@CONFERENCE{MTMT:34821191,
	title = {Chemical differences in the non-protected carbon pool of four Hungarian soils with different vegetation types},
	url = {https://m2.mtmt.hu/api/publication/34821191},
	author = {Filep, Tibor and Zacháry, Dóra and Tőke, Orsolya and Domján, Attila and Szalai, Zoltán},
	booktitle = {EGU General Assembly 2024 : abstracts},
	doi = {10.5194/egusphere-egu24-8025},
	unique-id = {34821191},
	year = {2024},
	orcid-numbers = {Szalai, Zoltán/0000-0001-5267-411X}
}

@article{MTMT:34510717,
	title = {Dynamic Structures of Bioactive Proteins as Determined by Nuclear Magnetic Resonance},
	url = {https://m2.mtmt.hu/api/publication/34510717},
	author = {Tőke, Orsolya and Batta, Gyula},
	doi = {10.3390/ijms25010295},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {25},
	unique-id = {34510717},
	issn = {1661-6596},
	abstract = {According to “Panta rhei”, a phrase by the ancient Greeks, you cannot enter the same river two times [...]},
	year = {2024},
	eissn = {1422-0067},
	orcid-numbers = {Tőke, Orsolya/0000-0002-1741-1573; Batta, Gyula/0000-0002-0442-1828}
}

@article{MTMT:34499234,
	title = {Substantial solubility and fluorescence property changes upon inclusion of rutaecarpine in cucurbit[7]uril: Kinetics and thermodynamics of binding},
	url = {https://m2.mtmt.hu/api/publication/34499234},
	author = {Miskolczy, Zsombor and Megyesi, Mónika and Turczel, Gábor and Tőke, Orsolya and Biczók, László},
	doi = {10.1016/j.molliq.2024.124019},
	journal-iso = {J MOL LIQ},
	journal = {JOURNAL OF MOLECULAR LIQUIDS},
	volume = {396},
	unique-id = {34499234},
	issn = {0167-7322},
	year = {2024},
	eissn = {1873-3166},
	orcid-numbers = {Turczel, Gábor/0000-0002-6753-6796; Biczók, László/0000-0003-2568-5942}
}

@article{MTMT:34510707,
	title = {Three Decades of REDOR in Protein Science: A Solid-State NMR Technique for Distance Measurement and Spectral Editing},
	url = {https://m2.mtmt.hu/api/publication/34510707},
	author = {Tőke, Orsolya},
	doi = {10.3390/ijms241713637},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {34510707},
	issn = {1661-6596},
	abstract = {Solid-state NMR (ss-NMR) is a powerful tool to investigate noncrystallizable, poorly soluble molecular systems, such as membrane proteins, amyloids, and cell walls, in environments that closely resemble their physical sites of action. Rotational-echo double resonance (REDOR) is an ss-NMR methodology, which by reintroducing heteronuclear dipolar coupling under magic angle spinning conditions provides intramolecular and intermolecular distance restraints at the atomic level. In addition, REDOR can be exploited as a selection tool to filter spectra based on dipolar couplings. Used extensively as a spectroscopic ruler between isolated spins in site-specifically labeled systems and more recently as a building block in multidimensional ss-NMR pulse sequences allowing the simultaneous measurement of multiple distances, REDOR yields atomic-scale information on the structure and interaction of proteins. By extending REDOR to the determination of 1H–X dipolar couplings in recent years, the limit of measurable distances has reached ~15–20 Å, making it an attractive method of choice for the study of complex biomolecular assemblies. Following a methodological introduction including the most recent implementations, examples are discussed to illustrate the versatility of REDOR in the study of biological systems.},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Tőke, Orsolya/0000-0002-1741-1573}
}

@article{MTMT:34093500,
	title = {Effect of inclusion in sulfobutylether-β-cyclodextrin on the rate of merocyanine-spirobenzopyran reversible photochromic transformations},
	url = {https://m2.mtmt.hu/api/publication/34093500},
	author = {Miskolczy, Zsombor and Megyesi, Mónika and Turczel, Gábor and Tőke, Orsolya and Biczók, László},
	doi = {10.1016/j.dyepig.2023.111611},
	journal-iso = {DYES PIGMENTS},
	journal = {DYES AND PIGMENTS},
	volume = {219},
	unique-id = {34093500},
	issn = {0143-7208},
	year = {2023},
	eissn = {1873-3743},
	orcid-numbers = {Tőke, Orsolya/0000-0002-1741-1573; Biczók, László/0000-0003-2568-5942}
}

@article{MTMT:33660819,
	title = {Disordered-ordered protein binary classification by circular dichroism spectroscopy},
	url = {https://m2.mtmt.hu/api/publication/33660819},
	author = {Micsonai, András and Moussong, Éva and Murvai, Nikoletta and Tantos, Ágnes and Tőke, Orsolya and Réfrégiers, Matthieu and Wien, Frank and Kardos, József},
	doi = {10.1016/j.bpj.2022.11.1915},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {122},
	unique-id = {33660819},
	issn = {0006-3495},
	year = {2023},
	eissn = {1542-0086},
	pages = {344a},
	orcid-numbers = {Micsonai, András/0000-0002-2539-4080; Kardos, József/0000-0002-2135-2932}
}

@article{MTMT:33174847,
	title = {Multiple Timescale Dynamic Analysis of Functionally-Impairing Mutations in Human Ileal Bile Acid-Binding Protein},
	url = {https://m2.mtmt.hu/api/publication/33174847},
	author = {Horváth, Gergő and Balterer, Bence and Micsonai, András and Kardos, József and Tőke, Orsolya},
	doi = {10.3390/ijms231911346},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {23},
	unique-id = {33174847},
	issn = {1661-6596},
	abstract = {Human ileal bile acid-binding protein (hI-BABP) has a key role in the enterohepatic circulation of bile salts. Its two internal binding sites exhibit positive cooperativity accompanied by a site-selectivity of glycocholate (GCA) and glycochenodeoxycholate (GCDA), the two most abundant bile salts in humans. To improve our understanding of the role of dynamics in ligand binding, we introduced functionally impairing single-residue mutations at two key regions of the protein and subjected the mutants to NMR relaxation analysis and MD simulations. According to our results, mutation in both the vicinity of the C/D (Q51A) and the G/H (Q99A) turns results in a redistribution of motional freedom in apo hI-BABP. Mutation Q51A, deteriorating the site-selectivity of GCA and GCDA, results in the channeling of ms fluctuations into faster motions in the binding pocket hampering the realization of key side chain interactions. Mutation Q99A, abolishing positive binding cooperativity for GCDA, leaves ms motions in the C-terminal half unchanged but by decoupling βD from a dynamic cluster of the N-terminal half displays an increased flexibility in the vicinity of site 1. MD simulations of the variants indicate structural differences in the portal region and mutation-induced changes in dynamics, which depend on the protonation state of histidines. A dynamic coupling between the EFGH portal, the C/D-region, and the helical cap is evidenced highlighting the interplay of structural and dynamic effects in bile salt recognition in hI-BABP.},
	year = {2022},
	eissn = {1422-0067},
	orcid-numbers = {Micsonai, András/0000-0002-2539-4080; Kardos, József/0000-0002-2135-2932; Tőke, Orsolya/0000-0002-1741-1573}
}

@article{MTMT:32924494,
	title = {The Importance of Mg2+‐free State in Nucleotide Exchange of Oncogenic K‐Ras Mutants},
	url = {https://m2.mtmt.hu/api/publication/32924494},
	author = {Pálfy, Gyula and Karancsiné Menyhárd, Dóra and Ákontz-Kiss, Hanna and Vida, István and Batta, Gyula and Tőke, Orsolya and Perczel, András},
	doi = {10.1002/chem.202201449},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {28},
	unique-id = {32924494},
	issn = {0947-6539},
	abstract = {For efficient targeting of oncogenic K-Ras interaction sites, a mechanistic picture of the Ras-cycle is necessary. Herein, we used NMR relaxation techniques and molecular dynamics simulations to decipher the role of slow dynamics in wild-type and three oncogenic P-loop mutants of K-Ras. Our measurements reveal a dominant two-state conformational exchange on the ms timescale in both GDP- and GTP-bound KRas. The identified low-populated higher energy state in GDPloaded K-Ras has a conformation reminiscent of a nucleotidebound/Mg2+-free state characterized by shortened β2/β3-strands and a partially released switch-I region preparing K-Ras for the interaction with the incoming nucleotide exchange factor and subsequent reactivation. By providing insight into mutationspecific differences in K-Ras structural dynamics, our systematic analysis improves our understanding of prolonged K-Ras signaling and may aid the development of allosteric inhibitors targeting nucleotide exchange in K-Ras.},
	keywords = {NMR spectroscopy; K-RAS; molecular dynamics; Slow dynamics; Ras cycle},
	year = {2022},
	eissn = {1521-3765},
	orcid-numbers = {Pálfy, Gyula/0000-0003-1590-5331; Karancsiné Menyhárd, Dóra/0000-0002-0095-5531; Batta, Gyula/0000-0002-0442-1828; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:32819946,
	title = {Disordered–Ordered Protein Binary Classification by Circular Dichroism Spectroscopy},
	url = {https://m2.mtmt.hu/api/publication/32819946},
	author = {Micsonai, András and Moussong, Éva and Murvai, Nikoletta and Tantos, Ágnes and Tőke, Orsolya and Réfrégiers, Matthieu and Wien, Frank and Kardos, József},
	doi = {10.3389/fmolb.2022.863141},
	journal-iso = {FRONT MOL BIOSCI},
	journal = {FRONTIERS IN MOLECULAR BIOSCIENCES},
	volume = {9},
	unique-id = {32819946},
	year = {2022},
	eissn = {2296-889X},
	orcid-numbers = {Micsonai, András/0000-0002-2539-4080; Kardos, József/0000-0002-2135-2932}
}

@article{MTMT:32590583,
	title = {Structural and Dynamic Determinants of Molecular Recognition in Bile Acid-Binding Proteins},
	url = {https://m2.mtmt.hu/api/publication/32590583},
	author = {Tőke, Orsolya},
	doi = {10.3390/ijms23010505},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {23},
	unique-id = {32590583},
	issn = {1661-6596},
	year = {2022},
	eissn = {1422-0067}
}