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001-es BibID:	BIBFORM037108
Első szerző:	Renz, Malte
Cím:	Plasticity of the asialoglycoprotein receptor deciphered by ensemble FRET imaging and single-molecule counting PALM / Malte Renz, Brian Daniels, György Vámosi, Irwin M. Arias, Jennifer Lippincott-Schwartz
Dátum:	2012
ISSN:	0027-8424
Megjegyzések:	The stoichiometry and composition of membrane protein receptors are critical to their function. However, the inability to assess receptor subunit stoichiometry in situ has hampered efforts to relate receptor structures to functional states. Here, we address this problem for the asialoglycoprotein receptor using ensemble FRET imaging, analytical modeling, and single-molecule counting with photoactivated localization microscopy (PALM). We show that the two subunits of asialoglycoprotein receptor (RHL1, RHL2) can assemble into both homo- and hetero-oligomeric complexes, displaying three forms with distinct ligand specificities that co-exist on the plasma membrane: higher-order homo-oligomers of RHL1; higher-order hetero-oligomers of RHL1 and RHL2 with two-to-one stoichiometry; and the homo-dimer RHL2, with little tendency to further homo-oligomerize. Levels of these complexes can be modulated in the plasma membrane by exogenous ligands. Thus, even a simple two-subunit receptor can exhibit remarkable plasticity in structure, and consequently function, underscoring the importance of deciphering oligomerization in single cells at the single-molecule level.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban PALM single molecule counting receptor stoichiometry FRET Molekuláris Medicina
Megjelenés:	Proceedings Of The National Academy Of Sciences Of The United States Of America. - 109 : 44 (2012), p. E2989-E2997. -
További szerzők:	Daniels, Brian Vámosi György (1967-) (biofizikus) Arias, Irwin, M. Lippincott-Schwartz, Jennifer
Pályázati támogatás:	TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP Fehérje-fehérje kölcsönhatások limfociták membránjában és a sejtmagban K 77600 OTKA K 103965 OTKA
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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001-es BibID:	BIBFORM095083
035-os BibID:	(cikkazonosító)e62241
Első szerző:	Vámosi György (biofizikus)
Cím:	Assessing Protein Interactions in Live-Cells with FRET-Sensitized Emission / György Vámosi, Sarah Miller, Molika Sinha, Gabor Mocsár, Malte Renz
Dátum:	2021
ISSN:	1940-087X
Megjegyzések:	Förster Resonance Energy Transfer (FRET) is the radiationless transfer of energy from an excited donor to an acceptor molecule and depends upon the distance and orientation of the molecules as well as the extent of overlap between the donor emission and acceptor absorption spectra. FRET permits to study the interaction of proteins in the living cell over time and in different subcellular compartments. Different intensity-based algorithms to measure FRET using microscopy have been described in the literature. Here, a protocol and an algorithm are provided to quantify FRET efficiency based on measuring both the sensitized emission of the acceptor and quenching of the donor molecule. The quantification of ratiometric FRET in the living cell not only requires the determination of the crosstalk (spectral spill-over, or bleedthrough) of the fluorescent proteins but also the detection efficiency of the microscopic setup. The protocol provided here details how to assess these critical parameters
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Journal of Visualized Experiments. - 2021 : 170 (2021), p. 1-15. -
További szerzők:	Miller, Sarah Sinha, Molika Mocsár Gábor (1981-) (biofizikus) Renz, Malte
Pályázati támogatás:	GINOP-2.3.2-15-2016-00026 GINOP GINOP-2.3.3-15-2016-00030 GINOP NN129371 OTKA ANN135107 OTKA
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