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001-es BibID:BIBFORM098704
035-os BibID:(cikkazonosító)5652 (WoS)000723448300001 (Scopus)85118861202
Első szerző:Bankó Csaba (molekuláris biológus)
Cím:Isocyanide Substitution in Acridine Orange Shifts DNA Damage-Mediated Phototoxicity to Permeabilization of the Lysosomal Membrane in Cancer Cells / Bankó Csaba, Nagy Zsolt László, Nagy Miklós, Szemán-Nagy Gábor György, Rebenku István, Imre László, Tiba Attila, Hajdu András, Szöllősi János, Kéki Sándor, Bacso Zsolt
Dátum:2021
ISSN:2072-6694
Megjegyzések:Aside from tissue cell renewal, tumor cells are also produced every day. In ordinary conditions, immunologically controlled cell death mechanisms limit cancer development. There are several cell death processes used for how normal and tumor cells are eliminated at the end of their lifespan. In cancer therapy, cells dying via immunological death are more efficiently eradicated than cells dying by classical apoptosis. Photodynamic treatments with some photosensitizers target lysosomes. Lysosomal death diverts apoptosis to the immunologically more pertinent necrosis-like death pathways. Acridine orange (AO), a well-known photosensitizer, targets lysosomes as well. We have synthesized a new compound abbreviated as DM, a modified AO, and examined details of intracellular processes leading to photodynamic cell death. We have proven that DM targets lysosomes better than AO. Remarkably, with DM, we could visualize an abrupt nuclear DNA release from cells during the photodynamic process. Our work highlights which cellular events may enhance immunological cell death.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Cancers. - 13 : 22 (2021), p. 1-24. -
További szerzők:Nagy Zsolt László (1989-) (gyógyszerész) Nagy Miklós (1976-) (vegyész) Szemán-Nagy Gábor (1975-) (biológia tanár-molekuláris biológus) Rebenku István Imre László (1979-) (biológus) Tiba Attila (1990-) (informatikus, matematikus) Hajdu András (1973-) (matematikus, informatikus) Szöllősi János (1953-) (biofizikus) Kéki Sándor (1964-) (polimer kémikus) Bacsó Zsolt (1963-) (biofizikus)
Pályázati támogatás:GINOP-2.3.2-15-2016-00041
GINOP
GINOP 2.3.4- 15-2020-00008
GINOP
K-132685
Egyéb
FIKP-20428-3/2018/FEKUTSTRAT
Egyéb
EFOP-3.6.3-VEKOP-16-2017-00009
EFOP
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2.

001-es BibID:BIBFORM087409
Első szerző:Hajdu Tímea (biomérnök)
Cím:Comprehensive Model for Epidermal Growth Factor Receptor Ligand Binding Involving Conformational States of the Extracellular and the Kinase Domains / Tímea Hajdu, Tímea Váradi, István Rebenku, Tamás Kovács, János Szöllösi, Péter Nagy
Dátum:2020
ISSN:2296-634X
Megjegyzések:The epidermal growth factor (EGF) receptor (EGFR) undergoes ligand-dependent dimerization to initiate transmembrane signaling. Although crystallographic structures of the extracellular and kinase domains are available, ligand binding has not been quantitatively analyzed taking the influence of both domains into account. Here, we developed a model explicitly accounting for conformational changes of the kinase and extracellular domains, their dimerizations and ligand binding to monomeric and dimeric receptor species. The model was fitted to ligand binding data of suspended cells expressing receptors with active or inactive kinase conformations. Receptor dimers with inactive, symmetric configuration of the kinase domains exhibit positive cooperativity and very weak binding affinity for the first ligand, whereas dimers with active, asymmetric kinase dimers are characterized by negative cooperativity and subnanomolar binding affinity for the first ligand. The homodimerization propensity of EGFR monomers with active kinase domains is _100-times higher than that of dimers with inactive kinase domains. Despite this fact, constitutive, ligand-independent dimers are mainly generated from monomers with inactive kinase domains due to the excess of such monomers in the membrane. The experimental finding of increased positive cooperativity at high expression levels of EGFR was recapitulated by the model. Quantitative prediction of ligand binding to different receptor species revealed that EGF binds to receptor monomers and dimers in an expression-level dependent manner without significant recruitment of monomers to dimers upon EGF stimulation below the phase transition temperature of the membrane. Results of the fitting offer unique insight into the workings of the EGFR.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
EGF
EGFR
Megjelenés:Frontiers in Cell and Developmental Biology. - 8 (2020), p. 1-53. -
További szerzők:Váradi Tímea (1973-) (biológus) Rebenku István Kovács Tamás (1985-) (általános orvos) Szöllősi János (1953-) (biofizikus) Nagy Péter (1971-) (biofizikus)
Pályázati támogatás:GINOP-2.3.2-15-2016-00020
GINOP
GINOP-2.2.1-15-2017-00044
GINOP
NKFIH K120302
Egyéb
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Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM109070
035-os BibID:(cikkazonosító)2934 (Scopus)85148394136 (WoS)000955795600021
Első szerző:Rebenku István
Cím:Pixel-by-pixel autofluorescence corrected FRET in fluorescence microscopy improves accuracy for samples with spatially varied autofluorescence to signal ratio / Rebenku István, Lloyd Cameron B., Szöllősi János, Vereb György
Dátum:2023
ISSN:2045-2322
Megjegyzések:The actual interaction between signaling species in cellular processes is often more important than their expression levels. Förster resonance energy transfer (FRET) is a popular tool for studying molecular interactions, since it is highly sensitive to proximity in the range of 2-10 nm. Spectral spillover-corrected quantitative (3-cube) FRET is a cost efective and versatile approach, which can be applied in fow cytometry and various modalities of fuorescence microscopy, but may be hampered by varying levels of autofuorescence. Here, we have implemented pixel-by-pixel autofuorescence correction in microscopy FRET measurements, exploiting cell-free calibration standards void of autofuorescence that allow the correct determination of all spectral spillover factors. We also present an ImageJ/Fiji plugin for interactive analysis of single images as well as automatic creation of quantitative FRET efciency maps from large image sets. For validation, we used bead and cell based FRET models covering a range of signal to autofuorescence ratios and FRET efciencies and compared the approach with conventional average autofuorescence/background correction. Pixel-by-pixel autofuorescence correction proved to be superior in the accuracy of results, particularly for samples with spatially varying autofuorescence and low fuorescence to autofuorescence ratios, the latter often being the case for physiological expression levels.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Scientific Reports. - 13 : 1 (2023), p. 1-15. -
További szerzők:Lloyd, Cameron B. Szöllősi János (1953-) (biofizikus) Vereb György (1965-) (biofizikus, orvos)
Pályázati támogatás:GINOP-2.2.1-15-2017-00072
GINOP
K135938
OTKA
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Intézményi repozitóriumban (DEA) tárolt változat
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