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001-es BibID:	BIBFORM036993
Első szerző:	Borbásné Sebestyén Veronika (biofizikus)
Cím:	Membrane potential influences mobility, interactions and signaling of interleukin-2 and-15 receptors in T cells / Sebestyén Veronika, Nagy Éva, Mocsár Gábor, Papp Ferenc, Hajdú Péter, Panyi György, Tóth Katalin, Thomas A. Waldmann, Damjanovich Sándor, Bodnár Andrea, Vámosi György
Dátum:	2011
Tárgyszavak:	Természettudományok Biológiai tudományok idézhető absztrakt MHC I interleukin-2 receptor IL-15 receptor protein cluster FRET IL-2 signaling Molekuláris Medicina Molekuláris Medicina
Megjelenés:	European Biophysics Journal with Biophysics Letters. - 40 : 1 (2011), p. 86. -
További szerzők:	Nagy Éva (1980-) (molekuláris biológus) Mocsár Gábor (1981-) (biofizikus) Papp Ferenc (1979-) (biofizikus) Hajdu Péter (1975-) (biofizikus) Panyi György (1966-) (biofizikus) Tóth Katalin Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus)
Pályázati támogatás:	K77600 OTKA 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-4.2.1/B-09/1/KONV-2010-0007 TÁMOP K+ csatornák élettani szerepe az immunrendszer sejtjeiben
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
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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
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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
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