@article{MTMT:34677129,
	title = {Role of CFTR in diabetes‐induced pancreatic ductal fluid and HCO 3 − secretion},
	url = {https://m2.mtmt.hu/api/publication/34677129},
	author = {Ébert, Attila and Gál, Eleonóra and Tóth, Emese and Szögi, Titanilla and Hegyi, Péter and Venglovecz, Viktória},
	doi = {10.1113/JP285702},
	journal-iso = {J PHYSIOL-LONDON},
	journal = {JOURNAL OF PHYSIOLOGY-LONDON},
	volume = {602},
	unique-id = {34677129},
	issn = {0022-3751},
	year = {2024},
	eissn = {1469-7793},
	pages = {1065-1083},
	orcid-numbers = {Szögi, Titanilla/0000-0002-9854-7340; Hegyi, Péter/0000-0003-0399-7259; Venglovecz, Viktória/0000-0002-2316-7247}
}

@CONFERENCE{MTMT:33570390,
	title = {Post-diaminoenzidine treatments for double stainings : extension of sulfide-silver-gold internsification for light and fluorescent microscopy},
	url = {https://m2.mtmt.hu/api/publication/33570390},
	author = {Apróné Török, Ibolya and Seprényi, György and Pór, Erzsébet and Emőke, Borbély and Szögi, Titanilla and Dobó, Endre},
	booktitle = {Magyar Anatómus Társaság 2022. évi konferenciája},
	unique-id = {33570390},
	year = {2022},
	pages = {60-61},
	orcid-numbers = {Apróné Török, Ibolya/0000-0002-2441-8925; Szögi, Titanilla/0000-0002-9854-7340}
}

@article{MTMT:33111245,
	title = {Examination of Longitudinal Alterations in Alzheimer’s Disease-Related Neurogenesis in an APP/PS1 Transgenic Mouse Model, and the Effects of P33, a Putative Neuroprotective Agent Thereon},
	url = {https://m2.mtmt.hu/api/publication/33111245},
	author = {Szögi, Titanilla and Borbély, Emőke and Schuster, Ildikó and Bozsó, Zsolt and Sántha, Miklós and Tóth, Erzsébet Melinda and Penke, Botond and Fülöp, Lívia},
	doi = {10.3390/ijms231810364},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {23},
	unique-id = {33111245},
	issn = {1661-6596},
	abstract = {Neurogenesis plays a crucial role in cognitive processes. During aging and in Alzheimer’s disease (AD), altered neurogenesis and neuroinflammation are evident both in C57BL/6J, APPSwe/PS1dE9 (Tg) mice and humans. AD pathology may slow down upon drug treatment, for example, in a previous study of our group P33, a putative neuroprotective agent was found to exert advantageous effects on the elevated levels of APP, Aβ, and neuroinflammation. In the present study, we aimed to examine longitudinal alterations in neurogenesis, neuroinflammation and AD pathology in a transgenic (Tg) mouse model, and assessed the putative beneficial effects of long-term P33 treatment on AD-specific neurological alterations. Hippocampal cell proliferation and differentiation were significantly reduced between 8 and 12 months of age. Regarding neuroinflammation, significantly elevated astrogliosis and microglial activation were observed in 6- to 7-month-old Tg animals. The amounts of the molecules involved in the amyloidogenic pathway were altered from 4 months of age in Tg animals. P33-treatment led to significantly increased neurogenesis in 9-month-old animals. Our data support the hypothesis that altered neurogenesis may be a consequence of AD pathology. Based on our findings in the transgenic animal model, early pharmacological treatment before the manifestation of AD symptoms might ameliorate neurological decline.},
	year = {2022},
	eissn = {1422-0067},
	orcid-numbers = {Szögi, Titanilla/0000-0002-9854-7340; Schuster, Ildikó/0000-0001-9997-5729; Bozsó, Zsolt/0000-0002-5713-3096; Penke, Botond/0000-0003-0938-0567; Fülöp, Lívia/0000-0002-8010-0129}
}

@article{MTMT:32753550,
	title = {Impact of Two Neuronal Sigma-1 Receptor Modulators, PRE084 and DMT, on Neurogenesis and Neuroinflammation in an Aβ1–42-Injected, Wild-Type Mouse Model of AD},
	url = {https://m2.mtmt.hu/api/publication/32753550},
	author = {Borbély, Emőke and Varga, Viktória and Szögi, Titanilla and Schuster, Ildikó and Bozsó, Zsolt and Penke, Botond and Fülöp, Lívia},
	doi = {10.3390/ijms23052514},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {23},
	unique-id = {32753550},
	issn = {1661-6596},
	year = {2022},
	eissn = {1422-0067},
	orcid-numbers = {Szögi, Titanilla/0000-0002-9854-7340; Schuster, Ildikó/0000-0001-9997-5729; Bozsó, Zsolt/0000-0002-5713-3096; Penke, Botond/0000-0003-0938-0567; Fülöp, Lívia/0000-0002-8010-0129}
}

@article{MTMT:31807147,
	title = {Neuroinflammatory processes are augmented in mice overexpressing human heat-shock protein B1 following ethanol-induced brain injury},
	url = {https://m2.mtmt.hu/api/publication/31807147},
	author = {Dukay, Brigitta and Walter, Fruzsina and Vigh, Judit Piroska and Barabási, Beáta and Hajdu, Petra and Balassa, Tamás and Migh, Ede and Kincses, András and Hoyk, Zsófia and Szögi, Titanilla and Borbély, Emőke and Csoboz, Bálint and Horváth, Péter and Fülöp, Lívia and Penke, Botond and Vigh, László and Deli, Mária Anna and Sántha, Miklós and Tóth, Erzsébet Melinda},
	doi = {10.1186/s12974-020-02070-2},
	journal-iso = {J NEUROINFLAMM},
	journal = {JOURNAL OF NEUROINFLAMMATION},
	volume = {18},
	unique-id = {31807147},
	year = {2021},
	eissn = {1742-2094},
	orcid-numbers = {Walter, Fruzsina/0000-0001-8145-2823; Szögi, Titanilla/0000-0002-9854-7340; Fülöp, Lívia/0000-0002-8010-0129; Penke, Botond/0000-0003-0938-0567; Deli, Mária Anna/0000-0001-6084-6524}
}

@article{MTMT:31439812,
	title = {Post-diaminobenzidine Treatments for Double Stainings. Extension of Sulfide-Silver-Gold Intensification for Light and Fluorescent Microscopy},
	url = {https://m2.mtmt.hu/api/publication/31439812},
	author = {Apróné Török, Ibolya and Seprényi, György and Pór, Erzsébet and Borbély, Emőke and Szögi, Titanilla and Dobó, Endre},
	doi = {10.1369/0022155420942213},
	journal-iso = {J HISTOCHEM CYTOCHEM},
	journal = {JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY},
	volume = {68},
	unique-id = {31439812},
	issn = {0022-1554},
	abstract = {Double staining protocols using the most popular immunoperoxidase techniques may raise difficulties. The two ordinary detection systems may cross-talk, when the primary antibodies are derived from phylogenetically closely related animals. A color shift of the 3,3 '-diaminobenzidine (DAB) polymer may occur during the second development, resulting in poor distinction between the two kinds of deposits. A post-DAB technique, sulfide-silver-gold intensification, was fine tuned to eliminate these difficulties, which may be especially suitable for colocalization of cell nuclei and perikarya of the same cells. The revised method was probed in combination with a subsequent other immunoperoxidase step or fluorochrome-tagged reagents. The nuclear antigens (BrdU, c-Fos, and Prox-1) were first visualized with DAB polymer, which were then treated with SSGI, turning the deposit black. Thereafter, cytoplasmic antigens (doublecortin, neuronal nuclei, and calbindin) were detected with either another immunoperoxidase using DAB again or immunofluorescence labeling. In both approaches, the immunopositive nuclei and cytoplasmic sites could be easily distinguished even at low magnifications. Different shielding or eluting posttreatments were compared for consecutive acetylcholinesterase histochemistry terminated with DAB development and immunohistochemistry in the same sections. In conclusion, we recommend post-DAB treatments that abolish interactions between detection systems and allow clear distinction between the two signals under various conditions:},
	keywords = {immunohistochemistry; immunofluorescence; silver enhancement; DAB; Double staining; Diisopropyl fluorophosphate; acetylcholinesterase histochemistry},
	year = {2020},
	eissn = {1551-5044},
	pages = {571-582},
	orcid-numbers = {Apróné Török, Ibolya/0000-0002-2441-8925; Szögi, Titanilla/0000-0002-9854-7340}
}

@article{MTMT:30744451,
	title = {Effects of the Pentapeptide P33 on Memory and Synaptic Plasticity in APP/PS1 Transgenic Mice: A Novel Mechanism Presenting the Protein Fe65 as a Target},
	url = {https://m2.mtmt.hu/api/publication/30744451},
	author = {Szögi, Titanilla and Schuster, Ildikó and Borbély, Emőke and Gyebrovszki, Andrea and Bozsó, Zsolt and Gera, Janos and Rajkó, Róbert and Sántha, Miklós and Penke, Botond and Fülöp, Lívia},
	doi = {10.3390/ijms20123050},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {20},
	unique-id = {30744451},
	issn = {1661-6596},
	abstract = {Regulated intramembrane proteolysis (RIP) of the amyloid precursor protein (APP) leads to the formation of fragments, among which the intracellular domain of APP (AICD) was also identified to be a causative of early pathological events. AICD-counteracting proteins, such as Fe65, may serve as alternative therapeutic targets of Alzheimer's disease (AD). The detection of elevated levels of Fe65 in the brains of both human patients and APP transgenic mice may further strengthen the hypothesis that influencing the interaction between Fe65 and APP may have a beneficial effect on the course of AD. Based on a PXP motif, proven to bind to the WW domain of Fe65, a new pentapeptide was designed and tested. The impedimental effect of P33 on the production of beta amyloid (A beta) (soluble fraction and aggregated plaques) and on the typical features of the AD pathology (decreased dendritic spine density, synaptic markers, elevated inflammatory reactions) was also demonstrated. Significant enhancements of both learning ability and memory function were observed in a Morris water maze paradigm. The results led us to formulate the theory that P33 acts by altering the conformation of Fe65 via binding to its WW domain, consequently hindering any interactions between Fe65 and key members involved in APP processing.},
	year = {2019},
	eissn = {1422-0067},
	orcid-numbers = {Szögi, Titanilla/0000-0002-9854-7340; Schuster, Ildikó/0000-0001-9997-5729; Bozsó, Zsolt/0000-0002-5713-3096; Rajkó, Róbert/0000-0002-6234-658X; Penke, Botond/0000-0003-0938-0567; Fülöp, Lívia/0000-0002-8010-0129}
}

@misc{MTMT:30433688,
	title = {Peroxidáz alapú technika alkalmazása nukleáris és citoplazmatikus antigének egymás melletti kimutatására fény- és fluoreszcens mikroszkópiában},
	url = {https://m2.mtmt.hu/api/publication/30433688},
	author = {Apróné Török, Ibolya and Seprényi, György and Borbély, Emőke and Szögi, Titanilla and Hegyi, Péter and Dobó, Endre},
	unique-id = {30433688},
	year = {2018},
	orcid-numbers = {Apróné Török, Ibolya/0000-0002-2441-8925; Szögi, Titanilla/0000-0002-9854-7340}
}

@article{MTMT:3405755,
	title = {Searching for improved mimetic peptides inhibitors preventing conformational transition of amyloid-β42 monomer},
	url = {https://m2.mtmt.hu/api/publication/3405755},
	author = {Gera, János and Szögi, Titanilla and Bozsó, Zsolt and Fülöp, Lívia and Barrera, Exequiel E and Rodriguez, Ana M and Méndez, Luciana and Delpiccolo, Carina ML and Mata, Ernesto G and Cioffi, Federica and Broersen, Kerensa and Paragi, Gábor and Enriz, Ricardo D},
	doi = {10.1016/j.bioorg.2018.08.018},
	journal-iso = {BIOORG CHEM},
	journal = {BIOORGANIC CHEMISTRY},
	volume = {81},
	unique-id = {3405755},
	issn = {0045-2068},
	abstract = {A series of novel mimetic peptides were designed, synthesised and biologically evaluated as inhibitors of Aβ42 aggregation. One of the synthesised peptidic compounds, termed compound 7 modulated Aβ42 aggregation as demonstrated by thioflavin T fluorescence, acting also as an inhibitor of the cytotoxicity exerted by Aβ42 aggregates. The early stage interaction between compound 7 and the Aβ42 monomer was investigated by replica exchange molecular dynamics (REMD) simulations and docking studies. Our theoretical results revealed that compound 7 can elongate the helical conformation state of an early stage Aβ42 monomer and it helps preventing the formation of β-sheet structures by interacting with key residues in the central hydrophobic cluster (CHC). This strategy where early “on-pathway” events are monitored by small molecules will help the development of new therapeutic strategies for Alzheimer’s disease.},
	keywords = {Alzheimer's disease; molecular dynamics; Molecular docking; Amyloid β-peptide; Aβ aggregation; Mimetic peptides},
	year = {2018},
	eissn = {1090-2120},
	pages = {211-221},
	orcid-numbers = {Szögi, Titanilla/0000-0002-9854-7340; Bozsó, Zsolt/0000-0002-5713-3096; Fülöp, Lívia/0000-0002-8010-0129; Paragi, Gábor/0000-0001-5408-1748}
}

@article{MTMT:3399101,
	title = {Peripheral cyclic β-amino acids balance the stability and edge-protection of β-sandwiches},
	url = {https://m2.mtmt.hu/api/publication/3399101},
	author = {Olajos, Gábor and Hetényi, Anasztázia and Wéber, Edit and Szögi, Titanilla and Fülöp, Lívia and Martinek, Tamás},
	doi = {10.1039/c8ob01322e},
	journal-iso = {ORG BIOMOL CHEM},
	journal = {ORGANIC & BIOMOLECULAR CHEMISTRY},
	volume = {16},
	unique-id = {3399101},
	issn = {1477-0520},
	abstract = {Engineering water-soluble stand-alone beta-sandwich mimetics is a current challenge because of the difficulties associated with tailoring long-range interactions. In this work, single cis-(1R,2S)-2-aminocyclohexanecarboxylic acid mutations were introduced into the edge strands of the eight-stranded beta-sandwich mimetic structures from the betabellin family. Temperature-dependent NMR and CD measurements, together with thermodynamic analyses, demonstrated that the modified peripheral strands exhibited an irregular and partially disordered structure but were able to exert sufficient shielding on the hydrophobic core to retain the predominantly beta-sandwich structure. Although the frustrated interactions decreased the free energy of unfolding, the temperature of the maximum stabilities increased to or remained at physiologically relevant temperatures. We found that the irregular peripheral strands were able to prevent edge-to-edge association and fibril formation in the aggregation-prone model. These findings establish a beta-sandwich stabilization and aggregation inhibition approach, which does not interfere with the pillars of the peptide bond or change the net charge of the peptide.},
	keywords = {INHIBITORS; SECONDARY STRUCTURE; DE-NOVO DESIGN; HEAT-CAPACITY; ALPHA/BETA-PEPTIDES; protein–protein interactions; SHEET PROTEIN; FOLDING THERMODYNAMICS; GAMMA-PEPTIDES},
	year = {2018},
	eissn = {1477-0539},
	pages = {5492-5499},
	orcid-numbers = {Olajos, Gábor/0000-0002-2479-4891; Hetényi, Anasztázia/0000-0001-8080-6992; Wéber, Edit/0000-0002-5904-0619; Szögi, Titanilla/0000-0002-9854-7340; Fülöp, Lívia/0000-0002-8010-0129; Martinek, Tamás/0000-0003-3168-8066}
}