@article{MTMT:32836988,
	title = {Control of plasmonic field enhancement by mode-mixing},
	url = {https://m2.mtmt.hu/api/publication/32836988},
	author = {Pápa, Zsuzsanna and Sándor, Péter and Lovász, Béla and Budai, Judit and Kasza, József and Márton, Zsuzsanna and Jójárt, Péter and Seres, Imre and Bengery, Zsolt Gábor and Németh, Csaba and Dombi, Péter and Rácz, Péter},
	doi = {10.1063/5.0072168},
	journal-iso = {APPL PHYS LETT},
	journal = {APPLIED PHYSICS LETTERS},
	volume = {120},
	unique-id = {32836988},
	issn = {0003-6951},
	year = {2022},
	eissn = {1077-3118},
	orcid-numbers = {Pápa, Zsuzsanna/0000-0003-3567-6468; Budai, Judit/0000-0001-9156-2233; Márton, Zsuzsanna/0000-0001-7625-3571; Jójárt, Péter/0000-0002-5161-2723; Dombi, Péter/0000-0002-0736-3512; Rácz, Péter/0000-0001-5099-1031}
}

@article{MTMT:32461679,
	title = {Combination of multifunctional ursolic acid with kinase inhibitors for anti-cancer drug carrier vesicles},
	url = {https://m2.mtmt.hu/api/publication/32461679},
	author = {Lőrincz, András and Mihály, Judith and Wacha, András Ferenc and Németh, Csaba and Besztercei, Balázs and Gyulavári, Pál and Varga, Zoltán and Peták, István and Bóta, Attila},
	doi = {10.1016/j.msec.2021.112481},
	journal-iso = {MAT SCI ENG C-MATER},
	journal = {MATERIALS SCIENCE & ENGINEERING C-MATERIALS FOR BIOLOGICAL APPLICATIONS},
	volume = {131},
	unique-id = {32461679},
	issn = {0928-4931},
	year = {2021},
	eissn = {1873-0191},
	orcid-numbers = {Wacha, András Ferenc/0000-0002-9609-0893; Besztercei, Balázs/0000-0002-5636-284X; Gyulavári, Pál/0000-0002-5850-0441; Varga, Zoltán/0000-0002-5741-2669; Peták, István/0000-0003-0422-9286}
}

@article{MTMT:32431325,
	title = {Structural studies of ligand stabilized Ni/Ga clusters by means of vibrational spectroscopy and theoretical calculations},
	url = {https://m2.mtmt.hu/api/publication/32431325},
	author = {Mink, János and Staiger, Lena and Muhr, Maximilian and Gemel, Christian and Drees, Markus and Hajba, László and Mihály, Judith and Németh, Csaba and Lokshin, Boris V and Hemmer, Karina and Schutz, Max and Cokoja, Mirza and Fischer, Roland A.},
	doi = {10.1002/jrs.6199},
	journal-iso = {J RAMAN SPECTROSC},
	journal = {JOURNAL OF RAMAN SPECTROSCOPY},
	volume = {52},
	unique-id = {32431325},
	issn = {0377-0486},
	abstract = {In order to explain the different catalytic activity in hydrogenation of two new intermetallic Ni/Ga clusters, [Ga-7](NiCp*)(6) (1A) and [NiGa6](NiCp*)(6) (1B) (Cp* = C5Me5), investigations of structure-function relationship have been performed based on Raman and infrared (IR) spectroscopy and theoretical (density functional theory [DFT] and normal coordinate) calculations. Full interpretation of the Raman, far-IR, and mid-IR spectra of these dark colored solids has been proposed. Based on the overview of metal-Cp* complexes, all the 14 characteristic Cp*(-) skeletal fundamental modes have been identified. By comparison of the Ni-Cp* stretching and tilting external modes (350-380 cm(-1)), their force constants, and bond lengths, cluster 1B exhibited slightly stronger metal-ligand bonding. Vibrations of Ga-7 and NiGa6 cluster cores showed that the stretching wavenumbers and force constants of Ni-Ga (100-350 cm(-1)) and Ga-Ga (60-250 cm(-1)) bonds are higher for cluster 1B, in agreement with the shorter averaged experimental and calculated bond lengths of Ga-Ga bonds (2.873 and 2823 angstrom for clusters 1A and 1B, respectively). Cluster hydrogenation experiments with H-2 and D-2 showed strong Ni-H and N-D stretching features (at 1750 and 1260 cm(-1), respectively), and at the same time, characteristic bands of self-hydrogenated Cp*H and remained nondegraded clusters have been detected. The extent of H-D exchange in cluster deuteration was obtained about 1.5 times more effective with cluster 1B than cluster 1A. The stronger hydrogen or deuterium uptake by cluster 1B and the more intensive self-hydrogenation of Cp* clearly support the higher hydrogenation activity of cluster 1B compared with that of 1A.},
	keywords = {DFT; Raman; Infrared; Far infrared; cluster catalysis},
	year = {2021},
	eissn = {1097-4555},
	pages = {2317-2337},
	orcid-numbers = {Muhr, Maximilian/0000-0002-6977-5002; Hajba, László/0000-0001-7937-4854}
}

@article{MTMT:32035457,
	title = {Surface enhanced Raman spectroscopic (SERS) behavior of phenylpyruvates used in heterogeneous catalytic asymmetric cascade reaction},
	url = {https://m2.mtmt.hu/api/publication/32035457},
	author = {Tálas, Emília and Szőllősi, György and Kristyán, Sándor and Németh, Csaba and Firkala, Tamás and Mink, János and Mihály, Judith},
	doi = {10.1016/j.saa.2021.119912},
	journal-iso = {SPECTROCHIM ACTA A},
	journal = {SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY},
	volume = {260},
	unique-id = {32035457},
	issn = {1386-1425},
	year = {2021},
	eissn = {1873-3557},
	orcid-numbers = {Szőllősi, György/0000-0003-4418-9530}
}

@article{MTMT:31819362,
	title = {(Me 2 NH 2 ) 10 [H 2 -Dodecatungstate] polymorphs: dodecatungstate cages embedded in a variable dimethylammonium cation + water of crystallization matrix},
	url = {https://m2.mtmt.hu/api/publication/31819362},
	author = {Lendvay, György and Majzik, Eszter and Nagyné Bereczki, Laura and Domján, Attila and Trif, László and Sajó, István and Paiva Franguelli, Fernanda and Farkas, Attila and Klébert, Szilvia and Bombicz, Petra and Németh, Csaba and Szilágyi, Imre Miklós and Kótai, László},
	doi = {10.1039/d0ra09997j},
	journal-iso = {RSC ADV},
	journal = {RSC ADVANCES},
	volume = {11},
	unique-id = {31819362},
	issn = {2046-2069},
	year = {2021},
	eissn = {2046-2069},
	pages = {3713-3724},
	orcid-numbers = {Lendvay, György/0000-0002-2150-0376; Trif, László/0000-0002-3960-1829; Sajó, István/0000-0002-1228-1407; Paiva Franguelli, Fernanda/0000-0003-2463-6970; Farkas, Attila/0000-0002-8877-2587; Klébert, Szilvia/0000-0002-3107-3371; Bombicz, Petra/0000-0002-5509-1515; Kótai, László/0000-0001-6375-3120}
}

@article{MTMT:31602701,
	title = {Deuteration and Vibrational Spectra of Dimethylammonium Paratungstate-B hydrates},
	url = {https://m2.mtmt.hu/api/publication/31602701},
	author = {Paiva Franguelli, Fernanda and Lendvay, György and Trif, László and Németh, Csaba and Farkas, Attila and Klébert, Szilvia and Nagyné Bereczki, Laura and Szilágyi, Imre Miklós and Kótai, László},
	doi = {10.1002/zaac.202000283},
	journal-iso = {Z ANORG ALLG CHEM},
	journal = {ZEITSCHRIFT FUR ANORGANISCHE UND ALLGEMEINE CHEMIE},
	volume = {647},
	unique-id = {31602701},
	issn = {0044-2313},
	year = {2021},
	eissn = {1521-3749},
	pages = {593-598},
	orcid-numbers = {Lendvay, György/0000-0002-2150-0376; Trif, László/0000-0002-3960-1829; Farkas, Attila/0000-0002-8877-2587; Klébert, Szilvia/0000-0002-3107-3371}
}

@article{MTMT:31344066,
	title = {Reagent-free total protein quantification of intact extracellular vesicles by attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopy},
	url = {https://m2.mtmt.hu/api/publication/31344066},
	author = {Szentirmai, Veronika and Wacha, András Ferenc and Németh, Csaba and Kitka, Diána and Rácz, Anita and Héberger, Károly and Mihály, Judith and Varga, Zoltán},
	doi = {10.1007/s00216-020-02711-8},
	journal-iso = {ANAL BIOANAL CHEM},
	journal = {ANALYTICAL AND BIOANALYTICAL CHEMISTRY},
	volume = {412},
	unique-id = {31344066},
	issn = {1618-2642},
	abstract = {Extracellular vesicles (EVs) are lipid bilayer-bounded particles that are actively synthesized and released by cells. The main components of EVs are lipids, proteins, and nucleic acids and their composition is characteristic to their type and origin, and it reveals the physiological and pathological conditions of the parent cells. The concentration and protein composition of EVs closely relate to their functions; therefore, total protein determination can assist in EV-based diagnostics and disease prognosis. Here, we present a simple, reagent-free method based on attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopy to quantify the protein content of EV samples without any further sample preparation. After calibration with bovine serum albumin, the protein concentration of red blood cell-derived EVs (REVs) were investigated by ATR-FTIR spectroscopy. The integrated area of the amide I band was calculated from the IR spectra of REVs, which was proportional to the protein quantity in the sample, regardless of its secondary structure. A spike test and a dilution test were performed to determine the ability to use ATR-FTIR spectroscopy for protein quantification in EV samples, which resulted in linearity with R-2 values as high as 0.992 over the concentration range of 0.08 to 1 mg/mL. Additionally, multivariate calibration with the partial least squares (PLS) regression method was carried out on the bovine serum albumin and EV spectra. R-2 values were 0.94 for the calibration and 0.91 for the validation set. The results indicate that ATR-FTIR measurements provide a reliable method for reagent-free protein quantification of EVs.},
	keywords = {SPECTRA; infrared spectroscopy; IR spectroscopy; ATR-FTIR; Multivariate calibration; Biochemical Research Methods; Extracellular vesicle (EV); protein quantification; univariate},
	year = {2020},
	eissn = {1618-2650},
	pages = {4619-4628},
	orcid-numbers = {Wacha, András Ferenc/0000-0002-9609-0893; Varga, Zoltán/0000-0002-5741-2669}
}

@article{MTMT:30432275,
	title = {Manipulating active structure and function of cationic antimicrobial peptide CM15 by the polysulfonated drug suramin: a step closer to in vivo complexity},
	url = {https://m2.mtmt.hu/api/publication/30432275},
	author = {Quemé Peña, Mayra and Juhász, Tünde and Mihály, Judith and Szigyártó, Imola Csilla and Horváti, Kata and Bősze, Szilvia and Henczkó, Judit and Pályi, Bernadett and Németh, Csaba and Varga, Zoltán and Zsila, Ferenc and Beke-Somfai, Tamás},
	doi = {10.1002/cbic.201800801},
	journal-iso = {CHEMBIOCHEM},
	journal = {CHEMBIOCHEM},
	volume = {20},
	unique-id = {30432275},
	issn = {1439-4227},
	year = {2019},
	eissn = {1439-7633},
	pages = {1578-1590},
	orcid-numbers = {Horváti, Kata/0000-0003-4092-6011; Varga, Zoltán/0000-0002-5741-2669}
}

@article{MTMT:3369818,
	title = {Vibrational properties and bonding analysis of copper hexacyanoferrate complexes in solid state. Latest articles},
	url = {https://m2.mtmt.hu/api/publication/3369818},
	author = {Mink, János and Stirling, András and Dickson, O Ojwang and Gunnar, Svensson and Mihály, Judith and Németh, Csaba and Markus, Drees and Hajba, László},
	doi = {10.1080/05704928.2018.1459659},
	journal-iso = {APPL SPECTROSC REV},
	journal = {APPLIED SPECTROSCOPY REVIEWS},
	volume = {54},
	unique-id = {3369818},
	issn = {0570-4928},
	year = {2019},
	eissn = {1520-569X},
	pages = {369-424},
	orcid-numbers = {Hajba, László/0000-0001-7937-4854}
}

@article{MTMT:30318630,
	title = {The lipid mediator lysophosphatidic acid induces folding of disordered peptides with basic amphipathic character into rare conformations},
	url = {https://m2.mtmt.hu/api/publication/30318630},
	author = {Juhász, Tünde and Mihály, Judith and Kohut, Gergely and Németh, Csaba and Liliom, Károly and Beke-Somfai, Tamás},
	doi = {10.1038/s41598-018-32786-4},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {8},
	unique-id = {30318630},
	issn = {2045-2322},
	abstract = {Membrane-active, basic amphipathic peptides represent a class of biomolecules with diverse functions. Sequentially close protein segments also show similar behaviour in several ways. Here we investigated the effect of the lipid mediator lysophosphatidic acid (LPA) on the conformation of structurally disordered peptides including extracellular antimicrobial peptides (AMPs), and calmodulin-binding motifs derived from cytosolic and membrane target proteins. The interaction with associated LPA resulted in gain of ordered secondary structure elements, which for most cases were previously uncharacteristic of the particular peptide. Results revealed mechanism of the LPA-peptide interactions with regulation of the lipid on peptide conformation and oligomerization in a concentration-dependent manner involving (1) relocation of tryptophan residues into the lipid cluster, (2) multiple contacts between the binding partners dictated by complex driving forces, (3) multiple peptide binding to LPA associates with an affinity in the low micromolar range, and (4) selectivity for LPA compared with structurally related lipids. In line with recent findings showing endogenous molecules inducing structural changes in AMPs, we propose that accumulation of LPA in signalling or pathological processes might modulate host-defense activity or trigger certain processes by direct interaction with cationic amphipathic peptide sequences.},
	year = {2018},
	eissn = {2045-2322},
	orcid-numbers = {Kohut, Gergely/0000-0002-6139-5136; Liliom, Károly/0000-0002-7177-6872}
}