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Stefan Eugen Szedlacsek

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I am primarily interested in understanding the relationship between the structure and function of enzymes involved in signal transduction processes. Specifically, I am studying together with my team, the protein tyrosine phosphatases: their structural and kinetic characteristics, their substrate specificities - all of them in connection with the physiological role they play in signalling processes.

Laboratorul de Enzimologie - Institutul de Biochimie al Academiei Romane, Bucuresti, .

E-mail: trimite un mesaj.

Pagina web a instituţiei: https://www.biochim.ro/
Pagina web personala: https://www.biochim.ro/researchers-staff/stefan.szedlacsek/

Urmareste linkul ResearcherID pentru toate articolele cercetatorului: F-1830-2010. Tabelul detaliat al articolelor este in josul paginii.

Nascut(a) in: 1952

Interese: enzimologie, receptori, structura proteica, transductie de semnal, cinetica enzimatica

flag Detalii:
In primul rand sunt interesat in intelegerea corelatiei dintre structura si functiile enzimelor implicate in procesele de transmitere a semnalului. In mod concret, studiez impreuna cu echipa mea, protein tirozin fosfatazele: caracteristicile lor structurale si cinetice, specificitatile lor de substrat - toate aceste in legatura cu rolul fiziologic pe care-l joaca in procesele de semnalizare.

Publicații selectate:

* Mentel M, Ionescu AE, Puscalau-Girtu I, Helm MS, Badea RA, Rizzoli SO, Szedlacsek SE., WDR1 is a novel EYA3 substrate and its dephosphorylation induces modifications of the cellular actin cytoskeleton, Nature Publishing Group, Scientific Reports, 8, 2018.

* Balasu MC, Spiridon LN, Miron S, Craescu CT, Scheidig AJ, Petrescu AJ, Szedlacsek SE, Interface analysis of the complex between ERK2 and PTP-SL, PLoS ONE, 4(5), 2009.

* Pascaru M, Tanase C, Vacaru AM, Boeti P, Neagu E, Popescu I, Szedlacsek SE., ANALYSIS OF MOLECULAR DETERMINANTS OF PRL-3., J Cell Mol Med, 13(9B), 2008.

* Tabernero L, Aricescu AR, Jones EY, Szedlacsek SE., Protein tyrosine phosphatases: structure-function relationships, FEBS J., 275(5), 2008.

* Köhn M, Gutierrez-Rodriguez M, Jonkheijm P, Wetzel S, Wacker R, Schroeder H, Prinz H, Niemeyer CM, Breinbauer R, Szedlacsek SE, Waldmann H., A microarray strategy for mapping the substrate specificity of protein tyrosine phosphatase., Angew Chem Int Ed Engl., 46(40), 2007.

* Vlad MO, Morán F, Popa VT, Szedlacsek SE, Ross J., Functional, fractal nonlinear response with application to rate processes with memory, allometry, and population genetics, Proc Natl Acad Sci U S A, 104(12), 2007.

* Dursina B, Reents R, Delon C, Wu Y, Kulharia M, Thutewohl M, Veligodsky A, Kalinin A, Evstifeev V, Ciobanu D, Szedlacsek SE, Waldmann H, Goody RS, Alexandrov K, Identification and specificity profiling of protein prenyltransferase inhibitors using new fluorescent phosphoisoprenoids, J. Am. Chem. Soc., 128, 2006.

* Vlad MO, Szedlacsek SE, Pourmand N, Cavalli-Sforza LL, Oefner P, Ross J., Fisher's theorems for multivariable, time- and space-dependent systems, with applications in population genetics and chemical kinetics., Proc Natl Acad Sci U S A., 102, 2005.

* Szedlacsek SE, Duggleby RG, Kinetics of slow and tight-binding inhibitors, Methods Enzymol., 249, 1995.

* Baici A, Szedlacsek SE, Fruh H, Michel BA., pH-dependent hysteretic behaviour of human myeloblastin (leucocyte proteinase 3), Biochem. J., 317 ( Pt 3), 1996.

* Szedlacsek SE, Aricescu AR, Havsteen BH., Time-dependent control of metabolic systems by external effectors, J. Theor. Biol., 182(3), 1996.

* Aricescu AR, Fulga TA, Cismasiu V, Goody RS, Szedlacsek SE., Intramolecular interactions in protein tyrosine phosphatase RPTPmu: kinetic evidence., Biochem. Biophys. Res. Commun., 280(1), 2001.

* Szedlacsek SE, Aricescu AR, Fulga TA, Renault L, Scheidig AJ., Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation., J. Mol. Biol., 311(3), 2001.

* Cismasiu VB, Denes SA, Reilander H, Michel H, Szedlacsek SE., The MAM (meprin/A5-protein/PTPmu) domain is a homophilic binding site promoting the lateral dimerization of receptor-like protein-tyrosine phosphatase mu., J Biol Chem., 279, 2004.