@article{MTMT:31876643,
	title = {Insights into graphene oxide interaction with human serum albumin in isolated state and in blood plasma},
	url = {https://m2.mtmt.hu/api/publication/31876643},
	author = {Taneva, Stefka G. and Krumova, Sashka and Bogár, Ferenc and Kincses, András and Stoichev, Svetozar and Todinova, Svetla and Danailova, Avgustina and Horváth, János and Násztor, Zoltán and Kelemen, Lóránd and Dér, András},
	doi = {10.1016/j.ijbiomac.2021.01.151},
	journal-iso = {INT J BIOL MACROMOL},
	journal = {INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES},
	volume = {175},
	unique-id = {31876643},
	issn = {0141-8130},
	year = {2021},
	eissn = {1879-0003},
	pages = {19-29},
	orcid-numbers = {Bogár, Ferenc/0000-0002-0611-1452; Kelemen, Lóránd/0000-0001-7772-2165}
}

@mastersthesis{MTMT:31364361,
	title = {A Hofmeister effektus vizsgálata szimulációs módszerekkel [Investigation of the Hofmeister effect utilizing computational tools]},
	url = {https://m2.mtmt.hu/api/publication/31364361},
	author = {Násztor, Zoltán},
	doi = {10.14232/phd.10377},
	publisher = {SZTE},
	unique-id = {31364361},
	year = {2020}
}

@article{MTMT:3271940,
	title = {Ion-induced alterations of the local hydration environment elucidate Hofmeister effect in a simple classical model of Trp-cage miniprotein},
	url = {https://m2.mtmt.hu/api/publication/3271940},
	author = {Násztor, Zoltán and Dér, András and Bogár, Ferenc},
	doi = {10.1007/s00894-017-3471-0},
	journal-iso = {J MOL MODEL},
	journal = {JOURNAL OF MOLECULAR MODELING},
	volume = {23},
	unique-id = {3271940},
	issn = {1610-2940},
	abstract = {Protein stability is known to be influenced by the presence of Hofmeister active ions in the solution. In addition to direct ion-protein interactions, this influence manifests through the local alterations of the interfacial water structure induced by the anions and cations present in this region. In our earlier works it was pointed out that the effects of Hofmeister active salts on the stability of Trp-cage miniprotein can be modeled qualitatively using non-polarizable force fields. These simulations reproduced the structure-stabilization and structure-destabilization effects of selected kosmotropic and chaotropic salts, respectively. In the present study we use the same model system to elucidate atomic processes behind the chaotropic destabilization and kosmotropic stabilization of the miniprotein. We focus on changes of the local hydration environment of the miniprotein upon addition of NaClO4 and NaF salts to the solution. The process is separated into two parts. In the first, ‘promotion’ phase, the protein structure is fixed, and the local hydration properties induced by the simultaneous presence of protein and ions are investigated, with a special focus on the interaction of Hofmeister active anions with the charged and polar sites. In the second, ‘rearrangement’ phase we follow changes of the hydration of ions and the protein, accompanying the conformational relaxation of the protein. We identify significant factors of an enthalpic and entropic nature behind the ion-induced free energy changes of the protein-water system, and also propose a possible atomic mechanism consistent with the Collins’s rule, for the chaotropic destabilization and kosmotropic stabilization of protein conformation.},
	year = {2017},
	eissn = {0948-5023},
	orcid-numbers = {Bogár, Ferenc/0000-0002-0611-1452}
}

@{MTMT:3149059,
	title = {The Collins's Rule and the Hofmeister Effect as Revealed by a Simple Molecular Dynamics Model},
	url = {https://m2.mtmt.hu/api/publication/3149059},
	author = {Násztor, Zoltán and Der, A and Bogár, Ferenc},
	booktitle = {8th Central European Conference "Chemistry towards Biology"},
	unique-id = {3149059},
	year = {2016},
	pages = {52-53},
	orcid-numbers = {Bogár, Ferenc/0000-0002-0611-1452}
}

@article{MTMT:3104900,
	title = {Characterizing the structural and folding properties of long-sequence hypomurocin B peptides and their analogs},
	url = {https://m2.mtmt.hu/api/publication/3104900},
	author = {Horváth, János and Násztor, Zoltán and Bartha, Ferenc and Bogár, Ferenc and Leitgeb, Balázs},
	doi = {10.1002/bip.22870},
	journal-iso = {BIOPOLYMERS},
	journal = {BIOPOLYMERS},
	volume = {106},
	unique-id = {3104900},
	issn = {0006-3525},
	keywords = {intramolecular H-bond; molecular dynamics; Helical structure; PEPTAIBOL; hypomurocin},
	year = {2016},
	eissn = {1097-0282},
	pages = {645-657},
	orcid-numbers = {Bogár, Ferenc/0000-0002-0611-1452}
}

@article{MTMT:3077934,
	title = {The interfacial tension concept, as revealed by fluctuations},
	url = {https://m2.mtmt.hu/api/publication/3077934},
	author = {Násztor, Zoltán and Bogár, Ferenc and Dér, András},
	doi = {10.1016/j.cocis.2016.05.007},
	journal-iso = {CURR OPIN COLLOID IN},
	journal = {CURRENT OPINION IN COLLOID & INTERFACE SCIENCE},
	volume = {23},
	unique-id = {3077934},
	issn = {1359-0294},
	abstract = {Abstract A simple, didactic model that could have conclusively interpreted the complexity of specific salt (Hofmeister-) effects on protein solubility and function, using a single physical quantity as a central parameter, has long been missing. Via surveying a row of recent papers we show in this review that a phenomenological formalism based on the salt-induced change of protein–water interfacial tension (∆γ) is able to account for a wide range of Hofmeister effects, including also such “exceptions”, where inverse or “V-shaped” Hofmeister series occurs. A close relationship between protein–water interfacial tension and conformational fluctuations is pinpointed on theoretical grounds, then it is shown how one can use a complex experimental arsenal to demonstrate conformational fluctuations on two prototypical proteins, the membrane protein bacteriorhodopsin and the cytoplasmic protein myoglobin. Finally, via the results of recent and new molecular dynamics simulations on a model peptide, the tryptophan-cage miniprotein, independent evidences are given in favor of the interfacial tension concept, at the same time demonstrating the predictive power of the theory. It is shown that salt-induced fluctuation changes of surface-exposed amino acid groups can be used as a sensitive measure for mapping the local features of Hofmeister effects on protein conformations. General implications of the interfacial tension concept are also discussed.},
	keywords = {Conformational fluctuations; Hofmeister effects; Protein–water interfacial tension},
	year = {2016},
	eissn = {1879-0399},
	pages = {29-40},
	orcid-numbers = {Bogár, Ferenc/0000-0002-0611-1452}
}

@article{MTMT:2974666,
	title = {Studying the Structural and Folding Features of Long-Sequence Trichobrachin Peptides},
	url = {https://m2.mtmt.hu/api/publication/2974666},
	author = {Násztor, Zoltán and Horváth, János and Leitgeb, Balázs},
	doi = {10.1002/cbdv.201400280},
	journal-iso = {CHEM BIODIVERS},
	journal = {CHEMISTRY & BIODIVERSITY},
	volume = {12},
	unique-id = {2974666},
	issn = {1612-1872},
	abstract = {In this theoretical study, the folding processes of long-sequence trichobrachin peptides (i.e., TB IIb peptides) were investigated by molecular dynamics methods. The formation of various helical structures (i.e., 3<inf>10</inf>-, α-, and left-handed α-helices) was studied with regard to the entire sequence of peptides, as well as to each amino acid. The results pointed out that TB IIb molecules showed a propensity to form helical conformations, and they could be characterized by 3<inf>10</inf>-helical structure rather than by α-helical structure. The formation of local (i.e., i←i+3 and i←i+4) as well as of non-local (i.e., i←i+n, where n>4; and all i→i+n) H-bonds was also examined. The results revealed that the occurrence of local, helix-stabilizing H-bonds was in agreement with the appearance of helical conformations, and the non-local H-bonds did not produce relevant effects on the evolution of helical structures. Based on the data obtained by our structural investigation, differences were observed between the TB IIb peptides, according to the type of amino acid located in the 17th position of their sequences. In summary, the folding processes were explored for TB IIb molecules, and our theoretical study led to the conclusion that these long-sequence peptaibols showed characteristic structural and folding features. © 2015 Verlag Helvetica Chimica Acta AG, Zrich.},
	keywords = {ARTICLE; amino acid sequence; nonhuman; Protein Folding; Protein Conformation; unclassified drug; crystal structure; theoretical study; helical structures; molecular dynamics; molecular evolution; alpha helix; intramolecular H-bonds; peptide derivative; fungal protein; Peptaibols; PEPTAIBOL; ALAMETHICIN; Trichobrachins; trichobrachin peptide},
	year = {2015},
	eissn = {1612-1880},
	pages = {1365-1377}
}

@article{MTMT:2942329,
	title = {Opposite effect of Ca2+/Mg2+ ions on the aggregation of native and precursor-derived Aβ42},
	url = {https://m2.mtmt.hu/api/publication/2942329},
	author = {Bogár, Ferenc and Simon, Dóra and Bozsó, Zsolt and Janáky, Tamás and Veszelka, Szilvia and Tóth, Andrea and Deli, Mária Anna and Borics, Attila and Násztor, Zoltán and Gyebrovszki, A and Penke, Botond and Fülöp, Lívia},
	doi = {10.1007/s11224-015-0660-2},
	journal-iso = {STRUCT CHEM},
	journal = {STRUCTURAL CHEMISTRY},
	volume = {26},
	unique-id = {2942329},
	issn = {1040-0400},
	year = {2015},
	eissn = {1572-9001},
	pages = {1389-1403},
	orcid-numbers = {Bogár, Ferenc/0000-0002-0611-1452; Bozsó, Zsolt/0000-0002-5713-3096; Janáky, Tamás/0000-0002-6466-8283; Deli, Mária Anna/0000-0001-6084-6524; Penke, Botond/0000-0003-0938-0567; Fülöp, Lívia/0000-0002-8010-0129}
}

@article{MTMT:2807137,
	title = {In Silico Conformational Analysis of the Short-Sequence Hypomurocin A Peptides},
	url = {https://m2.mtmt.hu/api/publication/2807137},
	author = {Násztor, Zoltán and Horváth, János and Leitgeb, Balázs},
	doi = {10.1155/2015/281065},
	journal-iso = {INT J PEPTIDES},
	journal = {INTERNATIONAL JOURNAL OF PEPTIDES},
	volume = {2015},
	unique-id = {2807137},
	issn = {1687-9767},
	year = {2015},
	eissn = {1687-9775}
}

@article{MTMT:2711661,
	title = {On the Hofmeister Effect: Fluctuations at the Protein-Water Interface and the Surface Tension.},
	url = {https://m2.mtmt.hu/api/publication/2711661},
	author = {Bogár, Ferenc and Bartha, Ferenc and Násztor, Zoltán and Fábián, László and Leitgeb, Balázs and Dér, András},
	doi = {10.1021/jp502505c},
	journal-iso = {J PHYS CHEM B},
	journal = {JOURNAL OF PHYSICAL CHEMISTRY B},
	volume = {118},
	unique-id = {2711661},
	issn = {1520-6106},
	abstract = {We performed mol. dynamics simulations on the tryptophane-cage miniprotein using a nonpolarizable force field, in order to model the effect of concd. water solns. of neutral salts on protein conformation, which is a manifestation of Hofmeister effects. From the equil. values and the fluctuations of the solvent accessible surface area of the miniprotein, the salt-induced changes of the mean value of protein-water interfacial tension were detd. At 300 K, the chaotropic ClO4- and NO3- decreased the interfacial tension according to their position in the Hofmeister series (by approx. 5 and 2.7 mN/m, resp.), while the kosmotropic F- increased it (by 1 mN/m). These values were compared to those obtained from the Gibbs equation using the excess surface adsorption calcd. from the probability distribution of the water mols. and ions around the miniprotein, and the two sets were found to be very close to each other. Our results present a direct evidence for the central role of interfacial tension and fluctuations at the protein-water interface in Hofmeister phenomena, and provide a computational method for the detn. of the protein-water interfacial tension, establishing a link between the phenomenol. and microscopic description of protein-water interfaces. [on SciFinder(R)]},
	year = {2014},
	eissn = {1520-5207},
	pages = {8496-8504},
	orcid-numbers = {Bogár, Ferenc/0000-0002-0611-1452}
}