@CONFERENCE{MTMT:34236962,
	title = {A rendezetlen fehérjék és az NMR spektroszkópia},
	url = {https://m2.mtmt.hu/api/publication/34236962},
	author = {Sebák, Fanni and Szabó, Csenge Lilla and Ecsédi, Péter and Burkhard, LUY and Nyitray, László and Bodor, Andrea},
	booktitle = {XXIX. Nemzetközi Vegyészkonferencia / 29th International Conference on Chemistry},
	unique-id = {34236962},
	year = {2023},
	pages = {1-2},
	orcid-numbers = {Sebák, Fanni/0000-0001-9252-9961; Szabó, Csenge Lilla/0000-0002-6508-3439; Ecsédi, Péter/0000-0002-4700-125X; Nyitray, László/0000-0003-4717-5994; Bodor, Andrea/0000-0002-7422-298X}
}

@article{MTMT:34213192,
	title = {Assignment of the disordered, proline-rich N-terminal domain of the tumour suppressor p53 protein using 1HN and 1Hα-detected NMR measurements},
	url = {https://m2.mtmt.hu/api/publication/34213192},
	author = {Sebák, Fanni and Ecsédi, Péter and Nyitray, László and Bodor, Andrea},
	doi = {10.1007/s12104-023-10160-4},
	journal-iso = {BIOMOL NMR ASSIGM},
	journal = {BIOMOLECULAR NMR ASSIGNMENTS},
	volume = {17},
	unique-id = {34213192},
	issn = {1874-2718},
	abstract = {Protein p53 is mostly known for playing a key role in tumour suppression, and mutations in the p53 gene are amongst the most frequent genomic events accompanying oncogenic transformation. Continuous research is conducted to target disordered proteins/protein regions for cancer therapy, for which atomic level information is also necessary. The disordered N-terminal part of p53 contains the transactivation and the proline-rich domains—which besides being abundant in proline residues—contains repetitive Pro-Ala motifs. NMR assignment of such repetitive, proline-rich regions is challenging due to the lack of amide protons in the 1 H N -detected approaches, as well as due to the small chemical shift dispersion. In the present study we perform the full assignment of the p53 1–100 region by applying a combination of 1 H N - and 1 H α -detected NMR experiments. We also show the increased information content when using real-time homo- and heteronuclear decoupled acquisition schemes. On the other hand, we highlight the presence of minor proline species, and using Pro-selective experiments we determine the corresponding cis or trans conformation. Secondary chemical shifts for (C α –C β ) atoms indicate the disordered nature of this region, with expected helical tendency for the TAD1 region. As the role of the proline-rich domain is yet not well understood our results can contribute to further successful investigations.},
	year = {2023},
	eissn = {1874-270X},
	pages = {309-314},
	orcid-numbers = {Sebák, Fanni/0000-0001-9252-9961; Ecsédi, Péter/0000-0002-4700-125X; Nyitray, László/0000-0003-4717-5994; Bodor, Andrea/0000-0002-7422-298X}
}

@article{MTMT:34087969,
	title = {3D cell segregation geometry and dynamics are governed by tissue surface tension regulation},
	url = {https://m2.mtmt.hu/api/publication/34087969},
	author = {Méhes, Előd and Mones, Enys and Varga, Máté and Zsigmond, Áron and Biri-Kovács, Beáta and Nyitray, László and Barone, Vanessa and Krens, Gabriel and Heisenberg, Carl-Philipp and Vicsek, Tamás},
	doi = {10.1038/s42003-023-05181-7},
	journal-iso = {COMMUN BIOL},
	journal = {COMMUNICATIONS BIOLOGY},
	volume = {6},
	unique-id = {34087969},
	abstract = {Tissue morphogenesis and patterning during development involve the segregation of cell types. Segregation is driven by differential tissue surface tensions generated by cell types through controlling cell-cell contact formation by regulating adhesion and actomyosin contractility-based cellular cortical tensions. We use vertebrate tissue cell types and zebrafish germ layer progenitors as in vitro models of 3-dimensional heterotypic segregation and developed a quantitative analysis of their dynamics based on 3D time-lapse microscopy. We show that general inhibition of actomyosin contractility by the Rho kinase inhibitor Y27632 delays segregation. Cell type-specific inhibition of non-muscle myosin2 activity by overexpression of myosin assembly inhibitor S100A4 reduces tissue surface tension, manifested in decreased compaction during aggregation and inverted geometry observed during segregation. The same is observed when we express a constitutively active Rho kinase isoform to ubiquitously keep actomyosin contractility high at cell-cell and cell-medium interfaces and thus overriding the interface-specific regulation of cortical tensions. Tissue surface tension regulation can become an effective tool in tissue engineering.},
	year = {2023},
	eissn = {2399-3642},
	orcid-numbers = {Méhes, Előd/0000-0003-2697-907X; Varga, Máté/0000-0003-4289-1705; Biri-Kovács, Beáta/0000-0001-5803-9969; Nyitray, László/0000-0003-4717-5994; Heisenberg, Carl-Philipp/0000-0002-0912-4566; Vicsek, Tamás/0000-0003-1431-2884}
}

@article{MTMT:34046199,
	title = {Chlorotoxin binds to both matrix metalloproteinase 2 and neuropilin 1},
	url = {https://m2.mtmt.hu/api/publication/34046199},
	author = {Farkas, Sándor and Cioca, Daniel and Murányi, József and Hornyák, Péter and Brunyánszki, Attila and Szekér, Patrik and Boros, Eszter and Horváth, Patrik and Hujber, Zoltán and Rácz, Gábor Z. and Nagy, Noémi and Tóth, Rebeka and Nyitray, László and Péterfi, Zalán},
	doi = {10.1016/j.jbc.2023.104998},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {299},
	unique-id = {34046199},
	issn = {0021-9258},
	year = {2023},
	eissn = {1083-351X},
	orcid-numbers = {Farkas, Sándor/0000-0001-6666-3112; Murányi, József/0000-0001-5672-6482; Nyitray, László/0000-0003-4717-5994}
}

@article{MTMT:33715979,
	title = {A Novel Fusion Protein System for the Production of Nanobodies and the SARS-CoV-2 Spike RBD in a Bacterial System},
	url = {https://m2.mtmt.hu/api/publication/33715979},
	author = {Nagy-Fazekas, Dóra and Stráner, Pál and Ecsédi, Péter and Taricska, Nóra and Borbély, Adina Noémi and Nyitray, László and Perczel, András},
	doi = {10.3390/bioengineering10030389},
	journal-iso = {BIOENGINEERING-BASEL},
	journal = {BIOENGINEERING},
	volume = {10},
	unique-id = {33715979},
	abstract = {Antibodies are key proteins of the immune system, and they are widely used for both research and theragnostic applications. Among them, camelid immunoglobulins (IgG) differ from the canonical human IgG molecules, as their light chains are completely missing; thus, they have only variable domains on their heavy chains (VHHs). A single VHH domain, often called a nanobody, has favorable structural, biophysical, and functional features compared to canonical antibodies. Therefore, robust and efficient production protocols relying on recombinant technologies are in high demand. Here, by utilizing ecotin, an Escherichia coli protein, as a fusion partner, we present a bacterial expression system that allows an easy, fast, and cost-effective way to prepare nanobodies. Ecotin was used here as a periplasmic translocator and a passive refolding chaperone, which allowed us to reach high-yield production of nanobodies. We also present a new, easily applicable prokaryotic expression and purification method of the receptor-binding domain (RBD) of the SARS-CoV-2 S protein for interaction assays. We demonstrate using ECD spectroscopy that the bacterially produced RBD is well-folded. The bacterially produced nanobody was shown to bind strongly to the recombinant RBD, with a Kd of 10 nM. The simple methods presented here could facilitate rapid interaction measurements in the event of the appearance of additional SARS-CoV-2 variants.},
	year = {2023},
	eissn = {2306-5354},
	orcid-numbers = {Stráner, Pál/0000-0003-2240-8501; Ecsédi, Péter/0000-0002-4700-125X; Taricska, Nóra/0000-0002-9721-953X; Borbély, Adina Noémi/0000-0002-5506-6555; Nyitray, László/0000-0003-4717-5994; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:32785740,
	title = {A scalable strategy to solve structures of PDZ domains and their complexes},
	url = {https://m2.mtmt.hu/api/publication/32785740},
	author = {Cousido-Siah, Alexandra and Carneiro, Laura and Kostmann, Camille and Ecsédi, Péter and Nyitray, László and Trave, Gilles and Gogl, Gergo},
	doi = {10.1107/S2059798322001784},
	journal-iso = {ACTA CRYSTALLOGR D STRUCT BIOL},
	journal = {ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY},
	volume = {78},
	unique-id = {32785740},
	issn = {2059-7983},
	year = {2022},
	eissn = {2059-7983},
	pages = {509-516},
	orcid-numbers = {Cousido-Siah, Alexandra/0000-0002-3051-1560; Ecsédi, Péter/0000-0002-4700-125X; Nyitray, László/0000-0003-4717-5994; Gogl, Gergo/0000-0002-8597-3711}
}

@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}
}

@article{MTMT:32252567,
	title = {Selective 1Hα NMR methods to reveal functionally relevant proline cis/trans isomers in IDPs. Characterization of minor forms, effects of phosphorylation and, occurrence in proteome},
	url = {https://m2.mtmt.hu/api/publication/32252567},
	author = {Sebák, Fanni and Ecsédi, Péter and Bermel, Wolfgang and Burkhard, Luy and Nyitray, László and Bodor, Andrea},
	doi = {10.1002/anie.202108361},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {61},
	unique-id = {32252567},
	issn = {1433-7851},
	abstract = {It is important to identify proline cis/trans isomers that appear in several regulatory mechanisms of proteins, and to characterize minor species that are present due to the conformational heterogeneity in intrinsically disordered proteins (IDPs). To obtain residue level information on these mobile systems we introduce two H-1(alpha)-detected, proline selective, real-time homodecoupled NMR experiments and analyze the proline abundant transactivation domain of p53. The measurements are sensitive enough to identify minor conformers present in 4-15 % amounts; moreover, we show the consequences of CK2 phosphorylation on the cis/trans-proline equilibrium. Using our results and available literature data we perform a statistical analysis on how the amino acid type effects the cis/trans-proline distribution. The methods are applicable under physiological conditions, they can contribute to find key proline isomers in proteins, and statistical analysis results may help in amino acid sequence optimization for biotechnological purposes.},
	year = {2022},
	eissn = {1521-3773},
	orcid-numbers = {Sebák, Fanni/0000-0001-9252-9961; Ecsédi, Péter/0000-0002-4700-125X; Nyitray, László/0000-0003-4717-5994; Bodor, Andrea/0000-0002-7422-298X}
}

@{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:32476060,
	title = {Studying the Structures of Relaxed and Fuzzy Interactions: The Diverse World of S100 Complexes},
	url = {https://m2.mtmt.hu/api/publication/32476060},
	author = {Ecsédi, Péter and Gógl, Gergő and Nyitray, László},
	doi = {10.3389/fmolb.2021.749052},
	journal-iso = {FRONT MOL BIOSCI},
	journal = {FRONTIERS IN MOLECULAR BIOSCIENCES},
	volume = {8},
	unique-id = {32476060},
	abstract = {S100 proteins are small, dimeric, Ca2+-binding proteins of considerable interest due to their associations with cancer and rheumatic and neurodegenerative diseases. They control the functions of numerous proteins by forming protein–protein complexes with them. Several of these complexes were found to display “fuzzy” properties. Examining these highly flexible interactions, however, is a difficult task, especially from a structural biology point of view. Here, we summarize the available in vitro techniques that can be deployed to obtain structural information about these dynamic complexes. We also review the current state of knowledge about the structures of S100 complexes, focusing on their often-asymmetric nature. © Copyright © 2021 Ecsédi, Gógl and Nyitray.},
	keywords = {NMR; S100 Proteins; X-RAY CRYSTALLOGRAPHY; p53; Annexin A2; fuzzy interactions; NM2A; RSK1},
	year = {2021},
	eissn = {2296-889X},
	orcid-numbers = {Ecsédi, Péter/0000-0002-4700-125X; Nyitray, László/0000-0003-4717-5994}
}