonal
Biophysics
Cell Line
chemistry
Comparative Study
Energy Transfer
Fluorescence
Human
Hungary
Image Processing, Computer-Assisted
immunology
Membrane Proteins
methods
Microscopy
Microscopy, Fluorescence
Models, Theoretical
Proteins
Signal Processing,Computer-Assisted
Spectrometry, Fluorescence
statistics and numerical data
Support, Non-U.S.Gov't
Megjelenés:European Biophysics Journal. - 27 : 4 (1998), p. 377-389. -
További szerzők:Vámosi György (1967-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Lockett, Steven J. Szöllősi János (1953-) (biofizikus)
Internet cím:elektronikus változat
Borító:

2.

001-es BibID:BIBFORM004882
Első szerző:Panyi György (biofizikus)
Cím:Biophysical and pharmacological aspects of K+ channels in T lymphocytes / Panyi, G.
Dátum:2005
ISSN:0175-7571
Megjegyzések:Voltage-gated Kv1.3 and Ca2+-activated IKCa1 K+ channels play a pivotal role in antigen-dependent activation and proliferation of lymphocytes.These channels primarily determine the membrane potential of T cells, and thus regulate the magnitude of the Ca2+ signal required for efficient gene transcription and subsequent proliferation. Although these facts are generally well described and acknowledged, some recent discoveries have motivated research in this field, which is reviewed herein along with the basic biophysical characterization of Kv1.3 and IKCa1. The discovery of T cell subset-specific expression of Kv1.3 points towards the potential therapeutic use of high affinity and high specificity Kv1.3 inhibitors as specific immunosuppressors in the management of autoimmune diseases, such as Multiple Sclerosis. In meeting the demands for an ideal immunosuppressor, several laboratories have discovered potent natural Kv1.3- specific inhibitors and engineered peptides which have a better pharmacological profile based on the biophysical characterization of the interaction surface between the channel pore and the toxins. In contrast to the generally accepted permissive role of Kv1.3 during lymphocyte activation, the discovery of the localization of Kv1.3 in the immunological synapse might open new opportunities in the regulation of T cell activation by this channel species.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Amino Acid Sequence
Animals
Antigens
Antigens,CD3
Autoimmune Diseases
Biophysics
biosynthesis
Calcium
Cell Proliferation
Cells
chemistry
cytology
Electrophysiology
Fluorescence Resonance Energy Transfer
Humans
Hungary
immunology
Immunosuppressive Agents
Lymphocyte Activation
Lymphocytes
metabolism
methods
Models,Biological
Molecular Sequence Data
Multiple Sclerosis
Peptides
pharmacology
Potassium
Protein Structure,Tertiary
Research
Sequence Homology,Amino Acid
Support
Synapses
T-Lymphocytes
therapeutic use
Time Factors
Toxins
article
Research Support
Megjelenés:European Biophysics Journal. - 34 : 6 (2005), p. 515-529. -
Internet cím:elektronikus változat
Borító:

3.

001-es BibID:BIBFORM004884
Első szerző:Rubovszky Bálint (élettanász)
Cím:Detection of channel proximity by nanoparticle-assisted delaying of toxin binding : a combined patch-clamp and flow cytometric energy transfer study / Rubovszky, B., Hajdu, P., Krasznai, Z., Gaspar, R., Waldmann, T. A., Damjanovich, S., Bene, L.
Dátum:2005
ISSN:0175-7571
Megjegyzések:Gold nanoparticles of 30 nm diameter bound to cell-surface receptor major histocompatibility complex glycoproteins (MHCI and MHCII), interleukin-2 receptor alpha subunit (IL-2Ralpha), very late antigen-4 (VLA-4) integrin, transferrin receptor, and the receptor-type protein tyrosin phosphatase CD45 are shown by the patch-clamp technique to selectively modulate binding characteristics of Pi(2) toxin, an efficient blocker of K(v)1.3 channels. After correlating the electrophysiological data with those on the underlying receptor clusters obtained by simultaneously conducted flow cytometric energy transfer measurements, the modulation was proved to be sensitive to the density and size of the receptor clusters, and to the locations of the receptors as well. Based on the observation that engagement of MHCII by a monoclonal antibody down-regulates channel current and based on the close nanometer-scale proximity of the MHCI and MHCII glycoproteins, an analogous experiment was carried out when gold nanoparticles bound to MHCI delayed down-regulation of the K(v)1.3 current initiated by ligation of MHCII. Localization of K(v)1.3 channels in the nanometer-scale vicinity of the MHC-containing lipid rafts is demonstrated for the first time. A method is proposed for detecting receptor-channel or receptor-receptor proximity by observing nanoparticle-induced increase in relaxation times following concentration jumps of ligands binding to channels or to receptors capable of regulating channel currents.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Antibodies
Biophysics
Cell Line
chemistry
drug effects
Energy Transfer
Flow Cytometry
Glycoproteins
Gold
Human
Humans
Interleukin-2
Interleukin-2 Receptor alpha Subunit
Ion Channel Gating
Kv1.3 Potassium Channel
Ligands
Major Histocompatibility Complex
methods
Nanotubes
Particle Size
Patch-Clamp Techniques
pharmacokinetics
physiology
Potassium
Potassium Channels
Potassium Channels,Voltage-Gated
Protein Binding
Research
Scorpion Venoms
Support
T-Lymphocytes
Megjelenés:European Biophysics Journal. - 34 : 2 (2005), p. 127-143. -
További szerzők:Hajdu Péter (1975-) (biofizikus) Krasznai Zoltán (1950-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus) Bene László (1963-) (biofizikus)
Internet cím:elektronikus változat
DOI
Borító:

4.

001-es BibID:BIBFORM005515
Első szerző:Somodi Sándor (belgyógyász)
Cím:Effects of changes in extracellular pH and potassium concentration on Kv1.3 inactivation / Somodi S., Hajdu P., Gáspár R., Panyi G., Varga Z.
Dátum:2008
Megjegyzések:The Kv1.3 channel inactivates via the P/C-type mechanism, which is influenced by a histidine residue in the pore region (H399, equivalent of Shaker 449). Previously we showed that the electric field of the protonated histidines at low extracellular pH (pH(e)) creates a potential barrier for K(+) ions just outside the pore that hinders their exit from the binding site controlling inactivation (control site) thereby slowing inactivation kinetics. Here we examined the effects of extracellular potassium [K(+)](e) and pH(e) on the rate of inactivation of Kv1.3 using whole-cell patch-clamp. We found that in 150 mM [K(+)](e )inactivation was accelerated upon switching to pH(e) 5.5 as opposed to the slowing at 5 mM [K(+)](e). The transition from slowing to acceleration occurred at 40 mM [K(+)](e), whereas this "turning point" was at 20 mM [K(+)](e) for inward currents. The rate of entry of Ba(2+) ions from the extracellular space to the control site was significantly slowed by low pH(e) in wild-type hKv1.3, but it was insensitive to pH(e) in H399K and H399L mutants. Based on these observations we expanded our model and propose that the potential barrier created by the protonated histidines impedes the passage of K(+) ions between the extracellular medium and the control site in both directions and the effect on inactivation rate (acceleration or slowing) depends on the relative contribution of filling from the extracellular and intracellular sides.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:European Biophysics Journal. - 37 : 7 (2008), p. 1145-1156. -
További szerzők:Hajdu Péter (1975-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Panyi György (1966-) (biofizikus) Varga Zoltán (1969-) (biofizikus, szakfordító)
Internet cím:elektronikus változat
DOI
Borító:

5.

001-es BibID:BIBFORM080932
Első szerző:Volkó Julianna (biotechnológus)
Cím:Assembly of interleukin receptor subunits during trafficking / J. Volkó, Á. Kenesei, P. Várnai, F. Bestvater, T. A. Waldmann, K. Tóth, G. Vámosi
Dátum:2017
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
folyóiratcikk
Megjelenés:European Biophysics Journal. - 46 (2017), p. S379-S379. -
További szerzők:Kenesei Ádám (1989-) Várnai Péter Bestvater, Felix Waldmann, Thomas A. Tóth Katalin Vámosi György (1967-) (biofizikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:
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