@article{MTMT:32111416,
	title = {Chiral HPLC separation of enantiomeric blebbistatin derivatives and racemization analysis in vertebrate tissues.},
	url = {https://m2.mtmt.hu/api/publication/32111416},
	author = {Suthar, Sharad Kumar and Rauscher, Anna Ágnes and Winternitz, Máté and Gyimesi, Máté and Málnási Csizmadia, András},
	doi = {10.1016/j.jpba.2021.114246},
	journal-iso = {J PHARMACEUT BIOMED ANAL},
	journal = {JOURNAL OF PHARMACEUTICAL AND BIOMEDICAL ANALYSIS},
	volume = {204},
	unique-id = {32111416},
	issn = {0731-7085},
	abstract = {Simple and consistent chiral HPLC methods for the efficient separation of enantiomeric blebbistatin derivatives, namely parent compound blebbistatin and derivatives 4-nitroblebbistatin, 4-aminoblebbistatin, 4-dimethylaminoblebbistatin, and 4-t-butylblebbistatin were developed using cellulose tris(3,5-dimethylphenylcarbamate) as a stationary phase (Lux cellulose-1 column). Blebbistatin, 4-aminoblebbistatin, and 4-dimethylaminoblebbistatin racemates were well-separated in normal-phase HPLC conditions while 4-nitroblebbistatin and 4-t-butylblebbistatin were effectively separated in both normal- and reversed-phase HPLC conditions. Furthermore, the order of elution of enantiopure compounds was found to be independent of mobile phase compositions and conditions used, and solely depends on the interaction between the enantiomer and the chiral stationary phase. We found that despite the chiral center being present far from the D-ring in the blebbistatin structure, the D-ring substitutions prominently affect the chiral separation. Ex vivo racemization studies of the most popular blebbistatin derivative (S)-(-)-4-aminoblebbistatin in rat blood and brain tissues revealed that the compound does not convert into the inactive enantiomer. This confirms that (S)-(-)-4-aminoblebbistatin is a useful tool compound in cellular and molecular biology studies without the risks of racemization and degradation effects.},
	keywords = {ENANTIOMERS; racemic mixture; blebbistatin; CHIRAL HPLC; biological matrices; Cellulose tris(3,5-dimethylphenylcarbamate)},
	year = {2021},
	eissn = {1873-264X},
	orcid-numbers = {Rauscher, Anna Ágnes/0000-0002-4062-960X; Gyimesi, Máté/0000-0002-7195-1925; Málnási Csizmadia, András/0000-0002-2430-8398}
}

@article{MTMT:31599696,
	title = {Insight into the hidden bacterial diversity of Lake Balaton, Hungary},
	url = {https://m2.mtmt.hu/api/publication/31599696},
	author = {M Tóth, Erika and Toumi, Marwene and Farkas, Rózsa and Takáts, Kornél and Somodi, Csenge and Ács, Éva},
	doi = {10.1007/s42977-020-00040-6},
	journal-iso = {BIOL FUTURA},
	journal = {BIOLOGIA FUTURA},
	volume = {71},
	unique-id = {31599696},
	issn = {2676-8615},
	abstract = {In the present study, the prokaryotic community structure of the water of Lake Balaton was investigated at the littoral region of three different points (Tihany, Balatonmariafurdo and Keszthely) by cultivation independent methods [next-generation sequencing (NGS), specific PCRs and microscopy cell counting] to check the hidden microbial diversity of the lake. The taxon-specific PCRs did not show pathogenic bacteria but at Keszthely and Mariafurdo sites extended spectrum beta-lactamase-producing microorganisms could be detected. The bacterial as well as archaeal diversity of the water was high even when many taxa are still uncultivable. Based on NGS, the bacterial communities were dominated by Proteobacteria, Bacteroidetes and Actinobacteria, while the most frequent Archaea belonged to Woesearchaeia (Nanoarchaeota). The ratio of the detected taxa differed among the samples. Three different types of phototrophic groups appeared: Cyanobacteria (oxygenic phototrophic organisms), Chloroflexi (anaerobic, organotrophic bacteria) and the aerobic, anoxic photoheterotrophic group (AAPs). Members of Firmicutes appeared only with low abundance, and Enterobacteriales (order within Proteobacteria) were present also only in low numbers in all samples.},
	keywords = {ARCHAEA; Lake Balaton; *Bacteria; next-generation sequencing (NGS); Bacterial diversity},
	year = {2020},
	eissn = {2676-8607},
	pages = {383-391},
	orcid-numbers = {M Tóth, Erika/0000-0001-9048-5758; Ács, Éva/0000-0003-1774-157X}
}

@article{MTMT:31179505,
	title = {Direct myosin-2 inhibition enhances cerebral perfusion resulting in functional improvement after ischemic stroke},
	url = {https://m2.mtmt.hu/api/publication/31179505},
	author = {Pénzes, Máté and Túrós, Demeter and Máthé, Domokos and Szigeti, Krisztián and Hegedűs, Nikolett and Rauscher, Anna Ágnes and Tóth, Péter József and Ivic, Ivan and Padmanabhan, Parasuraman and Pál, Gabriella and Dobolyi, Árpád and Gyimesi, Máté and Málnási Csizmadia, András},
	doi = {10.7150/thno.42077},
	journal-iso = {THERANOSTICS},
	journal = {THERANOSTICS},
	volume = {10},
	unique-id = {31179505},
	issn = {1838-7640},
	year = {2020},
	eissn = {1838-7640},
	pages = {5341-5356},
	orcid-numbers = {Hegedűs, Nikolett/0000-0003-1122-1872; Rauscher, Anna Ágnes/0000-0002-4062-960X; Dobolyi, Árpád/0000-0003-0397-2991; Gyimesi, Máté/0000-0002-7195-1925; Málnási Csizmadia, András/0000-0002-2430-8398}
}

@article{MTMT:3397475,
	title = {Non-blocking modulation contributes to sodium channel inhibition by a covalently attached photoreactive riluzole analog},
	url = {https://m2.mtmt.hu/api/publication/3397475},
	author = {Lukács, Péter and Földi, Mátyás Csaba and Valanszki, L and Casanova, E and Biri-Kovács, Beáta and Nyitray, László and Málnási Csizmadia, András and Mike, Árpád},
	doi = {10.1038/s41598-018-26444-y},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {8},
	unique-id = {3397475},
	issn = {2045-2322},
	abstract = {Sodium channel inhibitor drugs decrease pathological hyperactivity in various diseases including pain syndromes, myotonia, arrhythmias, nerve injuries and epilepsies. Inhibiting pathological but not physiological activity, however, is a major challenge in drug development. Sodium channel inhibitors exert their effects by a dual action: they obstruct ion flow ("block"), and they alter the energetics of channel opening and closing ("modulation"). Ideal drugs would be modulators without blocking effect, because modulation is inherently activity-dependent, therefore selective for pathological hyperactivity. Can block and modulation be separated? It has been difficult to tell, because the effect of modulation is obscured by conformation-dependent association/dissociation of the drug. To eliminate dynamic association/dissociation, we used a photoreactive riluzole analog which could be covalently bound to the channel; and found, unexpectedly, that drug-bound channels could still conduct ions, although with modulated gating. The finding that non-blocking modulation is possible, may open a novel avenue for drug development because non-blocking modulators could be more specific in treating hyperactivity-linked diseases.},
	keywords = {NEURONS; MECHANISMS; RECEPTORS; RECOMBINATION; CONFORMATIONS; Electrophysiology; lidocaine; DRUG DISCOVERY; LOCAL-ANESTHETICS; DEPENDENT BLOCK},
	year = {2018},
	eissn = {2045-2322},
	orcid-numbers = {Biri-Kovács, Beáta/0000-0001-5803-9969; Nyitray, László/0000-0003-4717-5994; Málnási Csizmadia, András/0000-0002-2430-8398; Mike, Árpád/0000-0002-9095-8161}
}

@article{MTMT:3247385,
	title = {Highly Soluble, Non-Phototoxic, Non-Fluorescent, Photostable Blebbistatin Derivatives},
	url = {https://m2.mtmt.hu/api/publication/3247385},
	author = {Rauscher, Anna A and Kumar, Sharad and Várkuti, Boglárka and Képiró, Miklós and Horvath, Adam I and Végner, László and Hegyi, György and Borhegyi, Zsolt and Varga, Máté and Lenkei, Zsolt and Málnási Csizmadia, András},
	journal-iso = {BIOPHYS J},
	journal = {BIOPHYSICAL JOURNAL},
	volume = {112},
	unique-id = {3247385},
	issn = {0006-3495},
	year = {2017},
	eissn = {1542-0086},
	pages = {266A-267A},
	orcid-numbers = {Borhegyi, Zsolt/0000-0001-5556-8742; Varga, Máté/0000-0003-4289-1705; Málnási Csizmadia, András/0000-0002-2430-8398}
}

@article{MTMT:3203729,
	title = {Interaction of mycotoxin zearalenone with human serum albumin},
	url = {https://m2.mtmt.hu/api/publication/3203729},
	author = {Poór, Miklós and Kunsági-Máté, Sándor and Bálint, Mónika Enikő and Hetényi, Csaba and Gerner, Zsófia and Lemli, Beáta},
	doi = {10.1016/j.jphotobiol.2017.03.016},
	journal-iso = {J PHOTOCH PHOTOBIO B},
	journal = {JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY},
	volume = {170},
	unique-id = {3203729},
	issn = {1011-1344},
	year = {2017},
	eissn = {1873-2682},
	pages = {16-24},
	orcid-numbers = {Lemli, Beáta/0000-0001-8903-1337}
}

@article{MTMT:3097533,
	title = {Comparative investigation of the in vitro inhibitory potencies of 13-epimeric estrones and D-secoestrones towards 17β-hydroxysteroid dehydrogenase type 1},
	url = {https://m2.mtmt.hu/api/publication/3097533},
	author = {Herman, Bianka Edina and Szabó, Johanna and Bacsa, Ildikó and Wölfling, János and Schneider, Gyula and Bálint, Mónika Enikő and Hetényi, Csaba and Mernyák, Erzsébet and Szécsi, Mihály},
	doi = {10.1080/14756366.2016.1204610},
	journal-iso = {J ENZYM INHIB MED CH},
	journal = {JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY},
	volume = {31},
	unique-id = {3097533},
	issn = {1475-6366},
	abstract = {The inhibitory effects of 13-epimeric estrones, D-secooxime and D-secoalcohol estrone compounds on human placental 17β-hydroxysteroid dehydrogenase type 1 isozyme (17β-HSD1) were investigated. The transformation of estrone to 17β-estradiol was studied by an in vitro radiosubstrate incubation method. 13α-Estrone inhibited the enzyme activity effectively with an IC50 value of 1.2 μM, which indicates that enzyme affinity is similar to that of the natural estrone substrate. The 13β derivatives and the compounds bearing a 3-hydroxy group generally exerted stronger inhibition than the 13α and 3-ether counterparts. The 3-hydroxy-13β-D-secoalcohol and the 3-hydroxy-13α-D-secooxime displayed an outstanding cofactor dependence, i.e. more efficient inhibition in the presence of NADH than NADPH. The 3-hydroxy-13β-D-secooxime has an IC50 value of 0.070 μM and is one of the most effective 17β-HSD1 inhibitors reported to date in the literature. © 2016 Informa UK Limited, trading as Taylor & Francis Group.},
	keywords = {NADPH; NADH; 13α-estrone; D-secoestrone; 17β-HSD1 inhibition},
	year = {2016},
	eissn = {1475-6374},
	pages = {61-69},
	orcid-numbers = {Bacsa, Ildikó/0000-0001-8277-631X; Wölfling, János/0000-0002-3037-309X; Mernyák, Erzsébet/0000-0003-4494-1817; Szécsi, Mihály/0000-0002-4272-1362}
}

@article{MTMT:3074596,
	title = {A highly soluble, non-phototoxic, non-fluorescent blebbistatin derivative.},
	url = {https://m2.mtmt.hu/api/publication/3074596},
	author = {Várkuti, Boglárka and Képiró, Miklós and Horváth, Ádám István and Végner, László and Ráti, S and Zsigmond, Áron and Hegyi, György and Lenkei, Z and Varga, Máté and Málnási Csizmadia, András},
	doi = {10.1038/srep26141},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {6},
	unique-id = {3074596},
	issn = {2045-2322},
	year = {2016},
	eissn = {2045-2322},
	orcid-numbers = {Horváth, Ádám István/0000-0003-0977-4734; Varga, Máté/0000-0003-4289-1705; Málnási Csizmadia, András/0000-0002-2430-8398}
}

@article{MTMT:2998137,
	title = {Exploration of Interfacial Hydration Networks of Target-Ligand Complexes.},
	url = {https://m2.mtmt.hu/api/publication/2998137},
	author = {Jeszenői, Norbert and Bálint, Mónika Enikő and Horváth, István and van der Spoel, D and Hetényi, Csaba},
	doi = {10.1021/acs.jcim.5b00638},
	journal-iso = {J CHEM INF MODEL},
	journal = {JOURNAL OF CHEMICAL INFORMATION AND MODELING},
	volume = {56},
	unique-id = {2998137},
	issn = {1549-9596},
	abstract = {Interfacial hydration strongly influences interactions between biomolecules. For example, drug-target complexes are often stabilized by hydration networks formed between hydrophilic residues and water molecules at the interface. Exhaustive exploration of hydration networks is challenging for experimental as well as theoretical methods due to high mobility of participating water molecules. In the present study, we introduced a tool for determination of the complete, void-free hydration structures of molecular interfaces. The tool was applied to 31 complexes including histone proteins, a HIV-1 protease, a G-protein-signaling modulator, and peptide ligands of various lengths. The complexes contained 344 experimentally determined water positions used for validation, and excellent agreement with these was obtained. High-level cooperation between interfacial water molecules was detected by a new approach based on the decomposition of hydration networks into static and dynamic network regions (subnets). Besides providing hydration structures at the atomic level, our results uncovered hitherto hidden networking fundaments of integrity and stability of complex biomolecular interfaces filling an important gap in the toolkit of drug design and structural biochemistry. The presence of continuous, static regions of the interfacial hydration network was found necessary also for stable complexes of histone proteins participating in chromatin assembly and epigenetic regulation.},
	year = {2016},
	eissn = {1549-960X},
	pages = {148-158},
	orcid-numbers = {Jeszenői, Norbert/0000-0002-6472-5807}
}

@article{MTMT:2923894,
	title = {The role of structural flexibility and stability in the interaction of serine proteases with their inhibitors},
	url = {https://m2.mtmt.hu/api/publication/2923894},
	author = {Gráf, László and Molnár, Tamás and Kardos, József and Gáspári, Zoltán and Katona, Gergely},
	doi = {10.2174/1389203716666150429123733},
	journal-iso = {CURR PROTEIN PEPT SCI},
	journal = {CURRENT PROTEIN AND PEPTIDE SCIENCE},
	volume = {16},
	unique-id = {2923894},
	issn = {1389-2037},
	abstract = {Serine proteases and their natural inhibitors have long been served as excellent models for studying (primary, secondary and tertiary) structure - activity relationships of biologically interacting proteins. As protein flexibility has been accepted as a “fourth dimension” of the protein structure, its contribution to the binding process has gained much interest. In this article we review extreme cases of serine protease interactions with canonical serine protease inhibitors that provide unique insights into the dynamics of protein- protein interactions. The major conclusions of our review article are: a) taxon-specific inhibitory effects of two highly homologous protease inhibitors from Schistocerca gregaria (SGCI and SGTI), as investigated by H/D exchange experiments and NMR spectroscopy, are due to their differential flexibilities, b) stabilities of some protease and inhibitor complexes, the wide-spread and increased flexibility of some segments in the protein-protein complexes, as studied by X-ray crystallography and NMR-spectroscopy, appear to be proportional to the physical stability of the complex. © 2015 Bentham Science Publishers.},
	keywords = {SERINE PROTEASES; SERPINS; STABILITY; FLEXIBILITY; protein–protein interactions; Canonical inhibitors},
	year = {2015},
	eissn = {1875-5550},
	pages = {521-531},
	orcid-numbers = {Molnár, Tamás/0000-0002-6842-2715; Kardos, József/0000-0002-2135-2932; Katona, Gergely/0000-0002-4173-0355}
}