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1.

001-es BibID:BIBFORM038449
Első szerző:Batista, Cesar V. F.
Cím:Two novel toxins from the Amazonian scorpion Tityus cambridgei that block Kv1.3 and Shaker B K(+)-channels with distinctly different affinities / Cesar V. F. Batista, Froylan Gómez-Lagunas, Ricardo C. Rodriguez de la Vega, Péter Hajdu, György Panyi, Rezső Gáspár, Lourival D. Possani
Dátum:2002
ISSN:1570-9639
Megjegyzések:Two novel toxic peptides (Tc30 and Tc32) were isolated and characterized from the venom of the Brazilian scorpion Tityus cambridgei. The first have 37 and the second 35 amino acid residues, with molecular masses of 3,871.8 and 3,521.5, respectively. Both contain three disulfide bridges but share only 27% identity. They are relatively potent inhibitors of K(+)-currents in human T lymphocytes with K(d) values of 10 nM for Tc32 and 16 nM for Tc30, but they are less potent or quite poor blockers of Shaker B K(+)-channels, with respective K(d) values of 74 nM and 4.7 microM. Tc30 has a lysine in position 27 and a tyrosine at position 36 identical to those of charybdotoxin. These two positions conform the dyad considered essential for activity. On the contrary, Tc32 has a serine in the position equivalent to lysine 27 of charybdotoxin and does not contain any aromatic amino acid. Due to its unique primary sequence and to its distinctive preference for K(+)-channels of T lymphocytes, it was classified as the first example of a new subfamily of K(+)-channel-specific peptides (alpha-KT x 18.1). Tc30 is a member of the Tityus toxin II-9 subfamily and was given the number alpha-KT x 4.4.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1601 : 2 (2002), p. 123-131. -
További szerzők:Gómez-Lagunas, Froylan Rodriguez de la Vega, Ricardo C. Hajdu Péter (1975-) (biofizikus) Panyi György (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Possani, Lourival Domingos
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DOI
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2.

001-es BibID:BIBFORM004728
Első szerző:Hajdu Péter (biofizikus)
Cím:Cholesterol modifies the gating of Kv1.3 in human T lymphocytes / Péter Hajdú, Zoltán Varga, Carlo Pieri, György Panyi, Rezső Gáspár
Dátum:2003
ISSN:0031-6768
Megjegyzések:The Kv1.3 potassium channel that belongs to the Shaker family of voltage-gated K(+) channels plays a crucial role in the mitogenic response of T cells. Because it spans the cell membrane its function can be influenced by lipid-protein interactions. In order to study the effect of lipid-protein interactions on the functioning of Kv1.3 we manipulated the membrane cholesterol content in T cells mimicking various physiological conditions by means of the oligosaccharide methyl-beta-cyclodextrin (MbetaCD) and its cholesterol-saturated complex (MbetaCD/C). Fluorescence polarization anisotropy and peak current density were used to monitor the efficiency of cholesterol removal (MbetaCD) and loading (MbetaCD/C). Using whole-cell patch-clamp technique we determined the kinetic and steady-state parameters of activation and inactivation of the Kv1.3 currents under different treatment conditions. Upon elevation of cholesterol content by 1 or 1.5 mg/ml MbetaCD/C the rates of both activation and inactivation were slowed. Moreover, the increased cholesterol level in the membrane resulted in a biphasic activation curve. Cholesterol depletion with MbetaCD (0.95 and 1.425 mg/ml) caused no significant changes in the gating characteristics of Kv1.3. The equilibrium between the open and the closed states of the channels was affected by increased cholesterol content, but at the same time steady-state inactivation was unchanged. We argue that manipulation of membrane cholesterol changed both the kinetic properties of Kv1.3 and steady-state parameters of activation by modifying lipid-protein interactions
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
beta-Cyclodextrins
Biophysics
Cell Membrane
Cells
Cholesterol
Cyclodextrins
drug effects
Electric Conductivity
Fluorescence
Fluorescence Polarization
Human
Humans
Hungary
Ion Channel Gating
Kinetics
Kv1.3 Potassium Channel
Lymphocytes
Membrane Microdomains
Membrane Potentials
metabolism
pharmacology
physiology
Potassium
Potassium Channels
Potassium Channels,Voltage-Gated
Research
Support
T-Lymphocytes
Megjelenés:Pflügers Archiv. - 445 : 6 (2003), p. 674-682. -
További szerzők:Varga Zoltán (1969-) (biofizikus, szakfordító) Pieri, Carlo Panyi György (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus)
Internet cím:DOI
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3.

001-es BibID:BIBFORM004715
Első szerző:Panyi György (biofizikus)
Cím:Pharmacological effects of melatonin on ion channels / Panyi, G., Somodi, S., Varga, Z., Hajdu, P., Pieri, C., Pandi-Perumal, S. R., Damjanovich, S., Gaspar, R., Hardar, C., Singaravel, M., Maitra, S. K.
Dátum:2002
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
Ion Channels
Melatonin
Megjelenés:Treatise on Pineal Gland and Melatonin. - p. 489-506.
További szerzők:Somodi Sándor (1977-) (belgyógyász) Varga Zoltán (1969-) (biofizikus, szakfordító) Hajdu Péter (1975-) (biofizikus) Pieri, Carlo Pandi-Perumal, Seithikurippu R. Damjanovich Sándor (1936-2017) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Hardar, C. Singaravel, M. Maitra, S. K.
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4.

001-es BibID:BIBFORM005189
Első szerző:Papp Ferenc (biofizikus)
Cím:CRAC channels in developing human dendritic cells / Papp, F., Hajdu, P., Varga, Z., Zsiros, E., Ludanyi, K., Gaspar, R., Rajnavolgyi, E., Panyi, Gy.
Dátum:2008
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Human
Dendritic Cells
Cells
Megjelenés:Biophysical Journal. - 94 : Suppl (2008), p. B290 -
További szerzők:Hajdu Péter (1975-) (biofizikus) Varga Zoltán (1969-) (biofizikus, szakfordító) Zsíros Emese (1980-) (orvos) Ludányi Katalin (1975-) (immunológus) Gáspár Rezső (1944-) (biofizikus) Rajnavölgyi Éva (1950-) (immunológus) Panyi György (1966-) (biofizikus)
Internet cím:elektronikus változat
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5.

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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6.

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:

7.

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
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8.

001-es BibID:BIBFORM004738
Első szerző:Somodi Sándor (belgyógyász)
Cím:C-type inactivation of Kv1.3 channels : combined effects of extracellular pH,K+ concentration and ionic strength / Somodi, S., Hajdu, P., Varga, Z., Gaspar, R., Panyi, G.
Dátum:2003
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:Biophysical Journal. - 84 : 2 Part 2 (2003), p. B240. -
További szerzők:Hajdu Péter (1975-) (biofizikus) Varga Zoltán (1969-) (biofizikus, szakfordító) Gáspár Rezső (1944-) (biofizikus) Panyi György (1966-) (biofizikus)
Borító:

9.

001-es BibID:BIBFORM004844
Első szerző:Somodi Sándor (belgyógyász)
Cím:pH-dependent modulation of Kv1.3 inactivation : role of His399 / Somodi, S., Varga, Z., Hajdu, P., Starkus, J. G., Levy, D. I., Gaspar, R., Panyi, G.
Dátum:2004
Megjegyzések:The Kv1.3 K(+) channel lacks N-type inactivation, but during prolonged depolarized periods it inactivates via the slow (P/C type) mechanism. It bears a titratable histidine residue in position 399 (equivalent of Shaker 449), a site known to influence the rate of slow inactivation. As opposed to several other voltage-gated K(+) channels, slow inactivation of Kv1.3 is slowed when extracellular pH (pH(o)) is lowered under physiological conditions. Our findings are as follows. First, when His399 was mutated to a lysine, arginine, leucine, valine or tyrosine, extracellular acidification (pH 5.5) accelerated inactivation reminiscent of other Kv channels. Second, inactivation of the wild-type channel was accelerated by low pH(o) when the ionic strength of the external solution was raised. Inactivation of the H399K mutant was also accelerated by high ionic strength at pH 7.35 but not the inactivation of H399L. Third, after the external application of blocking barium ions, recovery of the wild-type current during washout was slower in low pH(o). Fourth, the dissociation rate of Ba(2+) was pH insensitive for both H399K and H399L. Furthermore, Ba(2+) dissociation rates were equal for H399K and the wild type at pH 5.5 and were equal for H399L and the wild type at pH 7.35. These observations support a model in which the electric field of the protonated histidines creates a potential barrier for potassium ions just outside the external mouth of the pore that hinders their exit from the binding site controlling inactivation. In Kv1.3, this effect overrides the generally observed speeding of slow inactivation when pH(o) is reduced.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Animals
Barium
Biophysics
chemistry
Extracellular Fluid
genetics
Histidine
Human
Humans
Hungary
Hydrogen-Ion Concentration
Ion Channel Gating
Kv1.3 Potassium Channel
Lysine
Membrane Potentials
metabolism
Models,Biological
Mutation
Patch-Clamp Techniques
physiology
Potassium
Potassium Channels
Potassium Channels,Voltage-Gated
Research
Support
Megjelenés:American Journal of Physiology. Cell Physiology. - 287 : 4 (2004), p. C1067-C1076. -
További szerzők:Varga Zoltán (1969-) (biofizikus, szakfordító) Hajdu Péter (1975-) (biofizikus) Starkus, John G. Levy, Daniel I. Gáspár Rezső (1944-) (biofizikus) Panyi György (1966-) (biofizikus)
Internet cím:DOI
elektronikus változat
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10.

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:

11.

001-es BibID:BIBFORM002770
Első szerző:Varga Zoltán (biofizikus, szakfordító)
Cím:Involvement of membrane channels in autoimmune disorders / Zoltán Varga, Péter Hajdu, György Panyi, Rezső Gáspár, Zoltán Krasznai
Dátum:2007
Megjegyzések:Ion channels are ubiquitous transmembrane proteins that are involved in a wide variety of cellular functions by selectively controlling the passage of ions across the plasma membrane. Among these functions many immune processes, including those in autoimmune reactions, also rely on the operation of ion channels, but the roles of ion channels can be very diverse. Here the participation of ion channels in three different roles in autoimmune processes is discussed: 1. ion channels in effector immune cells attacking other tissues causing autoimmune diseases, such as multiple sclerosis; 2. ion channels as direct targets of the immune system whereby loss of channel function leads to disease, as in myasthenia gravis; 3. ion channels whose function is modulated in the target cells by an apoptotic signal transduction cascade, such as the Fas/Fas ligand pathway. The numerous tasks that ion channels perform in autoimmune disorders and the wealth of information that has been gathered about them in recent years together provide a good basis for the design and production of drugs that may be effectively used in the therapy of these diseases
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Animals
Autoimmune Diseases
Biophysics
Cell Membrane
Cells
Humans
Hungary
Immune System
Ion Channels
Lymphocyte Activation
metabolism
physiology
Proteins
Research
Signal Transduction
Support
T-Lymphocytes
therapy
Megjelenés:Current Pharmaceutical Design. - 13 : 24 (2007), p. 2456-2468. -
További szerzők:Hajdu Péter (1975-) (biofizikus) Panyi György (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Krasznai Zoltán (1950-) (biofizikus)
Internet cím:elektronikus változat
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12.

001-es BibID:BIBFORM010313
Első szerző:Zsíros Emese (orvos)
Cím:Developmental switch of the expression of ion channels in human dendritic cells / Zsiros Emese, Kis-Tóth Katalin, Hajdú Péter, Gáspár Rezső, Joanna Bielansk, Antonio Felipe, Rajnavölgyi Éva, Panyi György
Dátum:2009
ISSN:0022-1767
Megjegyzések:Modulation of the expression and activity of plasma membrane ion channels is one of the mechanisms by which immune cells can regulate their intracellular Ca2(+) signaling pathways required for proliferation and/or differentiation. Voltage-gated K+ channels, inwardly rectifying K+ channels, and Ca2+-activated K+ channels have been described to play a major role in controlling the membrane potential in lymphocytes and professional APCs, such as monocytes, macrophages, and dendritic cells (DCs). Our study aimed at the characterization and identification of ion channels expressed in the course of human DC differentiation from monocytes. We report in this study for the first time that immature monocyte-derived DCs express voltage-gated Na+ channels in their plasma membrane. The analysis of the biophysical and pharmacological properties of the current and PCR-based cloning revealed the presence of Nav1.7 channels in immature DCs. Transition from the immature to a mature differentiation state, however, was accompanied by the down-regulation of Nav1.7 expression concomitant with the up-regulation of voltage-gated Kv1.3 K+ channel expression. The presence of Kv1.3 channels seems to be common for immune cells; hence, selective Kv1.3 blockers may emerge as candidates for inhibiting various functions of mature DCs that involve their migratory, cytokine-secreting, and T cell-activating potential.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Union of Pharmacology
Dependent K+ channel
Human Lymhocytes T
Potassium channels
Sodium Channels
Electrophysiological properties
Peripheral nerve
Immune system
Macrophages
Activation
Megjelenés:The Journal of Immunology 183 : 7 (2009), p. 4483-4492. -
További szerzők:Kis-Tóth Katalin (1975-) (immunológus) Hajdu Péter (1975-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Bielansk, Joanna Felipe, Antonio Rajnavölgyi Éva (1950-) (immunológus) Panyi György (1966-) (biofizikus)
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DOI
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