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1.

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:

2.

001-es BibID:BIBFORM004856
Első szerző:Bagossi Péter (biokémikus, vegyész)
Cím:Molecular modeling of nearly full-length ErbB2 receptor / Bagossi, P., Horvath, G., Vereb, G., Szollosi, J., Tozser, J.
Dátum:2005
ISSN:0006-3495
Megjegyzések:Members of the epidermal growth factor receptor family play important roles in various cellular processes, both in physiological and in pathological conditions. Dimerization and autophosphorylation of these receptor tyrosine kinases are key events of signal transduction. Details of the molecular events of the signaling are not entirely known. To facilitate the understanding of receptor structure and function at the molecular level, a molecular model was built for the nearly full-length ErbB2 dimer. Modeling was based on the x-ray or nuclear-magnetic resonance structures of extracellular, transmembrane, and intracellular domains. The extracellular domain was positioned above the cell membrane based on the distance determined from experimentally measured fluorescence resonance energy transfer. Favorable dimerization interactions are predicted for the extracellular, transmembrane, and protein kinase domains in the model of a nearly full-length dimer of ErbB2, which may act in a coordinated fashion in ErbB2 homodimerization, and also in heterodimers of ErbB2 with other members of the ErbB family
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Cell Line, Tumor
Cell Membrane
chemistry
Comparative Study
Computer Simulation
Dimerization
Energy Transfer
Epidermal Growth Factor
Fluorescence
Fluorescence Resonance Energy Transfer
Humans
Hungary
Lipid Bilayers
methods
Models, Chemical
Models, Molecular
Neoplasms
Protein Conformation
Protein Structure, Tertiary
Receptor, erbB-2
Research
Signal Transduction
Structure-Activity Relationship
Support
ultrastructure
Megjelenés:Biophysical Journal. - 88 : 2 (2005), p. 1354-1363. -
További szerzők:Horváth Gábor (1974-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Szöllősi János (1953-) (biofizikus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Internet cím:elektronikus változat
Borító:

3.

001-es BibID:BIBFORM084527
035-os BibID:(WoS)000375141600351
Első szerző:Balajthy András (általános orvos)
Cím:7-Dehydrocholesterol Modifies the Operation of Kv1.3 Channels in T Cells Isolated from Smith-Lemli-Opitz Syndrome Patients / Balajthy Andras, Petho Zoltan, Somodi Sandor, Varga Zoltan, Peter Maria, Vígh Laszlo, Szabó Gabriella P., Paragh Gyorgy, Panyi Gyorgy, Hajdu Peter
Dátum:2016
ISSN:0006-3495
Tárgyszavak:Orvostudományok Klinikai orvostudományok idézhető absztrakt
folyóiratcikk
Megjelenés:Biophysical Journal. - 110 : 3 (2016), p. 278a-279a. -
További szerzők:Pethő Zoltán (1989-) (orvos) Somodi Sándor (1977-) (belgyógyász) Varga Zoltán (1969-) (biofizikus, szakfordító) Péter Mária Vígh László (orvos Szeged) P. Szabó Gabriella (1975-) (csecsemő- és gyermekgyógyász, klinikai genetikus) Paragh György (1953-) (belgyógyász) Panyi György (1966-) (biofizikus) Hajdu Péter (1975-) (biofizikus)
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM049426
Első szerző:Bene László (biofizikus)
Cím:Intensity correlation-based calibration of FRET / László Bene, Tamás Ungvári, Roland Fedor, László Sasi Szabó, László Damjanovich
Dátum:2013
ISSN:0006-3495
Megjegyzések:ABSTRACT Dual-laser flow cytometric resonance energy transfer (FCET) is a statistically efficient and accurate way of determiningproximity relationships for molecules of cells even under living conditions. In the framework of this algorithm, absolutefluorescence resonance energy transfer (FRET) efficiency is determined by the simultaneous measurement of donor-quenchingand sensitized emission. A crucial point is the determination of the scaling factor a responsible for balancing the differentsensitivities of the donor and acceptor signal channels. The determination of a is not simple, requiring preparation of specialsamples that are generally different from a double-labeled FRET sample, or by the use of sophisticated statistical estimation(least-squares) procedures. We present an alternative, free-from-spectral-constants approach for the determination of a andthe absolute FRET efficiency, by an extension of the presented framework of the FCET algorithm with an analysis of the secondmoments (variances and covariances) of the detected intensity distributions. A quadratic equation for a is formulated withthe intensity fluctuations, which is proved sufficiently robust to give accurate a-values on a cell-by-cell basis in a wide systemof conditions using the same double-labeled sample from which the FRET efficiency itself is determined. This seemingly newapproach is illustrated by FRET measurements between epitopes of the MHCI receptor on the cell surface of two cell lines,FT and LS174T. The figures show that whereas the common way of a determination fails at large dye-per-protein labeling ratiosof mAbs, this presented-as-new approach has sufficient ability to give accurate results. Although introduced in a flow cytometer,the new approach can also be straightforwardly used with fluorescence microscopes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
FRET
statistically efficient
Megjelenés:Biophysical Journal. - 105 : 9 (2013), p. 2024-2035. -
További szerzők:Ungvári Tamás Fedor Roland (1975-) (sebész) Sasi Szabó László András (1974-) (sebész) Damjanovich László (1960-) (általános sebész)
Pályázati támogatás:TÁMOP-4.2.2.A-11/1/KONV-2012-0045
TÁMOP
No. ASTF No 201-06
Egyéb
Short-term EMBO fellowship
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5.

001-es BibID:BIBFORM004943
Első szerző:Gadella, Theodorus W. Jr.
Cím:Microspectroscopic imaging of nodulation factor-binding sites on living Vicia sativa roots using a novel bioactive fluorescent nodulation factor / Gadella, T. W. Jr., Vereb, G. Jr., Hadri, A. E., Rohrig, H., Schmidt, J., John, M., Schell, J., Bisseling, T.
Dátum:1997
Megjegyzések:A novel bioactive fluorescent nodulation (Nod) factor, NodRlv-IV(BODIPY FL-C16), has been synthesized by attaching a BODIPY FL-C16 acyl chain to the primary amino group of chitotetraose deacetylated at the nonreducing terminus by recombinant NodB. The binding of the fluorescent Nod factor to root systems of Vicia sativa was investigated with fluorescence spectral imaging microscopy (FSPIM) and fluorescence ratio imaging microscopy (FRIM). Spatially resolved fluorescence spectra of living and labeled Vicia sativa root systems were measured by FSPIM. Strong autofluorescence, inherent to many plant systems when excited at 488 nm, was corrected for by utilizing the difference in fluorescence emission spectra of the autofluorescence and NodRlv- IV(BODIPY FL-C16). A methodology is presented to break down the in situ fluorescence emission spectra into spatially resolved autofluorescence and BODIPY FL fluorescence spectra. Furthermore, an FRIM method was developed for correcting autofluorescence in fluorescence micrographs for this system. After autofluorescence correction it was shown that NodRlv-IV(BODIPY FL-C16) was concentrated in the root hairs, but was also bound to other parts of the root surface.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Binding Sites
chemistry
Fluorescence
methods
Microscopy
Non-U.S.Gov't
Plant Proteins
Spectrometry
Support
Megjelenés:Biophysical Journal 72 : 5 (1997), p. 1986-1996. -
További szerzők:Vereb György (1965-) (biofizikus, orvos) Hadri, Azz-Eddine Röhrig, Horst Schmidt, Jürgen John, Michael Schell, Jeff Bisseling, Ton
Internet cím:elektronikus változat
Borító:

6.

001-es BibID:BIBFORM004727
Első szerző:Hajdu Péter (biofizikus)
Cím:Drug- and mutagenesis-induced changes in the selectivity filter of a 2-pore background K+ channel / Hajdu, P., Ulens, C., Panyi, G., Tytgat, J.
Dátum:2003
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:Biophysical Journal. - 84 : 2 (2003), p. 93A. -
További szerzők:Ulens, Chris Panyi György (1966-) (biofizikus) Tytgat, Jan
Borító:

7.

001-es BibID:BIBFORM004648
Első szerző:Jenei Attila (biofizikus)
Cím:Picosecond multiphoton scanning near-field optical microscopy / Jenei, A., Kirsch, A. K., Subramaniam, V., Arndt-Jovin, D. J., Jovin, T. M.
Dátum:1999
Megjegyzések:We have implemented simultaneous picosecond pulsed two- and three-photon excitation of near-UV and visible absorbing fluorophores in a scanning near-field optical microscope (SNOM). The 1064-nm emission from a pulsed Nd:YVO4 laser was used to excite the visible mitochondrial specific dye MitoTracker Orange CM-H2TMRos or a Cy3-labeled antibody by two-photon excitation, and the UV absorbing DNA dyes DAPI and the bisbenzimidazole BBI-342 by three-photon excitation, in a shared aperture SNOM using uncoated fiber tips. Both organelles in human breast adenocarcinoma cells (MCF 7) and specific protein bands on polytene chromosomes of Drosophila melanogaster doubly labeled with a UV and visible dye were readily imaged without photodamage to the specimens. The fluorescence intensities showed the expected nonlinear dependence on the excitation power over the range of 5-40 mW. An analysis of the dependence of fluorescence intensity on the tip-sample displacement normal to the sample surface revealed a higher-order function for the two-photon excitation compared to the one-photon mode. In addition, the sample photobleaching patterns corresponding to one- and two-photon modes revealed a greater lateral confinement of the excitation in the two-photon case. Thus, as in optical microscopy, two-photon excitation in SNOM is confined to a smaller volume
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Animal
Antibodies
Cells
chemistry
Chromosomes
Dna
Drosophila melanogaster
Dyes
Fluorescence
Fluorescent Dyes
genetics
Human
Lasers
metabolism
methods
Microscopy
Microscopy, Fluorescence
Mitochondria
Photons
Support, Non-U.S.Gov't
Tumor Cells,Cultured
ultrastructure
Ultraviolet Rays
külföldön készült közlemény
Megjelenés:Biophysical Journal. - 76 : 2 (1999), p. 1092-1100. -
További szerzők:Kirsch, Achim K. Subramaniam, Vinod Arndt-Jovin, Donna J. Jovin, Thomas M.
Internet cím:elektronikus változat
DOI
Borító:

8.

001-es BibID:BIBFORM079020
035-os BibID:(absztrakt azonosító)1849-Plat (WoS)000430450000363
Első szerző:Karbat, Izhar
Cím:An Allosteric Action Mechanism of a K+ Pore Blocker Revealed at the Atomic Level / Izhar Karbat, Hagit Altman-Gueta, G. Tibor Szántó, Shelly Hamer-Rogotner, Orly Dym, Felix Frolow, Dalia Gordon, Gyorgy Panyi, Michael Gurevitz, Eitan Reuveny
Dátum:2018
ISSN:0006-3495
Megjegyzések:Voltage gated ion channels gate in response to changes in the electrical membrane potential by the coupling of a voltage sensing module with an ion-selective pore. Toxins that target these channels are traditionally classified as either pore-blockers or gating-modifiers, the former bind and physically occlude the channel pore, while the later bind the voltage sensing module and restrict its movement in response to alterations in the membrane potential. Here we present Cs1, a kunitz-fold cone-snail toxin that blocks the Drosophila Shaker isoform with high affinity and seem to defy the traditional classification. We first obtained high resolution crystal structures of Cs1 and several of its mutants. Then, using site directed mutagenesis followed by double-mutant cycle analysis we identified key residue pairs in contact at the toxin-channel interface, which was clearly confined to the channel pore-module. Unconstrained rigid docking followed by a whole-atom molecular dynamics simulations yielded a model that was consistent with the experimental results, in which the toxin was bound off the pore axis and allowed the access of water molecules to the pore. Electrophysiological assays established that Cs1 does not dissociate from its binding site upon depolarization, and that its affinity for the channel is independent of the external K+ concentration, further setting it apart from the classical pore-blockers. Analysis of our MD simulations suggest that Cs1 blocks ion conductance using a novel allosteric mechanism that directly involves structural water molecules buried behind the selectivity filter of the channel.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
folyóiratcikk
Megjelenés:Biophysical Journal. - 114 : 3 (2018), p. 375a. -
További szerzők:Altman-Gueta, Hagit Szántó Gábor Tibor (1980-) (vegyész) Hamer-Rogotner, Shelly Dym, Orly Frolow, Felix Gordon, Dalia Panyi György (1966-) (biofizikus) Gurevitz, Michael Reuveny, Eitan
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Borító:

9.

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)
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Borító:

10.

001-es BibID:BIBFORM075364
035-os BibID:(WoS)000432700300024 (Scopus)85046862526
Első szerző:Nagy Éva (molekuláris biológus)
Cím:Membrane Potential Distinctly Modulates Mobility and Signaling of IL-2 and IL-15 Receptors in T Cells / Éva Nagy, Gábor Mocsár, Veronika Sebestyén, Julianna Volkó, Ferenc Papp, Katalin Tóth, Sándor Damjanovich, György Panyi, Thomas A. Waldmann, Andrea Bodnár, György Vámosi
Dátum:2018
ISSN:0006-3495
Megjegyzések:The high electric ?eld across the plasma membrane might in?uence the conformation and behavior of transmembrane proteins that have uneven charge distributions in or near their transmembrane regions. Membrane depolarization of T cells occurs in the tumor microenvironment and in in?amed tissues because of K ? release from necrotic cells and hypoxia affecting the expression of K ? channels. However, little attention has been given to the effect of membrane potential (MP) changes on membrane receptor function. Therefore, we studied the in?uence of membrane de- and hyperpolarization on the biophysical properties and signaling of interleukin-2 (IL-2) and interleukin-15 (IL-15) receptors, which play important roles in T cell function. We investigated the mobility, clustering, and signaling of these receptors and major histocompatibility complex (MHC) I/II glycoproteins forming coclusters in lipid rafts of T cells. Depolarization by high K ? buffer or K channel blockers resulted in a decrease in the mobility of IL-2Ra and MHC glycoproteins, as shown by ?uorescence correlation spectroscopy, whereas hyperpolarization by the K ? ionophore valinomycin increased their mobility. Contrary to this, the mobility of IL-15Ra decreased upon both de- and hyperpolarization. These changes in protein mobility are not due to an alteration of membrane ?uidity, as evidenced by ?uorescence anisotropy measurements. Fo ? rster resonance energy transfer measurements showed that most homo- or heteroassociations of IL-2R, IL-15R, and MHC I did not change considerably, either. MP changes modulated signaling by the two cytokines in distinct ways: depolarization caused a signi?cant increase in the IL-2-induced phosphorylation of signal transducer and activator of transcription 5, whereas hyperpolarization evoked a decrease only in the IL-15-induced signal. Our data imply that the MP may be an important modulator of interleukin receptor signaling and dynamics. Enhanced IL-2 signaling in depolarized T reg ? cells highly expressing IL-2R may contribute to suppression of antitumor immune surveillance
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Biophysical Journal. - 114 : 10 (2018), p. 2473-2482. -
További szerzők:Mocsár Gábor (1981-) (biofizikus) Borbásné Sebestyén Veronika (1990-) (biofizikus) Volkó Julianna (1983-) (biotechnológus) Papp Ferenc (1979-) (biofizikus) Tóth Katalin (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Panyi György (1966-) (biofizikus) Waldmann, Thomas A. Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus)
Pályázati támogatás:GINOP-2.3.2-15-2016-00026
GINOP
GINOP-2.3.3-15-2016-00003
GINOP
GINOP-2.3.3-15-2016-00030
GINOP
K103965
OTKA
EFOP-3.6.1-16-2016-00022
EFOP
K119417
OTKA
TÁMOP-4.2.4.A/2-11/1-2012-0001
TÁMOP
EFOP-3.6.3-VEKOP-16-2017-00009
EFOP
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Borító:

11.

001-es BibID:BIBFORM072316
035-os BibID:(WoS)000425895600022 (Scopus)85041571964
Első szerző:Nagyné Szabó Ágnes Timea (vegyész)
Cím:The Effect of Fluorophore Conjugation on Antibody Affinity and the Photophysical Properties of Dyes / Szabó Ágnes, Szendi-Szatmári Tímea, Ujlaky-Nagy László, Rádi Ildikó, Vereb György, Szöllősi János, Nagy Peter
Dátum:2018
ISSN:0006-3495
Megjegyzések:Because the degree of labeling (DOL) of cell-bound antibodies, often required in quantitative fluorescence measurements, is largely unknown, we investigated the effect of labeling with two different fluorophores (AlexaFluor546, AlexaFluor647) in a systematic way using antibody stock solutions with different DOLs. Here, we show that the mean DOL of the cell-bound antibody fraction is lower than that of the stock using single molecule fluorescence measurements. The effect is so pronounced that the mean DOL levels off at approximately two fluorophores/IgG for some antibodies. We developed a method for comparing the average DOL of antibody stocks to that of the isolated, cell-bound fraction based on fluorescence anisotropy measurements confirming the aforementioned conclusions. We created a model in which individual antibody species with different DOLs, present in an antibody stock solution, were assumed to have distinct affinities and quantum yields. The model calculations confirmed that a calibration curve constructed from the anisotropy of antibody stocks can be used for determining the DOL of the bound fraction. The fluorescence intensity of the cell-bound antibody fractions and of the antibody stocks exhibited distinctly different dependence on the DOL. The behavior of the two dyes was systematically different in this respect. Fitting of the model to these data revealed that labeling with each dye affects quantum yield and antibody affinity differentially. These measurements also implied that fluorophores in multiply labeled antibodies exhibit self-quenching and lead to decreased antibody affinity, conclusions directly confirmed by steady-state intensity measurements and competitive binding assays. Although the fluorescence lifetime of antibodies labeled with multiple fluorophores decreased, the magnitude of this change was not sufficient to account for self-quenching indicating that both dynamic and static quenching processes occur involving H-aggregate formation. Our results reveal multiple effects of fluorophore conjugation, which must not be overlooked in quantitative cell biological measurements.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Biophysical Journal. - 114 : 3 (2018), p. 688-700. -
További szerzők:Szendi-Szatmári Tímea (1989-) (molekuláris biológus) Ujlaky-Nagy László (1977-) (biofizikus) Rádi Ildikó Vereb György (1965-) (biofizikus, orvos) Szöllősi János (1953-) (biofizikus) Nagy Péter (1971-) (biofizikus)
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Borító:

12.

001-es BibID:BIBFORM012846
Első szerző:Nagyné Szabó Ágnes Timea (vegyész)
Cím:Coclustering of ErbB1 and ErbB2 Revealed by FRET-Sensitized Acceptor Bleaching / Szabó Ágnes, Szöllősi János, Nagy Péter
Dátum:2010
ISSN:0006-3495
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biophysical Journal. - 99 : 1 (2010), p. 105-114. -
További szerzők:Szöllősi János (1953-) (biofizikus) Nagy Péter (1971-) (biofizikus)
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