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Frontiers in Molecular Biosciences|October 28, 2021
Studying the Structures of Relaxed and Fuzzy Interactions: The Diverse World of S100 ComplexesPéter Ecsédi, Gergő Gógl, László Nyitray
Acta Crystallographica. Section D, Biological Crystallography|March 23, 2013
Protein-peptide complex crystallization: a case study on the ERK2 mitogen-activated protein kinaseGergő Gógl, Imre Törő, Attila Reményi
The Journal of Biological Chemistry|February 6, 2013
Structural mechanism for the specific assembly and activation of the extracellular signal regulated kinase 5 (ERK5) moduleGábor Glatz, Gergő Gógl, Anita Alexa, et al.
Trends in Biochemical Sciences|January 7, 2019
Disordered Protein Kinase Regions in Regulation of Kinase Domain CoresGergő Gógl, Alexandr P Kornev, Attila Reményi, et al.
Structure (London, England : 1993)|May 23, 2020
Structure Determination of the Transactivation Domain of p53 in Complex with S100A4 Using Annexin A2 as a Crystallization ChaperonePéter Ecsédi, Gergő Gógl, Henrietta Hóf, et al.
The Journal of Biological Chemistry|November 4, 2015
Structural Basis of Ribosomal S6 Kinase 1 (RSK1) Inhibition by S100B Protein: MODULATION OF THE EXTRACELLULAR SIGNAL-REGULATED KINASE (ERK) SIGNALING CASCADE IN A CALCIUM-DEPENDENT WAYGergő Gógl, Anita Alexa, Bence Kiss, et al.
The FEBS Journal|December 15, 2019
High-throughput competitive fluorescence polarization assay reveals functional redundancy in the S100 protein familyMárton A Simon, Péter Ecsédi, Gábor M Kovács, et al.
The Journal of Biological Chemistry|August 9, 2018
Multiple S100 protein isoforms and C-terminal phosphorylation contribute to the paralog-selective regulation of nonmuscle myosin 2 filamentsPéter Ecsédi, Neil Billington, Gyula Pálfy, et al.
Plos One|May 12, 2017
Ezrin interacts with S100A4 via both its N- and C-terminal domainsBeáta Biri-Kovács, Bence Kiss, Henrietta Vadászi, et al.
Scientific Reports|April 8, 2022
Promiscuity mapping of the S100 protein family using a high-throughput holdup assayMárton A Simon, Éva Bartus, Beáta Mag, et al.
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