@article{MTMT:33696970,
	title = {Structures of calmodulin-melittin complexes show multiple binding modes lacking classical anchoring interactions},
	url = {https://m2.mtmt.hu/api/publication/33696970},
	author = {Dürvanger, Zsolt and Juhász, Tünde and Liliom, Károly and Harmat, Veronika},
	doi = {10.1016/j.jbc.2023.104596},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {299},
	unique-id = {33696970},
	issn = {0021-9258},
	abstract = {Calmodulin (CaM) is a Ca2+ sensor protein found in all eukaryotic cells that regulates a large number of target proteins in a Ca2+ concentration-dependent manner. As a transient type hub protein, it recognizes linear motifs of its targets, though for the Ca2+-dependent binding no consensus sequence was identified. Its complex with melittin, a major component of bee venom, is often used as a model system of protein - protein complexes. Yet, the structural aspects of the binding are not well understood, as only diverse, low-resolution data are available concerning the association. We present the crystal structure of melittin in complex with Ca2+-saturated calmodulins from two, evolutionarily distant species, Homo sapiens and Plasmodium falciparum representing three binding modes of the peptide. Results - augmented by molecular dynamics simulations - indicate that multiple binding modes can exist for CaM-melittin complexes, as an intrinsic characteristic of the binding. While the helical structure of melittin remains, swapping of its salt bridges and partial unfolding of its C-terminal segment can occur. In contrast to the classical way of target recognition by CaM, we found that different sets of residues can anchor at the hydrophobic pockets of CaM, which were considered as main recognition sites. Finally, the nanomolar binding affinity of the CaM-melittin complex is created by an ensemble of arrangements of similar stability - tight binding is achieved not by optimized specific interactions but by simultaneously satisfying less optimal interaction patterns in co-existing different conformers.},
	keywords = {crystal structure; molecular dynamics; PROTEIN COMPLEX; Protein-protein interaction; fuzzy complex; calmodulin (CaM); linear motif-binding hub protein; multiple binding modes; polymorphic protein-protein complex},
	year = {2023},
	eissn = {1083-351X},
	orcid-numbers = {Dürvanger, Zsolt/0000-0002-2652-4916; Liliom, Károly/0000-0002-7177-6872; Harmat, Veronika/0000-0002-1866-9904}
}

@article{MTMT:34133855,
	title = {SYNERGY OF PROTEASE BINDING SITES WITHIN THE ECOTIN HOMODIMER IS CRUCIAL FOR INHIBITION OF MASP ENZYMES AND FOR BLOCKING LECTIN PATHWAY ACTIVATION},
	url = {https://m2.mtmt.hu/api/publication/34133855},
	author = {Nagy, Zoltán Attila and Héja, Dávid and Bencze, Dániel and Kiss, Bence and Boros, Eszter and Szakács, Dávid and Fodor, Krisztián and Wilmanns, Matthias and Kocsis, Andrea and Dobó, József and Gál, Péter and Harmat, Veronika and Pál, Gábor},
	journal-iso = {MOL IMMUNOL},
	journal = {MOLECULAR IMMUNOLOGY},
	volume = {150},
	unique-id = {34133855},
	issn = {0161-5890},
	year = {2022},
	eissn = {1872-9142},
	pages = {190-191},
	orcid-numbers = {Nagy, Zoltán Attila/0000-0001-7687-1011; Bencze, Dániel/0000-0001-7169-9515; Kiss, Bence/0000-0001-5810-5858; Szakács, Dávid/0000-0002-8758-6387; Harmat, Veronika/0000-0002-1866-9904}
}

@article{MTMT:33307131,
	title = {A carbapenem antibiotic inhibiting a mammalian serine protease: structure of the acylaminoacyl peptidase–meropenem complex},
	url = {https://m2.mtmt.hu/api/publication/33307131},
	author = {Kiss-Szemán, Anna Júlia and Takács, Luca and Orgován, Zoltán and Stráner, Pál and Jákli, Imre and Schlosser, Gitta (Vácziné) and Masiulis, Simonas and Harmat, Veronika and Karancsiné Menyhárd, Dóra and Perczel, András},
	doi = {10.1039/D2SC05520A},
	journal-iso = {CHEM SCI},
	journal = {CHEMICAL SCIENCE},
	volume = {13},
	unique-id = {33307131},
	issn = {2041-6520},
	abstract = {The structure of porcine AAP (pAAP) in a covalently bound complex with meropenem was determined by cryo-EM to 2.1 Å resolution, showing the mammalian serine-protease inhibited by a carbapenem antibiotic.},
	year = {2022},
	eissn = {2041-6539},
	pages = {14264-14276},
	orcid-numbers = {Kiss-Szemán, Anna Júlia/0000-0002-3039-0324; Takács, Luca/0000-0002-4864-8872; Stráner, Pál/0000-0003-2240-8501; Schlosser, Gitta (Vácziné)/0000-0002-7637-7133; Harmat, Veronika/0000-0002-1866-9904; Karancsiné Menyhárd, Dóra/0000-0002-0095-5531; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:33076479,
	title = {Thermally Induced Solid-Phase Quasi-Intramolecular Redox Reactions of [Hexakis(urea-O)iron(III)] Permanganate: An Easy Reaction Route to Prepare Potential (Fe,Mn)O x Catalysts for CO2 Hydrogenation},
	url = {https://m2.mtmt.hu/api/publication/33076479},
	author = {Béres, Kende Attila and Homonnay, Zoltán and Kvitek, L and Dürvanger, Zsolt and Kubikova, M and Harmat, Veronika and Szilágyi, F and Czégény, Zsuzsanna and Németh, Péter and Nagyné Bereczki, Laura and Petruševski, VM. and Pápai, Mátyás Imre and Farkas, Attila and Kótai, László},
	doi = {10.1021/acs.inorgchem.2c02265},
	journal-iso = {INORG CHEM},
	journal = {INORGANIC CHEMISTRY},
	volume = {61},
	unique-id = {33076479},
	issn = {0020-1669},
	year = {2022},
	eissn = {1520-510X},
	pages = {14403-14418},
	orcid-numbers = {Béres, Kende Attila/0000-0003-4257-0581; Homonnay, Zoltán/0000-0001-5299-5394; Kvitek, L/0000-0003-2005-560X; Dürvanger, Zsolt/0000-0002-2652-4916; Harmat, Veronika/0000-0002-1866-9904; Németh, Péter/0000-0001-5592-5877; Pápai, Mátyás Imre/0000-0002-4819-0611; Farkas, Attila/0000-0002-8877-2587}
}

@article{MTMT:32830377,
	title = {Cryo-EM structure of acylpeptide hydrolase reveals substrate selection by multimerization and a multi-state serine-protease triad},
	url = {https://m2.mtmt.hu/api/publication/32830377},
	author = {Kiss-Szemán, Anna Júlia and Stráner, Pál and Jákli, Imre and Hosogi, Naoki and Harmat, Veronika and Karancsiné Menyhárd, Dóra and Perczel, András},
	doi = {10.1039/D2SC02276A},
	journal-iso = {CHEM SCI},
	journal = {CHEMICAL SCIENCE},
	volume = {13},
	unique-id = {32830377},
	issn = {2041-6520},
	year = {2022},
	eissn = {2041-6539},
	pages = {7132-7142},
	orcid-numbers = {Kiss-Szemán, Anna Júlia/0000-0002-3039-0324; Stráner, Pál/0000-0003-2240-8501; Hosogi, Naoki/0000-0001-6662-1940; Harmat, Veronika/0000-0002-1866-9904; Karancsiné Menyhárd, Dóra/0000-0002-0095-5531; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:32801135,
	title = {Synergy of protease binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation},
	url = {https://m2.mtmt.hu/api/publication/32801135},
	author = {Nagy, Zoltán Attila and Héja, Dávid and Bencze, Dániel and Kiss, Bence and Boros, Eszter and Szakács, Dávid and Fodor, Krisztián and Wilmanns, Matthias and Kocsis, Andrea and Dobó, József and Gál, Péter and Harmat, Veronika and Pál, Gábor},
	doi = {10.1016/j.jbc.2022.101985},
	journal-iso = {J BIOL CHEM},
	journal = {JOURNAL OF BIOLOGICAL CHEMISTRY},
	volume = {298},
	unique-id = {32801135},
	issn = {0021-9258},
	year = {2022},
	eissn = {1083-351X},
	orcid-numbers = {Nagy, Zoltán Attila/0000-0001-7687-1011; Bencze, Dániel/0000-0001-7169-9515; Kiss, Bence/0000-0001-5810-5858; Szakács, Dávid/0000-0002-8758-6387; Harmat, Veronika/0000-0002-1866-9904; Pál, Gábor/0000-0001-7868-7971}
}

@article{MTMT:32778843,
	title = {Directed Evolution-Driven Increase of Structural Plasticity Is a Prerequisite for Binding the Complement Lectin Pathway Blocking MASP-Inhibitor Peptides},
	url = {https://m2.mtmt.hu/api/publication/32778843},
	author = {Dürvanger, Zsolt and Boros, Eszter and Nagy, Zoltán Attila and Hegedüs, Rózsa and Megyeri, Márton and Dobó, József and Gál, Péter and Schlosser, Gitta (Vácziné) and Ángyán, Annamária F. and Gáspári, Zoltán and Perczel, András and Harmat, Veronika and Mező, Gábor and Karancsiné Menyhárd, Dóra and Pál, Gábor},
	doi = {10.1021/acschembio.2c00114},
	journal-iso = {ACS CHEM BIOL},
	journal = {ACS CHEMICAL BIOLOGY},
	volume = {17},
	unique-id = {32778843},
	issn = {1554-8929},
	year = {2022},
	eissn = {1554-8937},
	pages = {969-986},
	orcid-numbers = {Dürvanger, Zsolt/0000-0002-2652-4916; Nagy, Zoltán Attila/0000-0001-7687-1011; Dobó, József/0000-0001-9187-8502; Schlosser, Gitta (Vácziné)/0000-0002-7637-7133; Ángyán, Annamária F./0000-0002-2283-7341; Gáspári, Zoltán/0000-0002-8692-740X; Perczel, András/0000-0003-1252-6416; Harmat, Veronika/0000-0002-1866-9904; Mező, Gábor/0000-0002-7618-7954; Karancsiné Menyhárd, Dóra/0000-0002-0095-5531; Pál, Gábor/0000-0001-7868-7971}
}

@article{MTMT:32163599,
	title = {Dynamic disorder in the high-temperature polymorph of bis[diamminesilver(I)] sulfate-reasons and consequences of simultaneous ammonia release from two different polymorphs},
	url = {https://m2.mtmt.hu/api/publication/32163599},
	author = {Nagyné Bereczki, Laura and Alexandre Fogaca, Lara and Dürvanger, Zsolt and Harmat, Veronika and Kamarás, Katalin and Németh, Gergely and Hollo, BB and Petrusevski, VM and Bódis, Eszter and Farkas, Attila and Szilágyi, Imre Miklós and Kótai, László},
	doi = {10.1080/00958972.2021.1953489},
	journal-iso = {J COORD CHEM},
	journal = {JOURNAL OF COORDINATION CHEMISTRY},
	volume = {74},
	unique-id = {32163599},
	issn = {0095-8972},
	year = {2021},
	eissn = {1029-0389},
	pages = {2144-2162},
	orcid-numbers = {Dürvanger, Zsolt/0000-0002-2652-4916; Harmat, Veronika/0000-0002-1866-9904; Kamarás, Katalin/0000-0002-0390-3331; Farkas, Attila/0000-0002-8877-2587}
}

@article{MTMT:31612193,
	title = {Comparison of ligand binding and conformational stability of human calmodulin with its homolog from the malaria parasite Plasmodium falciparum},
	url = {https://m2.mtmt.hu/api/publication/31612193},
	author = {Juhász, Tünde and Kardos, József and Dürvanger, Zsolt and Harmat, Veronika and Liliom, Károly},
	doi = {10.1096/fba.2020-00013},
	journal-iso = {FASEB BioAdv},
	journal = {FASEB BIOADVANCES},
	volume = {2},
	unique-id = {31612193},
	year = {2020},
	eissn = {2573-9832},
	pages = {489-505},
	orcid-numbers = {Kardos, József/0000-0002-2135-2932; Dürvanger, Zsolt/0000-0002-2652-4916; Harmat, Veronika/0000-0002-1866-9904; Liliom, Károly/0000-0002-7177-6872}
}

@article{MTMT:31409208,
	title = {Configuration-Controlled Crystal and/or Gel Formation of Protectedd-Glucosamines Supported by Promiscuous Interaction Surfaces and a Conformationally Heterogeneous Solution State},
	url = {https://m2.mtmt.hu/api/publication/31409208},
	author = {Kapros, Anita and Balázs, Attila and Harmat, Veronika and Halo, Adrienn and Budai, Lívia and Pintér, István and Karancsiné Menyhárd, Dóra and Perczel, András},
	doi = {10.1002/chem.202000882},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {26},
	unique-id = {31409208},
	issn = {0947-6539},
	abstract = {The configuration-dependent self-association mode of the two anomers ofO-Ac,N-Fmoc-d-glucosamine, a foldamer building block, leading to gel and/or single crystal formation is described. The beta-anomer of the sugar amino acid (2) forms a gel from various solvents (confirmed by SEM, rheology measurements, NMR, and ECD spectroscopy), whereas the alpha-anomer (1) does not form a gel with any solvent tested. Transition from the solution state to a gel is coupled to a concurrent shift of the Fmoc-groups: from a freely rotating (almost symmetrical) to a specific, asymmetric orientation. Whereas the crystal structure of the alpha-anomer is built as an evenly packed 3D system, the beta-anomer forms a looser superstructure of well-packed 2D layers. Modeling indicates that in the lowest energy, but scarcely sampled conformer of the beta-anomer, the Fmoc-group bends above the sugar moiety, stabilized by intramolecular CH <->pi interactions between the aromatic rings. It is concluded that possessing an extended and promiscuous interaction surface and a conformationally heterogeneous solution state are among the basic requirements of gel formation for a candidate molecule.},
	keywords = {RESOLUTION; RECOGNITION; WATER; GLUCOSE; Crystallography; NMR spectroscopy; DRUG-DELIVERY; Hydrogels; Gelation; CH-pi interactions; gel state; CH/PI INTERACTIONS; PI-INTERACTIONS},
	year = {2020},
	eissn = {1521-3765},
	pages = {11643-11655},
	orcid-numbers = {Harmat, Veronika/0000-0002-1866-9904; Budai, Lívia/0000-0002-6720-5989; Karancsiné Menyhárd, Dóra/0000-0002-0095-5531; Perczel, András/0000-0003-1252-6416}
}