Quantitative receptor analysis group

Prof. Péter Nagy

 

 

Head of the group

Peter Nagy, MD, PhD, DSc

email:

 

 

 

 

 

 

Introduction of the research group

 

 

 

Staff

  • Ágnes Szabó, PhD, research fellow
  • Tímea Váradi, PhD, research fellow 
  • Tamás Kovács, MD, PhD, research fellow
  • Gyula Batta, PhD, assistant professor
  • Tímea Hajdu, PhD student
  • Tímea Szendi-Szatmári, junior research fellow
  • Máté Szabó, undergraduate student
  • Rita Utasi-Szabó, laboratory assistant
 

 

 

 

 

 

 

 

Research projects

1. Clustering of ErbB proteins

2. The effect of the lipid environment of the cell membrane on the clustering and cell biological function of membrane proteins

3. Medical implications of the cell membrane and membrane lipids

4. Methodological developments related to fluorescence labeling of cells and Förster resonance energy transfer

 

Representative publications

  • 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

Updated: 2019.07.12.


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