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001-es BibID:	BIBFORM004644
Első szerző:	Brock Roland
Cím:	Rapid characterization of green fluorescent protein fusion proteins on the molecular and cellular level by fluorescence correlation microscopy / Brock, R., Vamosi, G., Vereb, G., Jovin, T. M.
Dátum:	1999
Megjegyzések:	Fluorescence correlation microscopy (FCM) was applied to characterize fusion proteins of the green fluorescent protein (GFP) on the cellular as well as molecular level within seconds in an integrated instrument. FCM combines the inherent sensitivity and high spatial resolution of fluorescence correlation spectroscopy with fluorescence imaging and micropositioning, thereby providing a spectrum of molecular information in the cellular context. Signatures of characteristic parameters derived from the autocorrelation functions served to distinguish a GFP fusion protein of the epidermal growth factor receptor from GFP fluorescence in the endoplasmic reticulum and cytoplasm. Diffusion constants measured for free transiently expressed GFP reproduced values reported previously with other techniques. The accessible concentration range extends from millions to only a few thousand molecules per cell, with single molecule detectability in the femtoliter detection volume. The detailed molecular characterization offered by FCM is fully compatible with automation in sample identification and detection, offering new possibilities for highly integrated high-throughput screening
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban analysis Animal Automation chemistry Cho Cells Cytoplasm Diffusion Endoplasmic Reticulum Epidermal Growth Factor Fluorescence Hamsters instrumentation Luminescent Proteins methods Microscopy Microscopy, Fluorescence Proteins Receptor, Epidermal Growth Factor Recombinant Fusion Proteins Sensitivity and Specificity Support, Non-U.S.Gov't Transfection ultrastructure
Megjelenés:	Proceedings of the National Academy of Sciences of the United States of America. - 96 : 18 (1999), p. 10123-10128. -
További szerzők:	Vámosi György (1967-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Jovin, Thomas M.
Internet cím:	elektronikus változat elektronikus változat
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001-es BibID:	BIBFORM079931
035-os BibID:	(cikkazonosító)3370 (scopus)85071327332 (wos)000477041100254
Első szerző:	Vámosi György (biofizikus)
Cím:	EGF Receptor Stalls upon Activation as Evidenced by Complementary Fluorescence Correlation Spectroscopy and Fluorescence Recovery after Photobleaching Measurements / Vámosi György, Friedländer-Brock Elza, Ibrahim Shehu M., Brock Roland, Szöllősi János, Vereb György
Dátum:	2019
ISSN:	1661-6596 1422-0067
Megjegyzések:	To elucidate the molecular details of the activation-associated clustering of epidermal growth factor receptors (EGFRs), the time course of the mobility and aggregation states of eGFP tagged EGFR in the membranes of Chinese hamster ovary (CHO) cells was assessed by in situ mobility assays. Fluorescence correlation spectroscopy (FCS) was used to probe molecular movements of small ensembles of molecules over short distances and time scales, and to report on the state of aggregation. The diffusion of larger ensembles of molecules over longer distances (and time scales) was investigated by fluorescence recovery after photobleaching (FRAP). Autocorrelation functions could be best fitted by a two-component diffusion model corrected for triplet formation and blinking. The slow, 100?1000 ms component was attributed to membrane localized receptors moving with free Brownian diffusion, whereas the fast, ms component was assigned to cytosolic receptors or their fragments. Upon stimulation with 50 nM EGF, a significant decrease from 0.11 to 0.07 ?m2/s in the diffusion coefficient of membrane-localized receptors was observed, followed by recovery to the original value in ~20 min. In contrast, the apparent brightness of diffusing species remained the same. Stripe FRAP experiments yielded a decrease in long-range molecular mobility directly after stimulation, evidenced by an increase in the recovery time of the slow component from 13 to 21.9 s. Our observations are best explained by the transient attachment of ligand-bound EGFRs to immobile or slowly moving structures such as the cytoskeleton or large, previously photobleached receptor aggregates.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban Fluorescence correlation spectroscopy FCS fluorescence recovery after photobleaching FRAP epidermal growth factor receptor translational diffusion EGFR?eGFP fusion protein
Megjelenés:	International Journal Of Molecular Sciences. - 20 : 13 (2019), p. 1-22. -
További szerzők:	Friedländer Elza (1980-) (biofizikus) Ibrahim, Shehu M. Brock Roland Szöllősi János (1953-) (biofizikus) Vereb György (1965-) (biofizikus, orvos)
Pályázati támogatás:	K119690 OTKA NN129371 OTKA GINOP-2.3.2-15-2016-00050 GINOP GINOP-2.3.3-15-2016-00003 GINOP
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