@article{MTMT:34127552,
	title = {Interaction of biomolecules with anatase, rutile and amorphous TiO2 surfaces: A molecular dynamics study},
	url = {https://m2.mtmt.hu/api/publication/34127552},
	author = {Tarjányi, Tamás and Bogár, Ferenc and Minárovits, János and Gajdács, Márió and Tóth, Zsolt},
	doi = {10.1371/journal.pone.0289467},
	journal-iso = {PLOS ONE},
	journal = {PLOS ONE},
	volume = {18},
	unique-id = {34127552},
	issn = {1932-6203},
	abstract = {The adhesion of biomolecules to dental and orthopedic implants is a fundamental step in the process of osseointegration. Short peptide motifs, such as RGD or KRSR, carried by extracellular matrix proteins or coated onto implant surfaces, accelerate cell adhesion and tissue formation. For this reason, understanding the binding mechanisms of adhesive peptides to oxidized surfaces of titanium implants is of paramount importance. We performed molecular dynamics simulations to compare the adhesion properties of 6 peptides, including the tripeptide RGD, its variants KGD and LGD, as well as the tetrapeptide KRSR, its variant LRSR and its truncated version RSR, on anatase, rutile, and amorphous titanium dioxide (TiO 2 ) surfaces. The migration of these molecules from the water phase to the surface was simulated in an aqueous environment. Based on these simulations, we calculated the residence time of each peptide bound to the three different TiO 2 structures. It was found that the presence of an N-terminal lysine or arginine amino acid residue resulted in more efficient surface binding. A pulling simulation was performed to detach the adhered molecules. The maximum pulling force and the binding energy were determined from the results of these simulations. The tri- and tetrapeptides had slightly greater adhesion affinity to the amorphous and anatase structure than to rutile in general, however specific surface and peptide binding characters could be detected. The binding energies obtained from our simulations allowed us to rank the adhesion strengths of the studied peptides.},
	year = {2023},
	eissn = {1932-6203},
	orcid-numbers = {Tarjányi, Tamás/0000-0002-9481-5977; Bogár, Ferenc/0000-0002-0611-1452; Gajdács, Márió/0000-0003-1270-0365}
}

@article{MTMT:34030642,
	title = {Alzheimer-kór: le tudjuk-e lassítani a betegséget, lesz-e oki terápia?},
	url = {https://m2.mtmt.hu/api/publication/34030642},
	author = {Penke, Botond and Szűcs, Mária and Bogár, Ferenc},
	journal-iso = {BIOKÉMIA},
	journal = {BIOKÉMIA: A MAGYAR BIOKÉMIAI EGYESÜLET FOLYÓIRATA},
	volume = {47},
	unique-id = {34030642},
	issn = {0133-8455},
	year = {2023},
	eissn = {2060-8152},
	pages = {10-29},
	orcid-numbers = {Penke, Botond/0000-0003-0938-0567; Bogár, Ferenc/0000-0002-0611-1452}
}

@article{MTMT:33712712,
	title = {Structural Adaptation of the Single-Stranded DNA-Binding Protein C-Terminal to DNA Metabolizing Partners Guides Inhibitor Design},
	url = {https://m2.mtmt.hu/api/publication/33712712},
	author = {Tököli, Attila and Bodnár, Brigitta and Bogár, Ferenc and Paragi, Gábor and Hetényi, Anasztázia and Bartus, Éva and Wéber, Edit and Hegedüs, Zsófia and Szabó, Zoltán and Kecskeméti, Gábor and Szakonyi, Gerda and Martinek, Tamás},
	doi = {10.3390/pharmaceutics15041032},
	journal-iso = {PHARMACEUTICS},
	journal = {PHARMACEUTICS},
	volume = {15},
	unique-id = {33712712},
	issn = {1999-4923},
	abstract = {Single-stranded DNA-binding protein (SSB) is a bacterial interaction hub and an appealing target for antimicrobial therapy. Understanding the structural adaptation of the disordered SSB C-terminus (SSB-Ct) to DNA metabolizing enzymes (e.g., ExoI and RecO) is essential for designing high-affinity SSB mimetic inhibitors. Molecular dynamics simulations revealed the transient interactions of SSB-Ct with two hot spots on ExoI and RecO. The residual flexibility of the peptide–protein complexes allows adaptive molecular recognition. Scanning with non-canonical amino acids revealed that modifications at both termini of SSB-Ct could increase the affinity, supporting the two-hot-spot binding model. Combining unnatural amino acid substitutions on both segments of the peptide resulted in enthalpy-enhanced affinity, accompanied by enthalpy–entropy compensation, as determined by isothermal calorimetry. NMR data and molecular modeling confirmed the reduced flexibility of the improved affinity complexes. Our results highlight that the SSB-Ct mimetics bind to the DNA metabolizing targets through the hot spots, interacting with both of segments of the ligands.},
	year = {2023},
	eissn = {1999-4923},
	orcid-numbers = {Tököli, Attila/0000-0001-8413-3182; Bogár, Ferenc/0000-0002-0611-1452; Paragi, Gábor/0000-0001-5408-1748; Hetényi, Anasztázia/0000-0001-8080-6992; Bartus, Éva/0000-0001-9976-6978; Wéber, Edit/0000-0002-5904-0619; Hegedüs, Zsófia/0000-0002-5546-8167; Szabó, Zoltán/0000-0001-8278-8038; Kecskeméti, Gábor/0000-0002-5584-6869; Szakonyi, Gerda/0000-0002-4366-4283; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:33702944,
	title = {New Pathways Identify Novel Drug Targets for the Prevention and Treatment of Alzheimer’s Disease},
	url = {https://m2.mtmt.hu/api/publication/33702944},
	author = {Penke, Botond and Szűcs, Mária and Bogár, Ferenc},
	doi = {10.3390/ijms24065383},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {33702944},
	issn = {1661-6596},
	abstract = {Alzheimer’s disease (AD) is an incurable, progressive neurodegenerative disorder. AD is a complex and multifactorial disease that is responsible for 60–80% of dementia cases. Aging, genetic factors, and epigenetic changes are the main risk factors for AD. Two aggregation-prone proteins play a decisive role in AD pathogenesis: β-amyloid (Aβ) and hyperphosphorylated tau (pTau). Both of them form deposits and diffusible toxic aggregates in the brain. These proteins are the biomarkers of AD. Different hypotheses have tried to explain AD pathogenesis and served as platforms for AD drug research. Experiments demonstrated that both Aβ and pTau might start neurodegenerative processes and are necessary for cognitive decline. The two pathologies act in synergy. Inhibition of the formation of toxic Aβ and pTau aggregates has been an old drug target. Recently, successful Aβ clearance by monoclonal antibodies has raised new hopes for AD treatments if the disease is detected at early stages. More recently, novel targets, e.g., improvements in amyloid clearance from the brain, application of small heat shock proteins (Hsps), modulation of chronic neuroinflammation by different receptor ligands, modulation of microglial phagocytosis, and increase in myelination have been revealed in AD research.},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Penke, Botond/0000-0003-0938-0567; Bogár, Ferenc/0000-0002-0611-1452}
}

@article{MTMT:33265905,
	title = {Effects of sub-chronic, in vivo administration of sigma-1 receptor ligands on platelet and aortic arachidonate cascade in streptozotocin-induced diabetic rats},
	url = {https://m2.mtmt.hu/api/publication/33265905},
	author = {Váczi, Sándor and Barna, Lilla and Laczi, Krisztián and Tömösi, Ferenc and Rákhely, Gábor and Penke, Botond and Fülöp, Lívia and Bogár, Ferenc and Janáky, Tamás and Deli, Mária Anna and Mezei, Zsófia},
	doi = {10.1371/journal.pone.0265854},
	journal-iso = {PLOS ONE},
	journal = {PLOS ONE},
	volume = {17},
	unique-id = {33265905},
	issn = {1932-6203},
	year = {2022},
	eissn = {1932-6203},
	orcid-numbers = {Váczi, Sándor/0000-0002-9642-7126; Laczi, Krisztián/0000-0002-9399-7406; Tömösi, Ferenc/0000-0002-6657-5777; Rákhely, Gábor/0000-0003-2557-3641; Penke, Botond/0000-0003-0938-0567; Fülöp, Lívia/0000-0002-8010-0129; Bogár, Ferenc/0000-0002-0611-1452; Janáky, Tamás/0000-0002-6466-8283; Deli, Mária Anna/0000-0001-6084-6524}
}

@CONFERENCE{MTMT:33118459,
	title = {Osszeointegráció molekuláris megközelítésben: kristályos és amorf titán-oxid felületekkel kölcsönható biomolekulák},
	url = {https://m2.mtmt.hu/api/publication/33118459},
	author = {Tarjányi, Tamás and Bogár, Ferenc and Gajdács, Márió and Minárovits, János and Tóth, Zsolt},
	booktitle = {Szegedi Fogorvosnapok 2022. Szegedi Fogorvos Találkozó és Tudományos Konferencia, Magyar Gyermekfogászati és Fogszabályozási Társaság IX. Tóth Pál Vándorgyűlés},
	unique-id = {33118459},
	year = {2022},
	pages = {25-25},
	orcid-numbers = {Tarjányi, Tamás/0000-0002-9481-5977; Bogár, Ferenc/0000-0002-0611-1452; Gajdács, Márió/0000-0003-1270-0365}
}

@article{MTMT:32803926,
	title = {sVmKTx, a transcriptome analysis-based synthetic peptide analogue of Vm24, inhibits Kv1.3 channels of human T cells with improved selectivity},
	url = {https://m2.mtmt.hu/api/publication/32803926},
	author = {Csóti, Ágota and del Carmen Nájera Meza, Rosby and Bogár, Ferenc and Tajti, Gábor and Szántó, Gábor Tibor and Varga, Zoltán and Gurrola, Georgina B. and Tóth, Gábor and Possani, Lourival D. and Panyi, György},
	doi = {10.1016/j.bcp.2022.115023},
	journal-iso = {BIOCHEMIC PHARMACOL},
	journal = {BIOCHEMICAL PHARMACOLOGY},
	volume = {199},
	unique-id = {32803926},
	issn = {0006-2952},
	year = {2022},
	eissn = {1873-2968},
	orcid-numbers = {Bogár, Ferenc/0000-0002-0611-1452; Tóth, Gábor/0000-0002-3604-4385; Panyi, György/0000-0001-6227-3301}
}

@article{MTMT:32801748,
	title = {Effects of sub-chronic, in vivo administration of sigma non-opioid intracellular receptor 1 ligands on platelet and aortic arachidonate cascade in rats},
	url = {https://m2.mtmt.hu/api/publication/32801748},
	author = {Váczi, Sándor and Barna, Lilla and Laczi, Krisztián and Tömösi, Ferenc and Rákhely, Gábor and Penke, Botond and Fülöp, Lívia and Bogár, Ferenc and Janáky, Tamás and Deli, Mária Anna and Mezei, Zsófia},
	doi = {10.1016/j.ejphar.2022.174983},
	journal-iso = {EUR J PHARMACOL},
	journal = {EUROPEAN JOURNAL OF PHARMACOLOGY},
	volume = {925},
	unique-id = {32801748},
	issn = {0014-2999},
	year = {2022},
	eissn = {1879-0712},
	orcid-numbers = {Váczi, Sándor/0000-0002-9642-7126; Laczi, Krisztián/0000-0002-9399-7406; Tömösi, Ferenc/0000-0002-6657-5777; Rákhely, Gábor/0000-0003-2557-3641; Penke, Botond/0000-0003-0938-0567; Fülöp, Lívia/0000-0002-8010-0129; Bogár, Ferenc/0000-0002-0611-1452; Janáky, Tamás/0000-0002-6466-8283; Deli, Mária Anna/0000-0001-6084-6524}
}

@article{MTMT:32753552,
	title = {Novel Therapeutic Target for Prevention of Neurodegenerative Diseases: Modulation of Neuroinflammation with Sig-1R Ligands},
	url = {https://m2.mtmt.hu/api/publication/32753552},
	author = {Bogár, Ferenc and Fülöp, Lívia and Penke, Botond},
	doi = {10.3390/biom12030363},
	journal-iso = {BIOMOLECULES},
	journal = {BIOMOLECULES},
	volume = {12},
	unique-id = {32753552},
	issn = {2218-273X},
	year = {2022},
	eissn = {2218-273X},
	orcid-numbers = {Bogár, Ferenc/0000-0002-0611-1452; Fülöp, Lívia/0000-0002-8010-0129; Penke, Botond/0000-0003-0938-0567}
}

@article{MTMT:32529630,
	title = {Interaction of KRSR Peptide with Titanium Dioxide Anatase (100) Surface: A Molecular Dynamics Simulation Study},
	url = {https://m2.mtmt.hu/api/publication/32529630},
	author = {Tarjányi, Tamás and Bogár, Ferenc and Minárovits, János and Gajdács, Márió and Tóth, Zsolt},
	doi = {10.3390/ijms222413251},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {22},
	unique-id = {32529630},
	issn = {1661-6596},
	year = {2021},
	eissn = {1422-0067},
	orcid-numbers = {Tarjányi, Tamás/0000-0002-9481-5977; Bogár, Ferenc/0000-0002-0611-1452; Gajdács, Márió/0000-0003-1270-0365}
}