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1.

001-es BibID:	BIBFORM006027
Első szerző:	Bene László (biofizikus)
Cím:	Lateral organization of the ICAM-1 molecule at the surface of human lymphoblasts : a possible model for its co-distribution with the IL-2 receptor, class I and class II HLA molecules / Bene L., Balázs M., Matkó J., Möst J., Dierich M. P., Szöllösi J., Damjanovich S.
Dátum:	1994
Megjegyzések:	Lateral distribution of the ICAM-1 molecule and its topological relationship (mutual proximity) to the heavy and light chains of class I HLA molecules, HLA-DR and interleukin-2 receptor alpha-chain (IL-2R alpha) were studied in the plasma membrane of HUT-102B2 T and JY B lymphoblastoid cell lines by the technique of flow cytometric energy transfer (FCET). Effects of adherency and treatments with recombinant interferon-gamma or tumor necrosis factor-alpha on the relative expression level of ICAM-1 to the above cell surface proteins were also investigated. While the cytokines did not significantly affect the ICAM-1 level of either cell line, an increased ICAM-1 expression was found on adherent JY cells. The ICAM-1 expression varied significantly with the cell cycle and culture conditions, as well. The statistical analysis of the differences observed in the energy transfer efficiency histograms resulted in a possible model of lateral co-distribution of these proteins in the plasma membrane. These two-dimensional patterns proved to be different for T and B lymphoma lines. ICAM-1 molecules showed a high degree of self-association on HUT-102B2 (T) cells, while they were mainly expressed as monomers on the surface of JY (B) cells. Both cells showed a significant (ca. 30%) difference between densities of the heavy and light chains of class I HLA antigen, suggesting a substantial amount of beta 2-microglobulin free heavy chains on these cell lines. The class I HLA molecules also showed partial self-association, but on both cell lines. The beta 2-microglobulin and the heavy chain of the class I HLA showed strongly different proximities to the IL-2R alpha, HLA-DR and ICAM-1 molecules, indicating that their orientations relative to the other proteins are dissimilar. IL-2R alpha molecules of the HUT-102B2 (T) cells are located mostly in the vicinity of the beta 2-microglobulin. In contrast, the local density of HLA-DR antigens is higher in the proximity of the heavy chain than in the vicinity of the beta 2-microglobulin. The possible functional significance of these protein patterns is also discussed herein.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban analysis Antibodies,Monoclonal B-Lymphocyte Subsets beta 2-Microglobulin Cell Adhesion Cell Adhesion Molecules Cell Cycle Cell Line Energy Transfer Flow Cytometry Histocompatibility Antigens Class I HLA Antigens HLA-D Antigens HLA-DR Antigens Human Hungary immunology Intercellular Adhesion Molecule-1 Interferon Type II Interleukin-2 Light physiology Receptors,Interleukin-2 Support,Non-U.S.Gov't Support,U.S.Gov't,Non-P.H.S. T-Lymphocyte Subsets Tumor Necrosis Factor
Megjelenés:	European Journal of Immunology. - 24 : 9 (1994), p. 2115-2123. -
További szerzők:	Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Matkó János (1952-) (biológus) Most, J. Dierich, Manfred P. Szöllősi János (1953-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
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2.

001-es BibID:	BIBFORM005968
035-os BibID:	(scopus)0023260317
Első szerző:	Damjanovich Sándor (biofizikus)
Cím:	Cyclosporin depolarizes human lymphocytes : earliest observed effect on cell metabolism / S. Damjanovich, A. Aszalos, S. A. Mulhern, J. Szollosi, M. Balazs, L. Tron, M. J. Fulwyler
Dátum:	1987
Megjegyzések:	Cyclosporin A (CsA) produced dose-dependent membrane depolarization of human peripheral blood lymphocytes. The phenomenon was investigated applying the membrane potential probe dihexyloxacarbocyanine iodide in a flow cytometer in combination with ionophores, hormones and monoclonal antibodies binding to different subclasses of lymphocytes and the anti-interleukin 2 receptor antibody. Human interferon-gamma abolished the depolarizing effect of cyclosporin on lymphocytes. Interleukin 2 caused depolarization and also enhanced the effect of CsA. OKT4 and OKT8 monoclonal antibodies slightly hindered depolarization by CsA while OKT3, OKT11 and OKIa1 antibodies had no such effect. Valinomycin decreased CsA's effect on the membrane potential while the ionophore A-23187 and ionomycin caused depolarizations that were additive with CsA's. CsA treatment released the isotope from 42K-loaded human lymphocytes in a dose-dependent fashion. CsA addition increased intracellular calcium content. CsA decreased the motional freedom of a spin probe in the membrane, but did not hinder the binding of fluoresceinated antibodies to the cell surface. These results suggest immediate alteration in membrane structure upon CsA treatment, causing potassium leakage and calcium ion uptake. These are the earliest detected effects of CsA on cells so far.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Antibodies,Monoclonal blood Calcium Carbocyanines Cell Membrane classification Cyclosporins Cytoplasm Dimethyl Sulfoxide drug effects Electron Spin Resonance Spectroscopy Flow Cytometry Human immunology Interferon Type II Interleukin-2 Intracellular Membranes Ion Channels Ionomycin Ionophores Lymphocytes Membrane Fluidity Membrane Potentials metabolism methods pharmacology Potassium Potassium Radioisotopes Spectrometry,Fluorescence ultrastructure Valinomycin
Megjelenés:	European Journal of Immunology. - 17 : 6 (1987), p. 763-768. -
További szerzők:	Aszalos Adorján Mulhern, Sally Szöllősi János (1953-) (biofizikus) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Trón Lajos (1941-) (biofizikus) Fulwyler, Mack J.
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3.

001-es BibID:	BIBFORM060604
035-os BibID:	(scopus)0035871630 (wos)000170948300037
Első szerző:	Gáspár Rezső (biofizikus)
Cím:	Clustering of class I HLA oligomers with CD8 and TCR: three-dimensional models based on fluorescence resonance energy transfer and crystallographic data / Rezső Gáspár Jr., Péter Bagossi, László Bene, János Matkó, János Szöllősi, József Tőzsér, László Fésüs, Thomas A. Waldmann, Sándor Damjanovich
Dátum:	2001
Megjegyzések:	Fluorescence resonance energy transfer (FRET) data, in accordance with lateral mobility measurements, suggested the existence of class I HLA dimers and oligomers at the surface of live human cells, including the B lymphoblast cell line (JY) used in the present study. Intra- and intermolecular class I HLA epitope distances were measured on JY B cells by FRET using fluorophoreconjugated Ag-binding fragments of mAbs W6/32 and L368 directed against structurally well-characterized heavy and light chain epitopes, respectively. Out-of-plane location of these epitopes relative to the membrane-bound BODIPY-PC (2-(4,4-difluoro-5-(4- phenyl-1,3-butadienyl)-4-bora-3a,4a-diaza-s-indacene-3-pentanoyl)-1-hexadecanoyl-sn-glycero-3-phosphocholine) was also determined by FRET. Computer-simulated docking of crystallographic structures of class I HLA and epitope-specific Ag-binding fragments, with experimentally determined interepitope and epitope to cell surface distances as constraints, revealed several sterically allowed and FRET-compatible class I HLA dimeric and tetrameric arrangements. Extension of the tetrameric class I HLA model with interacting TCR and CD8 resulted in a model of a supramolecular cluster that may exist physiologically and serve as a functionally significant unit for a network of CD8-HLA-I complexes providing enhanced signaling efficiency even at low MHC-peptide concentrations at the interface of effector and APCs.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Journal of immunology. - 166 : 8 (2001), p. 5078-5086. -
További szerzők:	Bagossi Péter (1966-2011) (biokémikus, vegyész) Bene László (1963-) (biofizikus) Matkó János (1952-) (biológus) Szöllősi János (1953-) (biofizikus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Fésüs László (1947-) (orvos biokémikus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
Pályázati támogatás:	T029947 OTKA F020590 OTKA T019372 OTKA T030399 OTKA T023873 OTKA T030411 OTKA FKFP 327/2000 Egyéb ETT T05/102/2000 Egyéb FKFP 0518/99 Egyéb
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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4.

001-es BibID:	BIBFORM057538
035-os BibID:	(scopus)84910122146 (wos)000345023400059
Első szerző:	Govers, Coen
Cím:	TCRs genetically linked to CD28 and CD3[epszilon] do not mispair with endogenous TCR chains and mediate enhanced t cell persistence and anti-melanoma activity / Coen Govers, Zsolt Sebestyén, János Roszik, Mandy van Brakel, Cor Berrevoets, Árpád Szöőr, Konstantina Panoutsopoulou, Marieke Broertjes, Tan Van, György Vereb, János Szöllősi, Reno Debets
Dátum:	2014
ISSN:	0022-1767 1550-6606
Megjegyzések:	Adoptive transfer of T cells that are gene engineered to express a defined TCR represents a feasible and promising therapy for patients with tumors. However, TCR gene therapy is hindered by the transient presence and effectiveness of transferred T cells, which are anticipated to be improved by adequate T cell costimulation. In this article, we report the identification and characterization of a novel two-chain TCR linked to CD28 and CD3[epszilon] (i.e., TCR:28[epszilon]). This modified TCR demonstrates enhanced binding of peptide-MHC and mediates enhanced T cell function following stimulation with peptide compared with wild-type TCR. Surface expression of TCR:28[epszilon] depends on the transmembrane domain of CD28, whereas T cell functions depend on the intracellular domains of both CD28 and CD3[epszilon], with IL-2 production showing dependency on CD28:LCK binding. TCR:28[epszilon], but not wild-type TCR, induces detectable immune synapses in primary human T cells, and such immune synapses show significantly enhanced accumulation of TCR transgenes and markers of early TCR signaling, such as phosphorylated LCK and ERK. Importantly, TCR:28[epszilon] does not show signs of off-target recognition, as evidenced by lack of TCR mispairing, as well as preserved specificity. Notably, when testing TCR:28[epszilon] in immune-competent mice, we observed a drastic increase in T cell survival, which was accompanied by regression of large melanomas with limited recurrence. Our data argue that TCR transgenes that contain CD28, and, thereby, may provide T cell costimulation in an immune-suppressive environment, represent candidate receptors to treat patients with tumors.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk TCR T Cell
Megjelenés:	Journal Of Immunology. - 193 : 10 (2014), p. 5315-5326. -
További szerzők:	Sebestyén Zsolt Roszik János (1979-) (biofizikus) van Brakel, Mandy Berrevoets, Cor Szöőr Árpád (1984-) (orvos) Panoutsopoulou, Konstantina Broertjes, Marieke Van, Tan Vereb György (1965-) (biofizikus, orvos) Szöllősi János (1953-) (biofizikus) Debets, Reno
Pályázati támogatás:	TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP TÁMOP-4.2.2/B-10/1/2010-0024 TÁMOP TÁMOP-4.2.2/A-11/1/KONV-20120025 TÁMOP OTKA-NK101337 OTKA
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5.

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
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6.

001-es BibID:	BIBFORM020768
Első szerző:	Roszik János (biofizikus)
Cím:	T-cell synapse formation depends on antigen recognition but not CD3 interaction : studies with TCR : zeta, a candidate transgene for TCR gene therapy / Roszik J., Sebestyén Z., Govers C., Guri Y., Szöor A., Pályi-Krekk Z., Vereb G., Nagy P., Szöllosi J., Debets R.
Dátum:	2011
Megjegyzések:	T-cell receptors (TCRs) can be genetically modified to improve gene-engineered T-cell responses, a strategy considered critical for the success of clinical TCR gene therapy to treat cancers. TCR:zeta, which is a heterodimer of TCRalpha and beta chains each coupled to complete human CD3zeta, overcomes issues of mis-pairing with endogenous TCR chains, shows high surface expression and mediates antigen-specific T-cell functions in vitro. In the current study, we further characterized TCR:zeta in gene-engineered T cells and assessed whether this receptor is able to interact with surface molecules and drive correct synapse formation in Jurkat T cells. The results showed that TCR:zeta mediates the formation of synaptic areas with antigen-positive target cells, interacts closely with CD8alpha and MHC class I (MHCI), and co-localizes with CD28, CD45 and lipid rafts, similar to WT TCR. TCR:zeta did not closely associate with endogenous CD3epsilon, despite its co-presence in immune synapses, and TCR:zeta showed enhanced synaptic accumulation in T cells negative for surface-expressed TCR molecules. Notably, synaptic TCR:zeta demonstrated lowered densities when compared with TCR in dual TCR T cells, a phenomenon that was related to both extracellular and intracellular CD3zeta domains present in the TCR:zeta molecule and responsible for enlarged synapse areas
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Adoptive Transfer Antigens Antigens,CD28 Antigens,CD3 Antigens,CD45 Antigens,CD8 article Biophysics Cells Flow Cytometry Gene Therapy genetics Histocompatibility Antigens Histocompatibility Antigens Class I Human Humans Hungary Immunity,Cellular Immunological Synapses immunology In Vitro Jurkat Cells lipid raft LIPID RAFTS Membrane Microdomains metabolism physiology Receptor-CD3 Complex,Antigen,T-Cell Receptors,Antigen,T-Cell,alpha-beta Research Research Support Support Synapses T-Lymphocytes therapy Transgenes
Megjelenés:	European Journal of Immunology. - 41 : 5 (2011), p. 1288-1297. -
További szerzők:	Sebestyén Zsolt Govers, Coen Guri, Yakir Szöőr Árpád (1984-) (orvos) Pályiné Krekk Zsuzsanna (1974-) (molekuláris biológus) Vereb György (1965-) (biofizikus, orvos) Nagy Péter (1971-) (biofizikus) Szöllősi János (1953-) (biofizikus) Debets, Reno
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7.

001-es BibID:	BIBFORM005192
035-os BibID:	(WOS)000257507300075
Első szerző:	Sebestyén Zsolt
Cím:	Human TCR that incorporate CD3 zeta induce highly preferred pairing between TCR alpha and beta chains following gene transfer / Zsolt Sebestyén, Erik Schooten, Tamara Sals, Irene Zaldivar, Esther San José, Balbino Alarcón, Sara Bobisse, Antonio Rosato, János Szöllősi, Jan Willem Gratama, Ralph A. Willemsen, Reno Debets
Dátum:	2008
ISSN:	0022-1767
Megjegyzések:	TCR gene therapy is adversely affected by newly formed TCR alpha beta heterodimers comprising exogenous and endogenous TCR chains that dilute expression of transgenic TCR alpha beta dimers and are potentially self-reactive. We have addressed TCR mispairing by using a modified two-chain TCR that encompasses total human CD3 with specificities for three different Ags. Transfer of either TCR alpha:CD3 zeta or beta:CD3 zeta genes alone does not result in surface expression, whereas transfer of both modified TCR chains results in high surface expression, binding of peptide-MHC complexes and Ag-specific T cell functions. Genetic introduction of TCR alpha beta:CD3 zeta does not compromise surface expression and functions of an endogenous TCR alpha beta. Flow cytometry fluorescence resonance energy transfer and biochemical analyses demonstrate that TCR alpha beta:CD3 zeta is the first strategy that results in highly preferred pairing between CD3 zeta-modified TCR alpha and beta chains as well as absence of TCR mispairing between TCR:CD3 zeta and nonmodified TCR chains. Intracellular assembly and surface expression of TCR:CD3 zeta chains is independent of endogenous CD3 gamma, 8 delta, and epsilon. Taken together, our data support the use of TCR alpha beta:CD3 zeta to prevent TCR mispairing, which may provide an adequate strategy to enhance efficacy and safety of TCR gene transfer.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Energy Transfer Flow Cytometry Fluorescence Fluorescence Resonance Energy Transfer Gene Therapy Human Support therapy
Megjelenés:	Journal of Immunology. - 180 : 11 (2008), p. 7736-7746. -
További szerzők:	Schooten, Erik Sals, Tamara Zaldivar, Irene San José, Esther Alarcón, Balbino Bobisse, Sara Rosato, Antonio Szöllősi János (1953-) (biofizikus) Gratama, Jan Willem Willemsen, Ralph A. Debets, Reno
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8.

001-es BibID:	BIBFORM046304
Első szerző:	Szöllősi János (biofizikus)
Cím:	Supramolecular complexes of MHC class I, MHC class II, CD20, and tetraspan molecules (CD53, CD81, and CD82) at the surface of a B cell line JY / Szollosi J., Horejsi V., Bene L., Angelisova P., Damjanovich S.
Dátum:	1996
Megjegyzések:	The results of previous biochemical studies indicated that a fraction of MHC class II proteins is associated with four proteins of the tetraspan family, CD37, CD53, CD81, and CD82, and possibly with other membrane components, at the surface of JY B lymphoma cells. In the present communication we used a biophysical technique, namely the flow cytometric energy transfer method, to demonstrate the proximity of these molecules at the surface of the cells. Significant energy transfer (and, therefore, proximity within the 2-10 nm range) was observed between fluorescently labeled mAbs to DR, DQ, and the tetraspan molecules CD53, CD81, and CD82. Moreover, two other B cell surface molecules, CD20 and MHC class I, were found to be close to each other and to MHC class II and the tetraspan proteins, based on the observed high energy transfer efficiencies between the relevant fluorescently labeled mAbs. The character of simultaneous energy transfer from CD20, CD53, CD81, and CD82 to DR suggests that all these molecules are in a single complex with the DR molecules (or a complex of several DR molecules) rather than that each of them is separately associated with different DR molecules. Based on these data and previous biochemical results, a model is proposed predicting that the B cell membrane contains multicomponent supramolecular complexes consisting of at least two MHC class I and at least one DR, DQ, CD20, CD53, CD81, and CD82 molecules. Closer analysis of the energy transfer efficiencies makes it possible to suggest mutual orientations of the components within the complex. Participation of other molecules, not examined in this study (CD19 and CD37), in these supramolecular structures cannot be ruled out. These large assemblies of multiple B cell surface molecules may play a role in signaling through MHC molecules and in Ag presentation to T cells.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	The Journal of Immunology. - 157 : 7 (1996), p. 2939-2946. -
További szerzők:	Horejsi, Václav Bene László (1963-) (biofizikus) Angelisova, P. Damjanovich Sándor (1936-2017) (biofizikus)
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9.

001-es BibID:	BIBFORM006010
Első szerző:	Szöllősi János (biofizikus)
Cím:	Physical association between MHC class I and class II molecules detected on the cell surface by flow cytometric energy transfer / J. Szollosi, S. Damjanovich, M. Balazs, P. Nagy, L. Tron, M. J. Fulwyler, F. M. Brodsky
Dátum:	1989
Megjegyzések:	The physical association of HLA class I and class II Ag in the membranes of PGF and JY lymphoblastoid cell lines was studied using flow cytometric energy transfer. This technique measures the proximity of cell surface molecules in the nm range and provides a distribution histogram of the average proximity of molecules on each cell of a population. HLA Ag were labeled with mAb conjugated to fluorescein, serving as donor, or tetramethylrhodamine, serving as acceptor molecules. Significant fluorescence energy transfer was detected between various combinations of class I and class II molecules indicating that these molecules are within 10 nanometers of each other. Specifically, energy transfer was observed between class I molecules and DR, DQ, or DP class II HLA molecules. In addition, energy transfer between all combinations of DR, DQ, and DP molecules was observed. No transfer was observed among class I molecules or among DR or among DP molecules. Among DQ molecules, subpopulations transferred fluorescence energy to each other. The close contact measured between class I and class II Ag correlates with previous reports of cocapping and may reflect an immunologically significant interaction or the reported tendency of class I Ag to associate with other cell surface receptors, including growth factor receptors. The energy transfer between fluorescent antibodies to class II Ag suggests the existence of heterodimers formed from the different locus products, as well as possible quaternary surface interactions between alpha/beta complexes from separate loci.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Antibodies,Monoclonal Antibody Specificity Antigens,Surface Binding Sites Binding Sites,Antibody Cell Line Cell Line,Transformed Cell Membrane Energy Transfer Flow Cytometry Fluorescence Histocompatibility Antigens Histocompatibility Antigens Class I HLA-D Antigens Human Hungary immunology Lymphocytes metabolism Support,Non-U.S.Gov't Support,U.S.Gov't,Non-P.H.S. Support,U.S.Gov't,P.H.S.
Megjelenés:	The Journal of Immunology. - 143 : 1 (1989), p. 208-213. -
További szerzők:	Damjanovich Sándor (1936-2017) (biofizikus) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Nagy P. Trón Lajos (1941-) (biofizikus) Fulwyler, Mack J. Brodsky, F. M.
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