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1.

001-es BibID:BIBFORM004855
Első szerző:Bagdány Miklós
Cím:Anuroctoxin, a new scorpion toxin of the alpha-KTx 6 subfamily, is highly selective for Kv1.3 over IKCa1 ion channels of human T lymphocytes / Bagdany, M., Batista, C. V. F., Valdez-Cruz, N. A., Somodi, S., Rodriguez de la Vega, R. C., Licea, A. F., Varga, Z., Gaspar, R., Possani, L. D., Panyi, G.
Dátum:2005
Megjegyzések:The physiological function of T lymphocytes can be modulated selectively by peptide toxins acting on Kv1.3 K(+) channels. Because Kv1.3-specific peptide toxins are considered to have a significant therapeutic potential in the treatment of autoimmune diseases, the discovery of new toxins is highly motivated. Through chromatographic procedures and electrophysiological assays, using patch-clamp methodology, the isolation of a novel peptide named anuroctoxin was accomplished using the venom of the Mexican scorpion Anuroctonus phaiodactylus. It has 35 amino acid residues with a molecular weight of 4082.8, tightly bound by four disulfide bridges whose complete covalent structure was determined. It has a pyroglutamic acid at the N-terminal region and an amidated C-terminal residue. Sequence comparison and phylogenetic clustering analysis classifies anuroctoxin into subfamily 6 of the alpha-KTx scorpion toxins (systematic name, alpha-KTx 6.12). Patch-clamp experiments show that anuroctoxin is a high-affinity blocker of Kv1.3 channels of human T lymphocytes with a K(d) of 0.73 nM, and it does not block the Ca(2+)-activated IKCa1 K(+) channels. These two channels play different but important roles in T-lymphocyte activation. Furthermore, the toxin practically does not inhibit Shaker IR, mKv1.1, and rKv2.1 channels, whereas the affinity of anuroctoxin for hKv1.2 is almost an order of magnitude smaller than for Kv1.3. The pharmacological profile and the selectivity of this new toxin for Kv1.3 over IKCa1 may provide an important tool for the modulation of the immune system, especially in cases in which selective inhibition of Kv1.3 is required.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Animals
antagonists & inhibitors
Autoimmune Diseases
Biophysics
chemistry
drug effects
Human
Humans
Hungary
Immune System
Intermediate-Conductance Calcium-Activated Potassium Channels
Ion Channels
isolation & purification
Kv1.3 Potassium Channel
Lymphocytes
Models,Molecular
Molecular Weight
pharmacology
Phylogeny
Potassium
Potassium Channel Blockers
Potassium Channels
Potassium Channels,Calcium-Activated
Potassium Channels,Voltage-Gated
Research
Scorpion Venoms
Sequence Alignment
Support
T-Lymphocytes
Toxins
Toxins,Biological
Megjelenés:Molecular Pharmacology. - 67 : 4 (2005), p. 1034-1044. -
További szerzők:Batista, Cesar V. F. Valdez-Cruz, Norma A. Somodi Sándor (1977-) (belgyógyász) Rodriguez de la Vega, Ricardo C. Licea, Alexei F. Varga Zoltán (1969-) (biofizikus, szakfordító) Gáspár Rezső (1944-) (biofizikus) Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Internet cím:elektronikus változat
DOI
elektronikus változat
Borító:

2.

001-es BibID:BIBFORM004700
Első szerző:Bagdány Miklós
Cím:Non-random distribution of Kv1.3 channels in the lymphocyte plasma membrane / Bagdany, M., Varga, S., Szentesi, G., Bodnar, A., Jenei, A., Damjanovich, S., Gaspar, R., Panyi, G.
Dátum:2002
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:Biophysical Journal. - 82 : 1 (2002), p. 1212. -
További szerzők:Varga Sándor (1943-) (biofizikus) Szentesi Gergely (1976-) (kémia-fizika tanár) Dóczy-Bodnár Andrea (1970-) (biofizikus) Jenei Attila (1966-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Panyi György (1966-) (biofizikus)
Borító:

3.

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
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM040778
Első szerző:Batta József Tamás (fül-orr-gégész)
Cím:Active and passive behaviour in the regulation of stiffness of the lateral wall in outer hair cells of the guinea-pig / Batta, T. J., Panyi, G., Gaspar, R., Sziklai, I.
Dátum:2003
ISSN:0031-6768
Megjegyzések:The stiffness of the outer hair cell (OHC) lateral wall, measured by the micropipette aspiration technique, is non-linear, decreasing from the ciliary pole (stiffness parameter Sp 1.83+/-0.13 nN/microm n=10) towards the cell base (Sp 1.14+/-0.16 nN/microm, n=10) irrespective of the cochleoapical or cochleobasal origin of the cells. The length of the aspirated lateral wall segment was related exponentially to the duration of the applied negative pressure (6 cm H2O) in the synaptic region of the OHCs whereas an active, sigmoid component was observed between 30 and 60 s in the supranuclear regions. A significant increase of the midlateral wall stiffness (to 1.91+/-0.23 nN/microm; n=10) was observed in calcium-free medium and the sigmoid component of the response of the lateral wall was abolished. Salicylate (5 mM) had no significant effect on the active sigmoid behaviour of the lateral wall (n=10). Gadolinium (5 mM), a non-specific cation channel blocker, increased the stiffness of the lateral wall and attenuated the active component (n=10). The motor protein prestin thus does not seem to be involved in the active stiffness regulation seen in this study. A role for the cortical cytoskeleton in the regulation of stiffness seems reasonable according to our model. The mechanism may involve calcium-dependent metabolic modification of cytoskeletal or membrane proteins.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Pflugers Archiv. - 447 : 3 (2003), p. 328-336. -
További szerzők:Panyi György (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Sziklai István (1954-) (fül-orr-gégész)
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DOI
Intézményi repozitóriumban (DEA) tárolt változat
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5.

001-es BibID:BIBFORM005176
Első szerző:Corzo, Gerardo
Cím:A selective blocker of Kv1.2 and Kv1.3 potassium channels from the venomof the scorpion Centruroides suffusus suffusus / Corzo G., Papp F., Varga Z., Barraza O., Espino-Solis P. G., Rodríguez de la Vega R. C., Gaspar R., Panyi G., Possani L. D.
Dátum:2008
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Kv1.3 Potassium Channel
Potassium
Potassium Channels
Megjelenés:Biochemical Pharmacology 76 : 9 (2008), p. 1142-1154. -
További szerzők:Papp Ferenc (1979-) (biofizikus) Varga Zoltán (1969-) (biofizikus, szakfordító) Barraza, Omar Espino-Solis, Pavel G. Rodriguez de la Vega, Ricardo C. Gáspár Rezső (1944-) (biofizikus) Panyi György (1966-) (biofizikus) Possani, Lourival Domingos
Internet cím:elektronikus változat
DOI
Borító:

6.

001-es BibID:BIBFORM004833
Első szerző:Damjanovich Sándor (biofizikus)
Cím:An alternative to conventional immunosuppression : small-molecule inhibitors of Kv1.3 channels / Damjanovich, S., Gaspar, R., Panyi, G.
Dátum:2004
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Biophysics
Hungary
Immunosuppression
Research
Megjelenés:Molecular Interventions. - 4 : 5 (2004), p. 250-254. -
További szerzők:Gáspár Rezső (1944-) (biofizikus) Panyi György (1966-) (biofizikus)
Internet cím:elektronikus változat
DOI
Borító:

7.

001-es BibID:BIBFORM015989
Első szerző:Gáspár Rezső (biofizikus)
Cím:Measurement and analysis of different aspects of potassium currents in human lymphocytes / R. Gáspár, Z. Varga, Gy. Panyi, Z. Krasznai, C. Pieri, S. Damjanovich
Dátum:1998
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
Megjelenés:Signal Transduction. Single cell techniques / eds. Bert van Duijn; Anneke Wiltink. - p. 214-235.
További szerzők:Varga Zoltán (1969-) (biofizikus, szakfordító) Panyi György (1966-) (biofizikus) Krasznai Zoltán (1950-) (biofizikus) Pieri, Carlo Damjanovich Sándor (1936-2017) (biofizikus)
Borító:

8.

001-es BibID:BIBFORM006036
Első szerző:Gáspár Rezső (biofizikus)
Cím:Effects of bretylium tosylate on voltage-gated potassium channels in human T lymphocytes / Gaspar, R., Panyi, G., Ypey, D. L., Krasznai, Z., Vereb, G., Pieri, C., Damjanovich, S.
Dátum:1994
Megjegyzések:Using the patch-clamp technique, we determined that bretylium tosylate, a quaternary ammonium compound possessing immunomodulating activity, decreased the whole-cell K+ current in human T lymphocytes, in a dose-dependent manner, in the 0.05-5 mM extracellular concentration range. Bretylium tosylate prolonged the recovery from inactivation and accelerated the inactivation and deactivation of the K+ current but did not influence the kinetics of activation or the voltage dependence of activation and steady state inactivation of the K+ conductance. The percentage of drug-induced block was independent of membrane potential. K+ channel block by bretylium tosylate was partially and slowly removable by washing with drug-free extracellular solution. Bovine serum albumin (10 mg/ml) in the bath lifted the drug-induced block almost instantaneously, although not completely. In control experiments bovine serum albumin increased the inactivation time constant of the K+ channels but left the peak K+ current amplitude unaffected. On the basis of the experimental evidence, a gating-dependent allosteric interaction is suggested for the mechanism of drug action. The effective dose range, time of exposure, and reversibility of bretylium tosylate-induced K+ channel block correlated well with the same parameters of the drug-induced inhibition of T lymphocyte activation. The reported effects of bretylium tosylate on T cell mitogenesis can be regarded partly as a consequence of its blocking effects on voltage-gated K+ channels.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Bretylium Tosylate
Cell Membrane
drug effects
Electrophysiology
Human
Hungary
In Vitro
Ion Channel Gating
Kinetics
Lymphocytes
pharmacology
physiology
Potassium
Potassium Channels
Support,Non-U.S.Gov't
T-Lymphocytes
Megjelenés:Molecular pharmacology. - 46 : 4 (1994), p. 762-766. -
További szerzők:Panyi György (1966-) (biofizikus) Ypey, Dirk L. Krasznai Zoltán (1950-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Pieri, Carlo Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:elektronikus változat
Borító:

9.

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
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

10.

001-es BibID:BIBFORM004687
Első szerző:Nagy Péter (biofizikus)
Cím:Cell fusion experiments reveal distinctly different association characteristics of cell-surface receptors / Péter Nagy, László Mátyus, Attila Jenei, György Panyi, Sándor Varga, János Matkó, János Szöllősi, Rezső Gáspár, Thomas M. Jovin, Sándor Damjanovich
Dátum:2001
Megjegyzések:The existence of small- and large-scale membrane protein clusters, containing dimers, oligomers and hundreds of proteins, respectively, has become widely accepted. However, it is largely unknown whether the internal structure of these formations is dynamic or static. Cell fusion was used to perturb the distribution of existing membrane protein clusters, and to investigate their mobility and associations. Scanning near-field optical microscopy, confocal and electron microscopy were applied to detect the exchange of proteins between large-scale protein clusters, whereas photobleaching fluorescence energy transfer was used to image the redistribution of existing small-scale membrane protein clusters. Large-scale clusters of major histocompatibility complex (MHC)-I exchanged proteins with each other and with MHC-II clusters. Similarly to MHC-I, large-scale MHC-II clusters were also dynamic. Exchange of components between small-scale protein clusters was not universal: intermixing did not take place in the case of MHC-II homoclusters; however, it was observed for homoclusters of MHC-I and for heteroclusters of MHC-I and MHC-II. These processes required a fluid state of the plasma membrane, and did not depend on endocytosis-mediated recycling of proteins. The redistribution of large-scale MHC-I clusters precedes the intermixing of small-scale clusters of MHC-I indicating a hierarchy in protein association. Investigation of a set of other proteins (alpha subunit of the interleukin 2 receptor, CD48 and transferrin receptor) suggested that a large-scale protein cluster usually exchanges components with the same type of clusters. These results offer new insight into processes requiring time-dependent changes in membrane protein interactions.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Biophysics
Cell Fusion
Cell Line
Cell Membrane
chemistry
Dyes
Energy Transfer
Fluorescence
Fluorescent Dyes
Gold Colloid
Histocompatibility Antigens
Histocompatibility Antigens Class I
Histocompatibility Antigens Class II
Human
Hungary
Interleukin-2
Major Histocompatibility Complex
Membrane Microdomains
metabolism
methods
Microscopy
Microscopy,Fluorescence
physiology
Proteins
Receptor Aggregation
Receptors,Cell Surface
Receptors,Interleukin-2
Support,Non-U.S.Gov't
Megjelenés:Journal of Cell Science 114 : Pt 22 (2001), p. 4063-4071. -
További szerzők:Mátyus László (1956-) (biofizikus) Jenei Attila (1966-) (biofizikus) Panyi György (1966-) (biofizikus) Varga Sándor (1943-) (biofizikus) Matkó János (1952-) (biológus) Szöllősi János (1953-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Jovin, Thomas M. Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:elektronikus változat
Szerző által megadott URL
Borító:

11.

001-es BibID:BIBFORM004881
Első szerző:Olamendi-Portugal, Timoteo
Cím:Novel alpha-KTx peptides from the venom of the scorpion Centruroides elegans selectively blockade Kv1.3 over IKCa1 K+ channels of T cells / Olamendi-Portugal, T., Somodi, S., Fernandez, J. A., Zamudio, F. Z., Becerril, B., Varga, Z., Panyi, G., Gaspar, R., Possani, L. D.
Dátum:2005
ISSN:0041-0101
Megjegyzések:From the venom of the Mexican scorpion Centruroides elegans Thorell five peptides were isolated to homogeneity by chromatographic procedures and their full amino acid sequence was determined by automatic Edman degradation. They all belong to the Noxiustoxin subfamily of scorpion toxins and were given the systematic names alpha-KTx 2.8 to 2.12, with trivial names Ce1 to Ce5, respectively. They have 39 amino acid residues, except for Ce3 which has only 38, but all of them have three disulfide bridges, and have molecular weights of 4255, 4267, 4249, 4295 and 4255 atomic mass units, respectively for Ce1 to Ce5. The C-terminal residues of Ce2, Ce4 and Ce5 were found to be amidated. The electrophysiological assay (whole-cell patch-clamp) showed that out of the five peptides, Ce1 (alpha-KTx 2.8), Ce2 (alpha-KTX2.9) and Ce4 (alpha-KTx 2.11) were effective blockers of Kv1.3 channels of human T lymphocytes, whereas these peptides did not inhibit the Ca2+-activated K+ channels (IKCa1) of the same cells. The equilibrium dissociation constants of these peptides for Kv1.3 were 0.70, 0.25 and 0.98nM for Ce1, Ce2 and Ce4, respectively. Furthermore, toxins Ce1, Ce2 and Ce4 practically did not inhibit the related voltage gated Shaker K+ channels, and rKv2.1 channels of the Shab family. The high affinity blockage of Kv1.3 channels by these peptides and their selectivity for Kv1.3 over IKCa1 may have significance in the development of novel tools for suppressing the function of those T cell subsets whose proliferation critically depends on the activity of Kv1.3 channels.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Amino Acid Sequence
Animals
antagonists & inhibitors
Bayes Theorem
Cell Line
Cells
chemistry
Chromatography,High Pressure Liquid
Comparative Study
Electrophysiology
Enzyme-Linked Immunosorbent Assay
genetics
Human
Humans
Intermediate-Conductance Calcium-Activated Potassium Channels
Kv1.3 Potassium Channel
Lymphocytes
Mass Spectrometry
metabolism
Mexico
Models,Genetic
Molecular Sequence Data
Molecular Weight
Organophosphorus Compounds
Peptides
Phylogeny
Potassium
Potassium Channels
Research
Scorpion Venoms
Scorpions
Sequence Analysis,Protein
Support
T-Lymphocytes
toxicity
Toxins
Megjelenés:Toxicon. - 46 : 4 (2005), p. 418-429. -
További szerzők:Somodi Sándor (1977-) (belgyógyász) Fernandez, Juan Antonio Zamudio, Fernando Z. Becerril, Baltazar Varga Zoltán (1969-) (biofizikus, szakfordító) Panyi György (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Possani, Lourival Domingos
Internet cím:elektronikus változat
DOI
Borító:

12.

001-es BibID:BIBFORM046300
Első szerző:Panyi György (biofizikus)
Cím:Immunosuppressors inhibit voltage-gated potassium channels in human peripheral blood lymphocytes / Panyi G., Gaspar R., Krasznai Z., ter Horst J. J., Ameloot M., Aszalos A., Steels P., Damjanovich S.
Dátum:1996
ISSN:0006-291X
Megjegyzések:The effects of immunosuppressive agents on the potassium current of human peripheral blood lymphocytes have been studied using the whole-cell patch-clamp technique. Cyclosporin A (10 micrograms/ml), rapamycin (10 micrograms/ml) and FK-506 (2.5 micrograms/ml) reduced the peak K+ current by approximately 40, 30 and 40% of the control, respectively, without any change in the reversal potential of the current. The current inhibition was similar at all membrane potentials studied and was accompanied with an increase in the rate of K+ current inactivation. Membrane potential measurements in current-clamp showed a marked depolarization of the membrane (>10 mV) upon the addition of either immunosuppressor to the cells. Our findings revealed that the voltage-dependent potassium current in human peripheral blood lymphocytes is inhibited by Cyclosporin A and other immunosuppressors, resulting in a depolarized membrane potential.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical and Biophysical Research Communications. - 221 : 2 (1996), p. 254-258. -
További szerzők:Gáspár Rezső (1944-) (biofizikus) Krasznai Zoltán (1950-) (biofizikus) ter Horst, Jan J. Ameloot, Marcel Aszalos Adorján Steels, Paul Damjanovich Sándor (1936-2017) (biofizikus)
Pályázati támogatás:1459
OTKA
1492
OTKA
6221
OTKA
E12533
OTKA
T14655
OTKA
F13335
OTKA
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:
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