I am the alpha and the ... gamma, and the G. Calibration of intensity-based FRET meaurements

Szabó Á, Nagy P

Cytometry, 99A:369-371. (2021)

https://pubmed.ncbi.nlm.nih.gov/32790096/

https://doi.org/10.1002/cyto.a.24206

Comprehensive Model for Epidermal Growth Factor Receptor Ligand Binding Involving Conformational States of the Extracellular and the Kinase Domains

Hajdu T, Váradi T, Rebenku I, Kovács T, Szöllősi J, Nagy P.

Frontiers in Cell and Developmental Biology 8:776. (2020)

https://pubmed.ncbi.nlm.nih.gov/32850868/

https://doi.org/10.3389/fcell.2020.00776

Quo vadis FRET? Förster's method in the era of superresolution

Szabó Á, Szendi-Szatmári T, Szöllősi J, Nagy P

Methods and Applications in Fluorescence, 8(3): 032003. (2020)

https://pubmed.ncbi.nlm.nih.gov/32521530

https://doi.org/10.1088/2050-6120/ab9b72

Homo- and heteroassociations drive activation of ErbB3

Váradi T, Schneider M, Sevcsik E, Kiesenhofer D, Baumgart F, Batta G, Kovács T, Platzer R, Huppa JB, Szöllősi J, Schütz GJ, Brameshuber M, Nagy P

Biophys J, 117: 1935–194 (2019)

https://www.ncbi.nlm.nih.gov/pubmed/31653451

https://dx.doi.org/10.1016/j.bpj.2019.10.001

Reducing the detrimental effects of saturation phenomena in FRET microscopy

Szendi-Szatmári T, Szabó Á, Szöllősi J, Nagy P

Anal Chem, 91: 6378-6382 (2019)

https://www.ncbi.nlm.nih.gov/pubmed/30993981

http://dx.doi.org/10.1021/acs.analchem.9b01504

Alterations in the properties of the cell membrane due to glycosphingolipid accumulation in a model of Gaucher disease

Batta G, Soltész L, Kovács T, Bozó T, Mészár Z, Kellermayer M, Szöllősi J, Nagy P.

Sci Rep. 8: 157 (2018)

https://www.ncbi.nlm.nih.gov/pubmed/29317695

http://dx.doi.org/10.1038/s41598-017-18405-8

The effect of fluorophore conjugation on antibody affinity and the photophysical properties of dyes

Szabó Á, Szenti-Szatmári T, Ujlaky-Nagy L, Rádi I, Vereb G, Szöllősi J, Nagy P.

Biophys J, 114:688-700 (2018)

https://www.ncbi.nlm.nih.gov/pubmed/29414714

http://dx.doi.org/10.1016/j.bpj.2017.12.011

The dipole potential correlates with lipid raft markers in the plasma membrane of living cells

Kovács T, Batta G, Zákány F, Szöllősi J, Nagy P.

J Lipid Res. 58(8):1681-1691 (2017)

https://www.ncbi.nlm.nih.gov/pubmed/28607008

http://dx.doi.org/10.1194/jlr.M077339

The Dipole Potential Modifies the Clustering and Ligand Binding Affinity of ErbB Proteins and Their Signaling Efficiency

Kovács T, Batta G, Hajdu T, Szabó Á, Váradi T, Zákány F, Csomós I, Szöllősi J, Nagy P.

Sci Rep. 6:35850 (2016)

https://www.ncbi.nlm.nih.gov/pubmed/27775011

http://dx.doi.org/10.1038/srep35850

 

rFRET: A comprehensive, Matlab-based program for analyzing intensity-based ratiometric microscopic FRET experiments

Nagy P, Szabó Á, Váradi T, Kovács T, Batta G, Szöllősi J.

Cytometry A. 89(4):376-84 (2016)

https://www.ncbi.nlm.nih.gov/pubmed/27003481

http://dx.doi.org/10.1002/cyto.a.22828

 

Maximum likelihood estimation of FRET efficiency and its implications for distortions in pixelwise calculation of FRET in microscopy

Nagy P, Szabó A, Váradi T, Kovács T, Batta G, Szöllősi J.

Cytometry A. 85(11):942-52 (2014)

https://www.ncbi.nlm.nih.gov/pubmed/25123296

http://dx.doi.org/10.1002/cyto.a.22518

 

Epigallocatechin 3-O-gallate induces 67 kDa laminin receptor-mediated cell death accompanied by downregulation of ErbB proteins and altered lipid raft clustering in mammary and epidermoid carcinoma cells

Mocanu MM, Ganea C, Georgescu L, Váradi T, Shrestha D, Baran I, Katona E, Nagy P, Szöllősi J.

J Nat Prod. 77(2):250-7 (2014)

https://www.ncbi.nlm.nih.gov/pubmed/24456004

http://dx.doi.org/10.1021/np4007712

 

Binding of trastuzumab to ErbB2 is inhibited by a high pericellular density of hyaluronan

Váradi T, Mersich T, Auvinen P, Tammi R, Tammi M, Salamon F, Besznyák I Jr, Jakab F, Baranyai Z, Szöllősi J, Nagy P.

J Histochem Cytochem. 60(8):567-75 (2012)

https://www.ncbi.nlm.nih.gov/pubmed/22562558

http://dx.doi.org/10.1369/0022155412448070

 

Distribution of resting and ligand-bound ErbB1 and ErbB2 receptor tyrosine kinases in living cells using number and brightness analysis

Nagy P, Claus J, Jovin TM, Arndt-Jovin DJ.

Proc Natl Acad Sci U S A. 107(38):16524-9 (2010)

https://www.ncbi.nlm.nih.gov/pubmed/20813958

http://dx.doi.org/10.1073/pnas.1002642107

 

Coclustering of ErbB1 and ErbB2 revealed by FRET-sensitized acceptor bleaching

Szabó A, Szöllősi J, Nagy P.

Biophys J. 99(1):105-14 (2010)

https://www.ncbi.nlm.nih.gov/pubmed/20655838

http://dx.doi.org/10.1016/j.bpj.2010.03.061

 

Quantitative characterization of the large-scale association of ErbB1 and ErbB2 by flow cytometric homo-FRET measurements

Szabó A, Horváth G, Szöllősi J, Nagy P.

Biophys J. 95(4):2086-96 (2008)

https://www.ncbi.nlm.nih.gov/pubmed/18487307

http://dx.doi.org/10.1529/biophysj.108.133371

 

EGFR and ErbB2 are functionally coupled to CD44 and regulate shedding, internalization and motogenic effect of CD44

Pályi-Krekk Z, Barok M, Kovács T, Saya H, Nagano O, Szöllősi J, Nagy P.

Cancer Lett. 263(2):231-42 (2008)

https://www.ncbi.nlm.nih.gov/pubmed/18276068

http://dx.doi.org/10.1016/j.canlet.2008.01.014

 

Hyaluronan-induced masking of ErbB2 and CD44-enhanced trastuzumab internalisation in trastuzumab resistant breast cancer

Pályi-Krekk Z, Barok M, Isola J, Tammi M, Szöllősi J, Nagy P.

Eur J Cancer. 43(16):2423-33 (2007)

https://www.ncbi.nlm.nih.gov/pubmed/17911008

http://dx.doi.org/10.1016/j.ejca.2007.08.018

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