CCL

Összesen 10 találat.
#/oldal:
Részletezés:
Rendezés:

1.

001-es BibID:BIBFORM099008
035-os BibID:(cikkazonosító)12974 (scopus)85120073703 (wos)000735015000001
Első szerző:Csomós István (molekuláris biológus)
Cím:Opposing Effects of Chelidonine on Tyrosine and Serine Phosphorylation of STAT3 in Human Uveal Melanoma Cells / Csomós István, Nagy Péter, Filep Csenge, Rebenku István, Nizsalóczki Enikő, Kovács Tamás, Vámosi György, Mátyus László, Bodnár Andrea
Dátum:2021
ISSN:1661-6596 1422-0067
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:International Journal Of Molecular Sciences. - 22 : 23 (2021), p. 1-14. -
További szerzők:Nagy Péter (1971-) (biofizikus) Filep Csenge Boróka (1993-) (biomérnök) Rebenku István Nizsalóczki Enikő Kovács Tamás (1985-) (általános orvos) Vámosi György (1967-) (biofizikus) Mátyus László (1956-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus)
Pályázati támogatás:EFOP-3.6.3-VEKOP-16-2017-00009
EFOP
K 138075
OTKA
ANN 135107
Egyéb
ANN 133421
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

2.

001-es BibID:BIBFORM004705
035-os BibID:(scopus)18544371851 (wos)000173421300040
Első szerző:Dornan, Saffron
Cím:Differential association of CD45 isoforms with CD4 and CD8 regulates the actions of specific pools of p56lck tyrosine kinase in T cell antigen receptor signal transduction / Dornan, S., Sebestyen, Z., Gamble, J., Nagy, P., Bodnar, A., Alldridge, L., Doe, S., Holmes, N., Goff, L. K., Beverley, P., Szollosi, J., Alexander, D. R.
Dátum:2002
Megjegyzések:An investigation into the role of CD45 isoforms in T cell antigen receptor signal transduction was carried out by transfecting CD45-negative CD4(+)CD8(+) HPB-ALL T cells with the CD45R0, CD45RBC, and CD45RABC isoforms. Fluorescence resonance energy transfer analysis showed that the CD45R0 isoform, but not the CD45RBC or CD45RABC isoforms, was found as homodimers and also preferentially associated with CD4 and CD8 at the cell-surface. A comparison was therefore made of T cell antigen receptor signaling between sub-clones expressing either CD45R0 or CD45RBC. Under basal conditions CD4-associated p56(lck) tyrosine kinase activity and cellular protein tyrosine phosphorylation levels were higher in the CD45R0(+) than in the CD45RBC(+) sub-clones. Upon CD3-CD4 ligation, TCR-zeta phosphorylation, ZAP-70 recruitment to the p21/p23 TCR-zeta phosphoisomers, ZAP-70 phosphorylation, as well as p56(lck), c-Cbl and Slp-76 phosphorylation, were all markedly increased in CD45R0(+) compared with CD45RBC(+) cells. T cell antigen receptor (TCR) stimulation alone also promoted c-Cbl phosphorylation in CD45R0(+) but not in CD45RBC(+) cells. Our results are consistent with a model in which association of CD45R0 with CD4 generates a more active pool of CD4-associated p56(lck) kinase molecules. Upon CD3-CD4 co-ligation, the active p56(lck) increases the intensity of T cell antigen receptor signal transduction coupling by promoting TCR-zeta chain phosphorylation and ZAP-70 recruitment.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
analysis
Antigens,CD4
Antigens,CD45
Antigens,CD8
Energy Transfer
Fluorescence
Human
immunology
Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
metabolism
Phosphorylation
Receptors,Antigen,T-Cell
Signal Transduction
Support,Non-U.S.Gov't
Megjelenés:The Journal of Biological Chemistry. - 277 : 3 (2002), p. 1912-1918. -
További szerzők:Sebestyén Zsolt Gamble, John Nagy Péter (1971-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Alldridge, Lou Doe, Senam Holmes, Nick Goff, Lindsey K. Beverley, Peter Szöllősi János (1953-) (biofizikus) Alexander, Denis R.
Internet cím:elektronikus változat
elektronikus változat
Borító:

3.

001-es BibID:BIBFORM023492
Első szerző:Matkó János (biológus)
Cím:Analysis of cell surface molecular distributions and cellular signaling by flow cytometry / J. Matkó, L. Mátyus, J. Szöllősi, L. Bene, A. Jenei, P. Nagy, A. Bodnár, S. Damjanovich
Dátum:1994
ISSN:1053-0509
Megjegyzések:Flow cytometry is a fast analysis and separation method for large cell populations, based on collection and processing of optical signals gained on a cell-by-cell basis. These optical signals are scattered light and fluorescence. Owing to its unique potential ofStatistical data analysis and sensitive monitoring of (micro)heterogeneities in large cell populations, flow cytometry?in combination with microscopic imaging techniques?is a powerful tool to study molecular details of cellular signal transduction processes as well. The method also has a widespread clinical application, mostly in analysis of lymphocyte subpopulations for diagnostic (or research) purposes in diseases related to the immune system. A special application of flow cytometry is the mapping of molecular interactions (proximity relationships between membrane proteins) at the cell surface, on a cell-by-cell basis. We developed two approaches to study such questions; both are based ondistance-dependent quenching of excited state fluorophores (donors) by fluorescent or dark (nitroxide radical) acceptors via Förstertype dipole-dipole resonance energy transfer (FRET) and long-range electron transfer (LRET) mechanisms, respectively. A critical evaluation of these methods using donor- or acceptor-conjugated monoclonal antibodies (or their Fab fragments) to select the appropriate cell surface receptor or antigen will be presented in comparison with other approaches for similar purposes. The applicability of FRET and LRET for two-dimensional antigen mapping as well as for detection of conformational changes in extracellular domains of membrane-bound proteins is discussed and illustrated by examples of several lymphoma cell lines. Another special application area of flow cytometry is the analysis of different aspects of cellular signal transduction, e.g., changes of intracellular ion (Ca2+, H+, Na+) concentrations, regulation of ion channel activities, or more complex physiological responses of cell to external stimuli via correlated fluorescence and scatter signal analysis, on a cell-by-cell basis. This way different signaling events such as changes in membrane permeability, membrane potential, cell size and shape, ion distribution, cell density, chromatin structure, etc., can be easily and quickly monitored over large cell populations with the advantage of revealing microheterogeneities in the cellular responses. Flow cytometry also offers the possibility to follow the kinetics of slow (minute- and hour-scale) biological processes in cell populations. These applications are illustrated by the example of complex flow cytometric analysis of signaling in extracellular ATP-triggered apoptosis (programmed cell death) of murine thymic lymphocytes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
fluorescence
flow cytometry
energy transfer
electron transfer
protein-protein interaction
signal transduction
egyetemen (Magyarországon) készült közlemény
Megjelenés:Journal Of Fluorescence 4 : 4 (1994), p. 303-314. -
További szerzők:Mátyus László (1956-) (biofizikus) Szöllősi János (1953-) (biofizikus) Bene László (1963-) (biofizikus) Jenei Attila (1966-) (biofizikus) Nagy Péter (1971-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változa
Borító:

4.

001-es BibID:BIBFORM065104
035-os BibID:(WoS)000380371400013 (Scopus)84993661764
Első szerző:Mocsár Gábor (biofizikus)
Cím:MHC I expression regulates co-clustering and mobility of interleukin-2 and -15 receptors in T cells / G. Mocsár, J. Volkó, D. Rönnlund, J. Widengren, P. Nagy, J. Szöllősi, K. Tóth, C. K. Goldman, S. Damjanovich, T. A. Waldmann, A. Bodnár, G. Vámosi
Dátum:2016
ISSN:0006-3495
Megjegyzések:MHC glycoproteins form supramolecular clusters with interleukin-2 and -15 receptors in lipid rafts of T cells.The role of highly expressed MHC I in maintaining these clusters is unknown. We knocked down MHC I inFT7.10 human T cells, and studied protein clustering at two hierarchic levels: molecular aggregations andmobility by FRET and fluorescence correlation spectroscopy, and segregation into larger domains orsuperclusters by superresolution STED microscopy. FCS based molecular brightness analysis revealed thatthe studied molecules diffused as tight aggregates of several proteins of a kind. Knockdown reduced thenumber of MHC I containing molecular aggregates and their average MHC I content, and decreased theheteroassociation of MHC I with IL-2R?/IL-15R?. The mobility of not only MHC I but also that of IL-2R?/IL-15R? increased, corroborating the general size decrease of tight aggregates. A multifaceted analysis of STEDimages revealed that the diameter of MHC I superclusters diminished from 400-600 to 200-300 nm, whereasthose of IL-2R?/IL-15R? hardly changed. MHC I and IL-2R?/IL-15R? colocalized with GM1 gangliosiderichlipid rafts, but MHC I clusters retracted to smaller subsets of GM1- and IL-2R?/IL-15R?-rich areas uponknockdown. Our results prove that changes in expression level may significantly alter the organization andmobility of interacting membrane proteins.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Biophysical Journal. - 111 : 1 (2016), p. 100-112. -
További szerzők:Volkó Julianna (1983-) (biotechnológus) Rönnlund, Daniel Widengren, Jerker Nagy Péter (1971-) (biofizikus) Szöllősi János (1953-) (biofizikus) Tóth Katalin (Heidelberg) Goldman, Caroline K. Damjanovich Sándor (1936-2017) (biofizikus) Waldmann, Thomas A. Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus)
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

5.

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:

6.

001-es BibID:BIBFORM076128
035-os BibID:(Wos)000450299400006 (Scopus)85055751019
Első szerző:Nizsalóczki Enikő
Cím:Minimum degree of overlap between IL-9R and IL-2R on human T lymphoma cells : a quantitative CLSM and FRET analysis / Nizsalóczki Enikő, Nagy Péter, Mocsár Gábor, Szabó Ágnes, Csomós István, Waldmann Thomas A., Vámosi György, Mátyus László, Bodnár Andrea
Dátum:2018
ISSN:1552-4922 1552-4930
Megjegyzések:The heterodimeric receptor complex of IL-9 consists of the cytokine-speci?c ?-subunit and the common ? -chain shared with other cytokines, including IL-2, a central regulator of T cell function. We have shown previously the bipartite spatial relationship of IL-9 and IL-2 receptors at the surface of human T lymphoma cells: in addition to common clusters, expression of the two receptor kinds could also be observed in segregated membrane areas. Here we analyzed further the mutual cell surface organization of IL-9 and IL-2 receptors. Complementing Pearson correlation data with co-occurrence analysis of confocal microscopic images revealed that a minimum degree of IL-9R/IL-2R co-localization exists at the cell surface regardless of the overall spatial correlation of the two receptor kinds. Moreover, our FRET experiments demonstrated molecular scale assemblies of the elements of the IL-9/IL-2R system. Binding of IL-9 altered the structure and/or composition of these clusters. It is hypothesized, that by sequestering receptor subunits in common membrane areas, the overlapping domains of IL-9R and IL-2R provide a platform enabling both the formation of the appropriate receptor complex as well as subunit sharing between related cytokines.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
IL-9 and -2 receptors
uorescence resonance energy transfer
Manders coef-cient
co-occurrence analysis
Pearson correlation analysis
confocal microscopy
human T lymphoma cells
co-localization of membrane proteins
Megjelenés:Cytometry Part A. - 93 : 11 (2018), p. 1106-1117. -
További szerzők:Nagy Péter (1971-) (biofizikus) Mocsár Gábor (1981-) (biofizikus) Nagyné Szabó Ágnes Timea (1982-) (vegyész) Csomós István (1983-) (molekuláris biológus) Waldmann, Thomas A. Vámosi György (1967-) (biofizikus) Mátyus László (1956-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus)
Pályázati támogatás:EFOP-3.6.3-VEKOP-16-2017-00009
EFOP
GINOP-2.3.2-15-2016-00026
GINOP
GINOP-2.3.3-15-2016-00003
GINOP
K120302
OTKA
Intramural research program of the National Cancer Institute, NIH
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

7.

001-es BibID:BIBFORM057902
Első szerző:Nizsalóczki Enikő
Cím:Distinct spatial relationship of the interleukin-9 receptor with interleukin-2 receptor and major histocompatibility complex glycoproteins in human T lymphoma cells / Enikő Nizsalóczki, István Csomós, Péter Nagy, Zsolt Fazekas, Carolyn K. Goldman, Thomas A. Waldmann, Sándor Damjanovich, György Vámosi, László Mátyus, Andrea Bodnár
Dátum:2014
ISSN:1439-4235
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
confocal microscopy
membrane proteins
FRET
protein protein interactions
receptors
Molekuláris Medicina
Doktori iskola
Megjelenés:Chemphyschem. - 15 : 18 (2014), p. 3969-3978. -
További szerzők:Csomós István (1983-) (molekuláris biológus) Nagy Péter (1971-) (biofizikus) Fazekas Zsolt (1971-) (biofizikus) Goldman, Caroline K. Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus) Vámosi György (1967-) (biofizikus) Mátyus László (1956-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Sejtfelszíni fehérjék szerveződése: az MHC I. szerepe
TÁMOP-4.2.2/B-10/1-2010-0024
TÁMOP
Molekuláris Orvostudomány Doktori Iskola
TÁMOP-4.2.2.A-11/1/KONV-2012-0023
TÁMOP
TÁMOP-4.2.2.A-11/1/KONV-2012-0025
TÁMOP
TÁMOP-4.2.4.A/2-11/1-2012-0001
TÁMOP
CK 78179
OTKA
K 103965
OTKA
K 103906
OTKA
NK 101337
OTKA
Baross Gábor Program REG-EA-09-1-2009-0010
Egyéb
Internal Research Program of the University of Debrecen RH/885/2013
Egyéb
Intramural Research Program of the National Cancer Institute, National Institutes of Health
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

8.

001-es BibID:BIBFORM004690
035-os BibID:(scopus)0035191769 (wos)000172278000004
Első szerző:Pfeiffer, Alexandra
Cím:Lipopolysaccharide and ceramide docking to CD14 provokes ligand-specific receptor clustering in rafts / Pfeiffer, A., Bottcher, A., Orso, E., Kapinsky, M., Nagy, P., Bodnar, A., Spreitzer, I., Liebisch, G., Drobnik, W., Gempel, K., Horn, M., Holmer, S., Hartung, T., Multhoff, G., Schutz, G., Schindler, H., Ulmer, A. J., Heine, H., Stelter, F., Schutt, C., Rothe, G., Szollosi, J., Damjanovich, S., Schmitz, G.
Dátum:2001
Megjegyzések:The glycosylphosphatidylinositol-anchored receptor CD14 plays a major role in the inflammatory response of monocytes to lipopolysaccharide. Here, we describe that ceramide, a constituent of atherogenic lipoproteins, binds to CD14 and induces clustering of CD14 to co-receptors in rafts. In resting cells, CD14 was associated with CD55, the Fcgamma-receptors CD32 and CD64 and the pentaspan CD47. Ceramide further recruited the complement receptor 3 (CD11b/CD18) and CD36 into proximity of CD14. Lipopolysaccharide, in addition, induced co-clustering with Toll-like receptor 4, Fcgamma-RIIIa (CD16a) and the tetraspanin CD81 while CD47 was dissociated. The different receptor complexes may be linked to ligand-specific cellular responses initiated by CD14.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Antigens,CD
Antigens,CD14
Carrier Proteins
Ceramides
chemistry
Glycoproteins
Human
Inflammation
Ligands
Lipopolysaccharides
Macrophage-1 Antigen
Membrane Glycoproteins
Membrane Microdomains
metabolism
Monocytes
pharmacology
Receptors,Cell Surface
Support,Non-U.S.Gov't
Megjelenés:European Journal of Immunology. - 31 : 11 (2001), p. 3153-3164. -
További szerzők:Böttcher, Alfred Orsó Evelyn Kapinsky, Michael Nagy Péter (1971-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Spreitzer, Ingo Liebisch, Gerhard Drobnik, Wolfgang Gempel, Klaus Horn, Markus Holmer, Stefan Hartung, Thomas Multhoff, Gabriele Schütz, Gerhard Schindler, Hansgeorg Ulmer, Artur J. Heine, Holger Stelter, Felix Schütt, Christine Rothe, Gregor Szöllősi János (1953-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Schmitz, Gerd
Internet cím:DOI
Borító:

9.

001-es BibID:BIBFORM005107
Első szerző:Vámosi György (biofizikus)
Cím:The role of supramolecular protein complexes and membrane potential in transmembrane signaling processes of lymphocytes / Vamosi, G., Bodnar, A., Damjanovich, S., Nagy, P., Varga, Z., Damjanovich, L.
Dátum:2006
ISSN:165-2478 (Print)
Megjegyzések:The formation of protein patterns in lymphocyte plasma membranes is analyzed in the light of past and, also, very recent experiments. The analysis surveys the lateral organization of major histocompatibility complex glycoproteins, intercellular adhesion molecule-1, interleukin-2 and -15 receptors, Kv1.3 K+ ion channels and the T-cell receptor as well as their behavior under different conditions. These molecules form small- and large-scale clusters in the membrane of human lymphocytes. Many of the association motifs occur in other investigated cell types. The conclusions point toward a possible role for ion channel activities, membrane potential changes and alterations of the lateral organization of proteins in transmembrane signaling and cytotoxic interactions. In our outlook new factors that potentially affect membrane protein cluster formation and interactions are discussed. A role for MHC glycoproteins in concentrating membrane proteins and organizing protein patterns is suggested, and the possibility that the membrane potential may modulate protein conformation and, thereby, affect protein-protein interactions is pointed out. A well-defined role for the presence of ion channels in the immune synapse is offered, which could explain the significance of ion channel accumulation in the immune synapse together with the T-cell receptor.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Animals
Biophysics
Cell Membrane
Glycoproteins
Human
Humans
Hungary
immunology
Intercellular Adhesion Molecule-1
Interleukin-2
Ion Channels
Light
Lymphocytes
Major Histocompatibility Complex
Membrane Potentials
Membrane Proteins
metabolism
Multiprotein Complexes
physiology
Protein Conformation
Proteins
Research
Signal Transduction
Support
T-Lymphocytes
Megjelenés:Immunology Letters. - 104 : 1-2 (2006), p. 53-58. -
További szerzők:Dóczy-Bodnár Andrea (1970-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Nagy Péter (1971-) (biofizikus) Varga Zoltán (1969-) (biofizikus, szakfordító) Damjanovich László (1960-) (általános sebész)
Internet cím:DOI
elektronikus változat
Borító:

10.

001-es BibID:BIBFORM036992
Első szerző:Volkó Julianna (biotechnológus)
Cím:MHC I organizes protein clusters and inhibits IL-2/IL-15 signaling in human T cells / Volkó Julianna, Mocsár Gábor, Menczel Enikő, Nagy Péter, 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. 86-86. -
További szerzők:Mocsár Gábor (1981-) (biofizikus) Menczel Enikő (1989-) (molekuláris biológus) Nagy Péter (1971-) (biofizikus) Tóth Katalin Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Fehérje-fehérje kölcsönhatások limfociták membránjában és a sejtmagban
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
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Rekordok letöltése1