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1.

001-es BibID:BIBFORM015990
Első szerző:Péter Mózes (orvos, neuroradiológus) ifj.
Cím:Recording and analysis of membrane potential and ion currents in cultured peripheral human lymphocytes / M. Peter, Z. Varga, Z. Krasznai, G. Panyi, R. Gaspar
Dátum:1998
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
Megjelenés:Practical guide to physical analysis of cell surface receptors / eds. Krasznai Z., Mátyus L. - p. 1-16
További szerzők:Varga Zoltán (1969-) (biofizikus, szakfordító) Krasznai Zoltán (1950-) (biofizikus) Panyi György (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus)
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2.

001-es BibID:BIBFORM004689
Első szerző:Péter Mózes (orvos, neuroradiológus) ifj.
Cím:Effects of toxins Pi2 and Pi3 on human T lymphocyte Kv1.3 channels : the role of Glu7 and Lys24 / Peter, M., Jr., Varga, Z., Hajdu, P., Gaspar, R., Damjanovich, S., Horjales, E., Possani, L. D., Panyi, G.
Dátum:2001
Megjegyzések:Pandinus imperator scorpion toxins Pi2 and Pi3 differ only by a single amino acid residue (neutral Pro7 in Pi2 vs. acidic Glu7 in Pi3). The binding kinetics of these toxins to human Kv1.3 showed that the decreased ON rate (k(ON) = 2.18 x 10(8) m(-1)sec(-1) for Pi2 and 1.28 x 10(7) m(-1)sec(-1) for Pi3) was almost entirely responsible for the increased dissociation constant (K(d)) of Pi3 (K(d) = 795 pm) as compared to Pi2 (K(d) = 44 pm). The ionic strength dependence of the association rates was exactly the same for the two toxins indicating that through-space electrostatic interactions can not account for the different ON rates. Results were further analyzed on the basis of the three-dimensional structural models of the toxins. A 3D structure of Pi3 was generated from the NMR spectroscopy coordinates of Pi2 by computer modeling. The Pi3 model resulted in a salt bridge between Glu7 and Lys24 in Pi3. Based on this finding our interpretation of the reduced ON rate of Pi3 is that the intramolecular salt bridge reduces the local positive electrostatic potential around Lys24 resulting in decreased short-range electrostatic interactions during the binding step. To support our finding, we constructed a 3D model of the Ser-10-Asp Charybdotoxin mutant displaying distinctly reduced affinity for Shaker channels. The mutant Charybdotoxin structure also displayed a salt bridge between residues Asp10 and Lys27 equivalent to the one between Glu7 and Lys24 in Pi3.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Amino Acid Sequence
Animal
Charybdotoxin
chemistry
drug effects
genetics
Glutamic Acid
Human
Hungary
In Vitro
Kinetics
Lysine
Membrane Potentials
metabolism
Models,Molecular
Molecular Sequence Data
pharmacology
Point Mutation
Potassium
Potassium Channel Blockers
Potassium Channels
Protein Conformation
Scorpion Venoms
Sequence Homology,Amino Acid
Support,Non-U.S.Gov't
T-Lymphocytes
Toxins
Megjelenés:The Journal of Membrane Biology. - 179 : 1 (2001), p. 13-25. -
További szerzők:Varga Zoltán (1969-) (biofizikus, szakfordító) Hajdu Péter (1975-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Horjales, E. Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Internet cím:DOI
elektronikus változat
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3.

001-es BibID:BIBFORM004670
Első szerző:Péter Mózes (orvos, neuroradiológus) ifj.
Cím:Blockage of human T lymphocyte Kv1.3 channels by Pi1, a novel class of scorpion toxin / Peter, M., Jr., Hajdu, P., Varga, Z., Damjanovich, S., Possani, L. D., Panyi, G., Gaspar, R.
Dátum:2000
Megjegyzések:Using the patch-clamp technique we determined that Pandinus imperator toxin Pi1, a recently described peptide toxin having four disulfide bridges instead of the usual three in scorpion toxins, blocked Kv1.3 channels of human T lymphocytes from the extracellular side with a 1:1 stoichiometry. Kv1.3 block was instantaneous and removable with toxin-free extracellular solution. The toxin did not influence activation or inactivation of the channels. We found that Pi1 blocked Kv1.3 with less affinity (K(d) = 11.4 nM) than the structurally related three disulfide bridge containing toxins Pi2 (50 pM) and Pi3 (0.5 nM). The fourth disulfide bridge in Pi1 had no influence on the channel binding ability of the toxin; the less effective block was due to differences in amino acid side chain properties at positions 11 and 35.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Amino Acid Sequence
Amino Acids
Animal
chemistry
Disulfides
drug effects
Human
Hungary
Kinetics
Lymphocytes
metabolism
Molecular Sequence Data
Patch-Clamp Techniques
pharmacology
Potassium
Potassium Channels
Protein Binding
Scorpion Venoms
Scorpions
Sequence Homology,Amino Acid
Support,Non-U.S.Gov't
T-Lymphocytes
Time Factors
Toxins
Megjelenés:Biochemical and Biophysical Research Communications. - 278 : 1 (2000), p. 34-37. -
További szerzők:Hajdu Péter (1975-) (biofizikus) Varga Zoltán (1969-) (biofizikus, szakfordító) Damjanovich Sándor (1936-2017) (biofizikus) Possani, Lourival Domingos Panyi György (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus)
Internet cím:elektronikus változat
DOI
Borító:

4.

001-es BibID:BIBFORM004635
Első szerző:Péter Mózes (orvos, neuroradiológus) ifj.
Cím:Pandinus imperator scorpion venom blocks voltage-gated K+ channels in human lymphocytes / Peter, M. Jr., Varga, Z., Panyi, G., Bene, L., Damjanovich, S., Pieri, C., Possani, L. D., Gaspar, R.
Dátum:1998
ISSN:006-291X
Megjegyzések:Using the patch-clamp technique, we determined that Pandinus imperator scorpion venom blocked whole-cell n-type K+ currents in human peripheral blood lymphocytes in a dose-dependent manner with Kd = 0.02 microgram/ml. K+ channel block was instantaneous and removable by washing with venom-free extracellular solution. The venom-induced block was independent of membrane potential. The venom did not influence activation and inactivation kinetics of the K+ channels, however, accelerated recovery from inactivation. Purified peptides Pi1, Pi2, and Pi3 from the P. imperator venom powerfully blocked Kv1.3 channels in human lymphocytes with Kd values of 9.7 nM, 50 pM, and 0.5 nM, respectively. Flow cytometric membrane potential measurements with the oxonol dye showed that Pi2, the most effective peptide toxin of the P. imperator venom, depolarizes human lymphocytes in accordance with its K+ channel blocking effect.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Barbiturates
blood
drug effects
Electrophysiology
Flow Cytometry
Fluorescent Dyes
Human
isolation and purification
Isoxazoles
Kinetics
Lymphocytes
Membrane Potentials
metabolism
Patch-Clamp Techniques
pharmacology
physiology
Potassium
Potassium Channel Blockers
Potassium Channels
Protein Binding
Scorpion Venoms
Support, Non-U.S.Gov't
Support, U.S.Gov't, P.H.S.
Toxins
Megjelenés:Biochemical and Biophysical Research Communications. - 242 : 3 (1998), p. 621-625. -
További szerzők:Varga Zoltán (1969-) (biofizikus, szakfordító) Panyi György (1966-) (biofizikus) Bene László (1963-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Pieri, Carlo Possani, Lourival Domingos Gáspár Rezső (1944-) (biofizikus)
Internet cím:DOI
elektronikus változat
Borító:

5.

001-es BibID:BIBFORM040092
Első szerző:Varga Zoltán (biofizikus, szakfordító)
Cím:Multiple Binding Sites for Melatonin on Kv1.3 / Varga, Z., Panyi, G., Peter, M., Jr., Pieri, C., Csecsei, G., Damjanovich, S., Gaspar, R.
Dátum:2001
ISSN:0006-3495
Megjegyzések:Melatonin is a small amino acid derivative hormone of the pineal gland. Melatonin quickly and reversibly blocked Kv1.3 channels, the predominant voltage-gated potassium channel in human T-lymphocytes, acting from the extracellular side. The block did not show state or voltage dependence and was associated with an increased inactivation rate of the current. A half-blocking concentration of 1.5 mM was obtained from the reduction of the peak current. We explored several models to describe the stoichiometry of melatonin-Kv1.3 interaction considering one or four independent binding sites per channel. The model in which the occupancy of one of four binding sites by melatonin is sufficient to block the channels gives the best fit to the dose-response relationship, although all four binding sites can be occupied by the drug. The dissociation constant for the individual binding sites is 8.11 mM. Parallel application of charybdotoxin and melatonin showed that both compounds can simultaneously bind to the channels, thereby localizing the melatonin binding site out of the pore region. However, binding of tetraethylammonium to its receptor decreases the melatonin affinity, and vice versa. Thus, the occupancy of the two separate receptor sites allosterically modulates each other.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biophysical Journal. - 80 : 3 (2001), p. 1280-1297. -
További szerzők:Panyi György (1966-) (biofizikus) Péter Mózes (1972-) (orvos, neuroradiológus) ifj. Pieri, Carlo Csécsei György (1948-2005) (idegsebész) Damjanovich Sándor (1936-2017) (biofizikus) Gáspár Rezső (1944-) (biofizikus)
Internet cím:Szerző által megadott URL
DOI
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