@article{MTMT:33666371,
	title = {Understanding impact of δF508 and G551D CFTR mutations on CFTR/PKA-c interaction},
	url = {https://m2.mtmt.hu/api/publication/33666371},
	author = {Simon, Márton},
	doi = {10.1016/j.bpj.2022.11.786},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {122},
	unique-id = {33666371},
	issn = {0006-3495},
	year = {2023},
	eissn = {1542-0086},
	pages = {112a-112a}
}

@article{MTMT:33636409,
	title = {Optimization of CFTR gating through the evolution of its extracellular loops},
	url = {https://m2.mtmt.hu/api/publication/33636409},
	author = {Simon, Márton and Csanády, László},
	doi = {10.1085/jgp.202213264},
	journal-iso = {J GEN PHYSIOL},
	journal = {JOURNAL OF GENERAL PHYSIOLOGY},
	volume = {155},
	unique-id = {33636409},
	issn = {0022-1295},
	year = {2023},
	eissn = {1540-7748},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@article{MTMT:34232792,
	title = {Estimating the true stability of the prehydrolytic outward-facing state in an ABC protein.},
	url = {https://m2.mtmt.hu/api/publication/34232792},
	author = {Simon, Márton and Iordanov, Iordan and Szöllősi, András and Csanády, László},
	doi = {10.7554/eLife.90736},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {12},
	unique-id = {34232792},
	issn = {2050-084X},
	abstract = {CFTR, the anion channel mutated in cystic fibrosis patients, is a model ABC protein whose ATP-driven conformational cycle is observable at single-molecule level in patch-clamp recordings. Bursts of CFTR pore openings are coupled to tight dimerization of its two nucleotide-binding domains (NBDs) and in wild-type (WT) channels are mostly terminated by ATP hydrolysis. The slow rate of non-hydrolytic closure - which determines how tightly bursts and ATP hydrolysis are coupled - is unknown, as burst durations of catalytic site mutants span a range of ~200-fold. Here, we show that Walker A mutation K1250A, Walker B mutation D1370N, and catalytic glutamate mutations E1371S and E1371Q all completely disrupt ATP hydrolysis. True non-hydrolytic closing rate of WT CFTR approximates that of K1250A and E1371S. That rate is slowed ~15-fold in E1371Q by a non-native inter-NBD H-bond, and accelerated ~15-fold in D1370N. These findings uncover unique features of the NBD interface in human CFTR.},
	keywords = {ZEBRAFISH; Xenopus; molecular biophysics; Structural biology; D-loop; composite ATP-binding site; flickery closure; mutant cycle},
	year = {2023},
	eissn = {2050-084X},
	orcid-numbers = {Iordanov, Iordan/0000-0001-8251-5857; Szöllősi, András/0000-0002-5570-4609; Csanády, László/0000-0002-6547-5889}
}

@mastersthesis{MTMT:34443688,
	title = {A CFTR anioncsatorna extracelluláris régiójának a csatorna működésére gyakorolt hatása},
	url = {https://m2.mtmt.hu/api/publication/34443688},
	author = {Simon, Márton},
	doi = {10.14753/SE.2023.2832},
	unique-id = {34443688},
	year = {2023}
}

@article{MTMT:32777033,
	title = {Promiscuity mapping of the S100 protein family using a high-throughput holdup assay},
	url = {https://m2.mtmt.hu/api/publication/32777033},
	author = {Simon, Márton and Bartus, Éva and Mag, Beáta Zsófia and Boros, Eszter and Roszjár, Lea and Gógl, Gergő and Travé, Gilles and Martinek, Tamás and Nyitray, László},
	doi = {10.1038/s41598-022-09574-2},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {12},
	unique-id = {32777033},
	issn = {2045-2322},
	year = {2022},
	eissn = {2045-2322},
	orcid-numbers = {Bartus, Éva/0000-0001-9976-6978; Martinek, Tamás/0000-0003-3168-8066; Nyitray, László/0000-0003-4717-5994}
}

@{MTMT:33787387,
	title = {Dynamic Control of Signaling by Phosphorylation of PDZ Binding Motifs},
	url = {https://m2.mtmt.hu/api/publication/33787387},
	author = {Simon, Márton and Nyitray, László},
	booktitle = {PDZ Mediated Interactions},
	doi = {10.1007/978-1-0716-1166-1_11},
	volume = {2256},
	unique-id = {33787387},
	abstract = {The dynamic regulation of protein-protein interactions (PPIs) involves phosphorylation of short liner motifs in disordered protein regions modulating binding affinities. The ribosomal-S6-kinase 1 is capable of binding to scaffold proteins containing PDZ domains through a PDZ-binding motif (PBM) located at the disordered C-terminus of the kinase. Phosphorylation of the PBM dramatically changes the interactome of RSK1 with PDZ domains exerting a fine-tuning mechanism to regulate PPIs. Here we present in detail highly effective biophysical (fluorescence polarization, isothermal calorimetry) and cellular (proteinfragment complementation) methods to study the effect of phosphorylation on RSK1-PDZ interactions that can be also applied to investigate phosphoregulation of other PPIs in signaling pathways.},
	keywords = {Humans; PHOSPHORYLATION; metabolism; signal transduction; BINDING SITES; BINDING SITE; human; controlled study; Protein Binding; Fluorescence Polarization; PROTEIN FUNCTION; protein domain; Protein-Serine-Threonine Kinases; protein protein interaction; ISOTHERMAL TITRATION CALORIMETRY; Microtubule-Associated Proteins; microtubule associated protein; PDZ DOMAIN; Protein Interaction Domains and Motifs; Protein-protein interaction; protein serine threonine kinase; S6 KINASE; procedures; PDZ Domains; Ribosomal Protein S6 Kinases, 90-kDa; protein-fragment complementation assay; NanoBiT; Bimolecular fragment complementation assay; MAST2 protein, human; RPS6KA1 protein, human},
	year = {2021},
	pages = {179-192},
	orcid-numbers = {Nyitray, László/0000-0003-4717-5994}
}

@article{MTMT:32573094,
	title = {Molecular pathology of the R117H cystic fibrosis mutation is explained by loss of a hydrogen bond},
	url = {https://m2.mtmt.hu/api/publication/32573094},
	author = {Simon, Márton and Csanády, László},
	doi = {10.7554/eLife.74693},
	journal-iso = {ELIFE},
	journal = {ELIFE},
	volume = {10},
	unique-id = {32573094},
	issn = {2050-084X},
	abstract = {The phosphorylation-activated anion channel cystic fibrosis transmembrane conductance regulator (CFTR) is gated by an ATP hydrolysis cycle at its two cytosolic nucleotide-binding domains, and is essential for epithelial salt-water transport. A large number of CFTR mutations cause cystic fibrosis. Since recent breakthrough in targeted pharmacotherapy, CFTR mutants with impaired gating are candidates for stimulation by potentiator drugs. Thus, understanding the molecular pathology of individual mutations has become important. The relatively common R117H mutation affects an extracellular loop, but nevertheless causes a strong gating defect. Here, we identify a hydrogen bond between the side chain of arginine 117 and the backbone carbonyl group of glutamate 1124 in the cryo-electronmicroscopic structure of phosphorylated, ATP-bound CFTR. We address the functional relevance of that interaction for CFTR gating using macroscopic and microscopic inside-out patch-clamp recordings. Employing thermodynamic double-mutant cycles, we systematically track gating-state-dependent changes in the strength of the R117-E1124 interaction. We find that the H-bond is formed only in the open state, but neither in the short-lived 'flickery' nor in the long-lived 'interburst' closed state. Loss of this H-bond explains the strong gating phenotype of the R117H mutant, including robustly shortened burst durations and strongly reduced intraburst open probability. The findings may help targeted potentiator design.},
	keywords = {PHOSPHORYLATION; AMINO-ACIDS; CONFORMATIONAL-CHANGES; IDENTIFICATION; TRANSMEMBRANE CONDUCTANCE REGULATOR; KINETIC-ANALYSIS; CFTR; gating defect; ABC protein; ATP-BINDING; CL-CHANNELS; class III mutant; R117H},
	year = {2021},
	eissn = {2050-084X},
	orcid-numbers = {Csanády, László/0000-0002-6547-5889}
}

@misc{MTMT:31867968,
	title = {Binding Profile Mapping of the S100 Protein Family Using a High-throughput Local Surface Mimetic Holdup Assay},
	url = {https://m2.mtmt.hu/api/publication/31867968},
	author = {Simon, Márton and Bartus, Éva and Mag, Beáta Zsófia and Boros, Eszter and Roszjár, Lea and Gógl, Gergő and Travé, Gilles and Martinek, Tamás and Nyitray, László},
	unique-id = {31867968},
	abstract = {S100 proteins are small, typically homodimeric, vertebrate-specific EF-hand proteins that establish Ca2+-dependent protein-protein interactions in the intra- and extracellular environment and are overexpressed in various pathologies. There are about 20 distinct human S100 proteins with numerous potential partner proteins. Here, we used a quantitative holdup assay to measure affinity profiles of most members of the S100 protein family against a library of chemically synthetized foldamers. The profiles allowed us to quantitatively map the binding promiscuity of each member towards the foldamer library. Since the library was designed to systematically contain most binary natural amino acid side chain combinations, the data also provide insight into the promiscuity of each S100 protein towards all potential naturally-occurring S100 partners in the human proteome. Such information will be precious for future drug design of modulators of S100 pathological activities.},
	year = {2020},
	orcid-numbers = {Bartus, Éva/0000-0001-9976-6978; Martinek, Tamás/0000-0003-3168-8066; Nyitray, László/0000-0003-4717-5994}
}

@article{MTMT:31009146,
	title = {High‐throughput competitive fluorescence polarization assay reveals functional redundancy in the S100 protein family},
	url = {https://m2.mtmt.hu/api/publication/31009146},
	author = {Simon, Márton and Ecsédi, Péter and Kovács, M. Gábor and Póti, Ádám Levente and Reményi, Attila and Kardos, József and Gógl, Gergő and Nyitray, László},
	doi = {10.1111/febs.15175},
	journal-iso = {FEBS J},
	journal = {FEBS JOURNAL},
	volume = {287},
	unique-id = {31009146},
	issn = {1742-464X},
	year = {2020},
	eissn = {1742-4658},
	pages = {2834-2846},
	orcid-numbers = {Ecsédi, Péter/0000-0002-4700-125X; Kovács, M. Gábor/0000-0001-9509-4270; Kardos, József/0000-0002-2135-2932; Nyitray, László/0000-0003-4717-5994}
}

@article{MTMT:31598466,
	title = {Proteomimetic surface fragments distinguish targets by function},
	url = {https://m2.mtmt.hu/api/publication/31598466},
	author = {Tököli, Attila and Mag, Beáta Zsófia and Bartus, Éva and Wéber, Edit and Szakonyi, Gerda and Simon, Márton and Czibula, Ágnes and Monostori, Éva and Nyitray, László and Martinek, Tamás},
	doi = {10.1039/d0sc03525d},
	journal-iso = {CHEM SCI},
	journal = {CHEMICAL SCIENCE},
	volume = {11},
	unique-id = {31598466},
	issn = {2041-6520},
	year = {2020},
	eissn = {2041-6539},
	pages = {10390-10398},
	orcid-numbers = {Tököli, Attila/0000-0001-8413-3182; Bartus, Éva/0000-0001-9976-6978; Wéber, Edit/0000-0002-5904-0619; Szakonyi, Gerda/0000-0002-4366-4283; Czibula, Ágnes/0000-0003-4461-2773; Monostori, Éva/0000-0002-7442-3562; Nyitray, László/0000-0003-4717-5994; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:30427214,
	title = {Rewiring of RSK-PDZ Interactome by Linear Motif Phosphorylation},
	url = {https://m2.mtmt.hu/api/publication/30427214},
	author = {Gógl, Gergő and Biri-Kovács, Beáta and Durbesson, Fabien and Jane, Pau and Nomine, Yves and Kostmann, Camille and Bilics, Viktória and Simon, Márton and Reményi, Attila and Vincentelli, Renaud and Trave, Gilles and Nyitray, László},
	doi = {10.1016/j.jmb.2019.01.038},
	journal-iso = {J MOL BIOL},
	journal = {JOURNAL OF MOLECULAR BIOLOGY},
	volume = {431},
	unique-id = {30427214},
	issn = {0022-2836},
	abstract = {Phosphorylation of short linear peptide motifs is a widespread process for the dynamic regulation of protein–protein interactions. However, the global impact of phosphorylation events on the protein–protein interactome is rarely addressed. The disordered C-terminal tail of ribosomal S6 kinase 1 (RSK1) binds to PDZ domain-containing scaffold proteins, and it harbors a phosphorylatable PDZ binding motif (PBM) responsive to epidermal growth factor (EGF) stimulation. Here, we examined binding of two versions of the RSK1 PBM, either phosphorylated or unphosphorylated at position −3, to almost all (95%) of the 266 PDZ domains of the human proteome. PBM phosphorylation dramatically altered the PDZ domain-binding landscape of RSK1, by strengthening or weakening numerous interactions to various degrees. The RSK-PDZome interactome analyzed in this study reveals how linear motif-based phospho-switches convey stimulus-dependent changes in the context of related network components.},
	keywords = {PHOSPHORYLATION; MAPK; Protein-protein interaction; PDZ; RSK},
	year = {2019},
	eissn = {1089-8638},
	pages = {1234-1249},
	orcid-numbers = {Biri-Kovács, Beáta/0000-0001-5803-9969; Nyitray, László/0000-0003-4717-5994}
}

@{MTMT:33787648,
	title = {Isolation and Characterization of S100 Protein-Protein Complexes},
	url = {https://m2.mtmt.hu/api/publication/33787648},
	author = {Kiss, Bence and Ecsédi, Péter and Simon, Márton and Nyitray, László},
	booktitle = {Calcium-binding proteins of the EF-hand superfamily : from basics to medical applications},
	doi = {10.1007/978-1-4939-9030-6_21},
	volume = {1929},
	unique-id = {33787648},
	abstract = {S100 proteins are small, mostly dimeric, EF-hand Ca2+ binding proteins. Upon Ca2+ binding, a conformational change occurs resulting in the exposure of a shallow hydrophobic binding groove in each subunit. Interestingly, S100 proteins can interact with their partners in two ways: symmetrically, when the two partners identically bind into each groove, or asymmetrically, when only one partner binds to the S100 dimer occupying both binding pockets. Here we present a heterologous expression and purification protocol for all known human S100 proteins as well as for their partner peptides. Moreover, we provide a detailed description of three in vitro methods to determine the affinity, stoichiometry, and kinetics of S100 protein-protein interactions.},
	keywords = {Humans; metabolism; KINETICS; human; Chemistry; Calorimetry; Escherichia coli; nonhuman; isolation and purification; Protein Binding; in vitro study; Models, Molecular; Multiprotein Complexes; Protein Conformation; Chemical Phenomena; Fluorescence Polarization; protein expression; Protein Denaturation; surface plasmon resonance; molecular model; recombinant protein; S100 Proteins; protein purification; protein protein interaction; stoichiometry; Hydrophobic and Hydrophilic Interactions; ISOTHERMAL TITRATION CALORIMETRY; protein s 100; protein isolation; heterologous expression; multiprotein complex; calvasculin; Surface plasmon resonance (SPR); EF-hand; Isothermal Titration Calorimetry (ITC); Fluorescence labelling; Fluorescence polarization (FP); Ca 2+ -binding},
	year = {2019},
	pages = {325-338},
	orcid-numbers = {Kiss, Bence/0000-0001-5810-5858; Ecsédi, Péter/0000-0002-4700-125X; Nyitray, László/0000-0003-4717-5994}
}