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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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001-es BibID:	BIBFORM004868
035-os BibID:	(scopus)20144375715 (wos)000228111600008
Első szerző:	Horváth András (vegyész)
Cím:	Potent inhibition of HIV-1 entry by (s4dU)35 / Horvath, A., Tokes, S., Hartman, T., Watson, K., Turpin, J. A., Buckheit, R. W., Jr., Sebestyen, Z., Szollosi, J., Benko, I., Bardos, T. J., Dunn, J. A., Fesus, L., D. Toth, F., Aradi, J.
Dátum:	2005
ISSN:	0042-6822
Megjegyzések:	We have previously reported the potent in vitro HIV-1 anti-reverse transcriptase activity of a 35-mer of 4-thio-deoxyuridylate [(s(4)dU)(35)]. In efforts to define its activity in a more physiological system, studies were carried out to determine the stage of viral infection that this compound mediates its anti-viral effect. Results of the studies reported herein show that (s(4)dU)(35) is nontoxic and is capable of inhibiting both single and multi-drug resistant HIV strains (IC(50): 0.8-25.4 microg/ml) in vitro. Besides its previously reported anti-RT activity, (s(4)dU)(35) mediated its antiviral action by preventing virus attachment (IC(50): 0.002-0.003 microg/ml), and was stable in vitro and slowly degraded by DNAses. Competition studies and fluorescence resonance energy transfer (FRET) experiments indicated that (s(4)dU)(35) preferentially binds to CD4 receptors, but not to CD48. Confocal laser scanning microscopy (CLSM) studies showed that (s(4)dU)(35) did not penetrate into the cells and colocalized with cell surface thioredoxin. Our studies identify (s(4)dU)(35) as a potential novel HIV entry inhibitor that may have utility as either a systemic antiretroviral or as a preventing agent for HIV transmission.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk antagonists and inhibitors Anti-HIV Agents Antigens,CD4 Cell Line Cells chemical synthesis Deoxyuracil Nucleotides drug effects Energy Transfer Fluorescence Fluorescence Resonance Energy Transfer genetics Hela Cells Hiv-1 HIV-1 Reverse Transcriptase Humans Hungary In Vitro metabolism methods Microbial Sensitivity Tests Microscopy Microscopy,Confocal pathogenicity pharmacology Research Reverse Transcriptase Inhibitors Support Thionucleotides toxicity
Megjelenés:	Virology. - 334 : 2 (2005), p. 214-223. -
További szerzők:	Tőkés Szilvia (1964-) (biológus) Hartman, Tracy Watson, Karen Turpin, Jim A. Buckheit, Robert W. Jr. Sebestyén Zsolt Szöllősi János (1953-) (biofizikus) Benkő Ilona (1954-) (orvos, farmakológus) Bardos, Thomas J. Dunn, Joseph A. Fésüs László (1947-) (orvos biokémikus) Tóth Ferenc, D. (1940-2004) (mikrobiológus, élettanász) Aradi János (1942-) (biokémikus, vegyész)
Internet cím:	elektronikus változat DOI
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