@article{MTMT:35835997,
	title = {Guide to the structural characterization of protein aggregates and amyloid fibrils by CD spectroscopy},
	url = {https://m2.mtmt.hu/api/publication/35835997},
	author = {Kardos, József and Nyiri, Márton Péter and Moussong, Éva and Wien, Frank and Molnár, Tamás and Murvai, Nikoletta and Tóth, Vilmos and Vadászi, Henrietta and Kun, Judit and Jamme, Frederic and Micsonai, András},
	doi = {10.1002/pro.70066},
	journal-iso = {PROTEIN SCI},
	journal = {PROTEIN SCIENCE},
	volume = {34},
	unique-id = {35835997},
	issn = {0961-8368},
	keywords = {AMYLOID-BETA; Alzheimer's disease; circular dichroism spectroscopy; protein aggregation; amyloid formation; SECONDARY STRUCTURE ESTIMATION; BeStSel},
	year = {2025},
	eissn = {1469-896X},
	orcid-numbers = {Kardos, József/0000-0002-2135-2932; Nyiri, Márton Péter/0009-0006-6035-2931; Wien, Frank/0000-0002-0752-8735; Molnár, Tamás/0000-0002-6842-2715; Murvai, Nikoletta/0000-0001-7477-0911; Tóth, Vilmos/0000-0001-8087-4880; Micsonai, András/0000-0002-2539-4080}
}

@article{MTMT:36141720,
	title = {BeStSel: analysis site for protein CD spectra—2025 update},
	url = {https://m2.mtmt.hu/api/publication/36141720},
	author = {Micsonai, András and Wien, Frank and Murvai, Nikoletta and Nyiri, Márton Péter and Balatoni, Bori and Lee, Young-Ho and Molnár, Tamás and Goto, Yuji and Jamme, Frédéric and Kardos, József},
	doi = {10.1093/nar/gkaf378},
	journal-iso = {NUCLEIC ACIDS RES},
	journal = {NUCLEIC ACIDS RESEARCH},
	volume = {53},
	unique-id = {36141720},
	issn = {0305-1048},
	abstract = {Circular dichroism (CD) spectroscopy is a widely used technique to characterize the secondary structure composition of proteins. We have developed the Beta Structure Selection (BeStSel) method (PNAS, 112, E3095), which solves the main problem of protein CD spectroscopy—namely, the spectral variability of β-structures. The BeStSel web server utilizes this method to provide tools to the community for CD spectrum analysis. BeStSel uniquely provides information on eight secondary structure components, including parallel β-structure and antiparallel β-sheets with three different twist groups. It outperforms all available methods in accuracy and information content, and is also able to predict protein folds down to the topology/homology level of the CATH classification. The algorithm has been further developed, and the accuracy of the estimation of the secondary structure elements is improved by 0.7% as an average on the reference dataset. A new module of the web server calculates protein stability from the thermal denaturation profile followed by CD. Secondary structure calculations of uploaded PDB and mmcif files support the experimental verification of MD simulations and AlphaFold models by CD spectroscopy. Well-proven modules for disorder–order classification and extinction coefficient calculation continue to work. The BeStSel server is freely accessible at https://bestsel.elte.hu.},
	year = {2025},
	eissn = {1362-4962},
	pages = {W73-W83},
	orcid-numbers = {Micsonai, András/0000-0002-2539-4080; Wien, Frank/0000-0002-0752-8735; Murvai, Nikoletta/0000-0001-7477-0911; Nyiri, Márton Péter/0009-0006-6035-2931; Molnár, Tamás/0000-0002-6842-2715; Goto, Yuji/0000-0003-1221-1270; Jamme, Frédéric/0000-0002-7398-7868; Kardos, József/0000-0002-2135-2932}
}

@article{MTMT:36172461,
	title = {Molecular encapsulation of the aminosteroid phytotoxins solanidine and α-solanine by sugammadex: new insights into atomic-level interactions},
	url = {https://m2.mtmt.hu/api/publication/36172461},
	author = {Kalydi, Eszter and Murvai, Nikoletta and Saridakis, Emmanuel and Mavridis, Irene M. and Malanga, Milo and Kardos, József and Yannakopoulou, Konstantina and Béni, Szabolcs},
	doi = {10.1016/j.carbpol.2025.123824},
	journal-iso = {CARBOHYD POLYM},
	journal = {CARBOHYDRATE POLYMERS},
	volume = {366},
	unique-id = {36172461},
	issn = {0144-8617},
	year = {2025},
	eissn = {1879-1344},
	orcid-numbers = {Murvai, Nikoletta/0000-0001-7477-0911; Kardos, József/0000-0002-2135-2932; Béni, Szabolcs/0000-0001-7056-6825}
}

@article{MTMT:36335112,
	title = {BPS2025 - From prediction to proof: High-throughput validation of AlphaFold-generated structures by circular dichroism spectroscopy},
	url = {https://m2.mtmt.hu/api/publication/36335112},
	author = {Kardos, József and Wien, Frank and Moussong, Éva and Murvai, Nikoletta and Nyiri, Márton Péter and Molnár, Tamás and Jamme, Frederic and Micsonai, András},
	doi = {10.1016/j.bpj.2024.11.1184},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {124},
	unique-id = {36335112},
	issn = {0006-3495},
	year = {2025},
	eissn = {1542-0086},
	pages = {214a},
	orcid-numbers = {Kardos, József/0000-0002-2135-2932; Murvai, Nikoletta/0000-0001-7477-0911; Nyiri, Márton Péter/0009-0006-6035-2931; Molnár, Tamás/0000-0002-6842-2715; Micsonai, András/0000-0002-2539-4080}
}

@article{MTMT:33641256,
	title = {Effect of nanoparticles on the aggregation and amyloid formation of amyloid-beta peptide},
	url = {https://m2.mtmt.hu/api/publication/33641256},
	author = {Moussong, Éva and Nyiri, Márton Péter and Murvai, Nikoletta and Kun, Judit and Kovács, Attila and Molnár, Tamás and Micsonai, András and Kardos, József},
	doi = {10.1016/j.bpj.2022.11.1854},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {122},
	unique-id = {33641256},
	issn = {0006-3495},
	year = {2023},
	eissn = {1542-0086},
	pages = {332a},
	orcid-numbers = {Nyiri, Márton Péter/0009-0006-6035-2931; Murvai, Nikoletta/0000-0001-7477-0911; Molnár, Tamás/0000-0002-6842-2715; Micsonai, András/0000-0002-2539-4080; Kardos, József/0000-0002-2135-2932}
}

@article{MTMT:33641398,
	title = {Bestsel: Updated webserver for secondary structure and fold prediction for protein CD spectroscopy},
	url = {https://m2.mtmt.hu/api/publication/33641398},
	author = {Micsonai, András and Moussong, Éva and Wien, Frank and Boros, Eszter and Vadászi, Henrietta and Murvai, Nikoletta and Lee, Young-Ho and Molnár, Tamás and Réfrégiers, Matthieu and Goto, Yuji and Tantos, Ágnes and Kardos, József},
	doi = {10.1016/j.bpj.2022.11.1110},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {122},
	unique-id = {33641398},
	issn = {0006-3495},
	year = {2023},
	eissn = {1542-0086},
	pages = {179a},
	orcid-numbers = {Micsonai, András/0000-0002-2539-4080; Murvai, Nikoletta/0000-0001-7477-0911; Molnár, Tamás/0000-0002-6842-2715; Kardos, József/0000-0002-2135-2932}
}

@article{MTMT:33641452,
	title = {Inhibition studies on aggregation and cytotoxicity of Alzheimer's amyloid-β peptide},
	url = {https://m2.mtmt.hu/api/publication/33641452},
	author = {Murvai, Nikoletta and Lin, Yuxi and Molnár, Tamás and Kovács, Attila and Micsonai, András and Kyu Bang, Jeong and Lee, Young-Ho and Kardos, József},
	doi = {10.1016/j.bpj.2022.11.1945},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {122},
	unique-id = {33641452},
	issn = {0006-3495},
	year = {2023},
	eissn = {1542-0086},
	pages = {350a-351a},
	orcid-numbers = {Murvai, Nikoletta/0000-0001-7477-0911; Molnár, Tamás/0000-0002-6842-2715; Micsonai, András/0000-0002-2539-4080; Kardos, József/0000-0002-2135-2932}
}

@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; Murvai, Nikoletta/0000-0001-7477-0911; Kardos, József/0000-0002-2135-2932}
}

@article{MTMT:34141758,
	title = {Cross-Linked α-Synuclein as Inhibitor of Amyloid Formation},
	url = {https://m2.mtmt.hu/api/publication/34141758},
	author = {Murvai, Nikoletta and Gellén, Gabriella and Micsonai, András and Schlosser, Gitta and Kardos, József},
	doi = {10.3390/ijms241713403},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {34141758},
	issn = {1661-6596},
	abstract = {The aggregation and amyloid formation of α-synuclein is associated with Parkinson’s disease and other synucleinopathies. In its native, monomeric form α-synuclein is an intrinsically disordered protein represented by highly dynamic conformational ensembles. Inhibition of α-synuclein aggregation using small molecules, peptides, or proteins has been at the center of interest in recent years. Our aim was to explore the effects of cross-linking on the structure and aggregation/amyloid formation properties of α-synuclein. Comparative analysis of available high-resolution amyloid structures and representative structural models and MD trajectory of monomeric α-synuclein revealed that potential cross-links in the monomeric protein are mostly incompatible with the amyloid forms and thus might inhibit fibrillation. Monomeric α-synuclein has been intramolecularly chemically cross-linked under various conditions using different cross-linkers. We determined the location of cross-links and their frequency using mass spectrometry and found that most of them cannot be realized in the amyloid structures. The inhibitory potential of cross-linked proteins has been experimentally investigated using various methods, including thioflavin-T fluorescence and transmission electron microscopy. We found that conformational constraints applied by cross-linking fully blocked α-synuclein amyloid formation. Moreover, DTSSP-cross-linked molecules exhibited an inhibitory effect on the aggregation of unmodified α-synuclein as well.},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Murvai, Nikoletta/0000-0001-7477-0911; Micsonai, András/0000-0002-2539-4080; Schlosser, Gitta/0000-0002-7637-7133; Kardos, József/0000-0002-2135-2932}
}

@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},
	abstract = {Intrinsically disordered proteins lack a stable tertiary structure and form dynamic conformational ensembles due to their characteristic physicochemical properties and amino acid composition. They are abundant in nature and responsible for a large variety of cellular functions. While numerous bioinformatics tools have been developed for <jats:italic>in silico</jats:italic> disorder prediction in the last decades, there is a need for experimental methods to verify the disordered state. CD spectroscopy is widely used for protein secondary structure analysis. It is usable in a wide concentration range under various buffer conditions. Even without providing high-resolution information, it is especially useful when NMR, X-ray, or other techniques are problematic or one simply needs a fast technique to verify the structure of proteins. Here, we propose an automatized binary disorder–order classification method by analyzing far-UV CD spectroscopy data. The method needs CD data at only three wavelength points, making high-throughput data collection possible. The mathematical analysis applies the <jats:italic>k</jats:italic>-nearest neighbor algorithm with cosine distance function, which is independent of the spectral amplitude and thus free of concentration determination errors. Moreover, the method can be used even for strong absorbing samples, such as the case of crowded environmental conditions, if the spectrum can be recorded down to the wavelength of 212 nm. We believe the classification method will be useful in identifying disorder and will also facilitate the growth of experimental data in IDP databases. The method is implemented on a webserver and freely available for academic users.},
	year = {2022},
	eissn = {2296-889X},
	orcid-numbers = {Micsonai, András/0000-0002-2539-4080; Murvai, Nikoletta/0000-0001-7477-0911; Kardos, József/0000-0002-2135-2932}
}