@article{MTMT:31612924,
	title = {AnnotatorJ: an ImageJ plugin to ease hand annotation of cellular compartments},
	url = {https://m2.mtmt.hu/api/publication/31612924},
	author = {Hollandi, Réka and Diósdi, Ákos and Hollandi, Gábor and Moshkov, Nikita and Horváth, Péter},
	doi = {10.1091/mbc.E20-02-0156},
	journal-iso = {MOL BIOL CELL},
	journal = {MOLECULAR BIOLOGY OF THE CELL},
	volume = {31},
	unique-id = {31612924},
	issn = {1059-1524},
	abstract = {AnnotatorJ combines single-cell identification with deep learning (DL) and manual annotation. Cellular analysis quality depends on accurate and reliable detection and segmentation of cells so that the subsequent steps of analyses, for example, expression measurements, may be carried out precisely and without bias. DL has recently become a popular way of segmenting cells, performing unimaginably better than conventional methods. However, such DL applications may be trained on a large amount of annotated data to be able to match the highest expectations. High-quality annotations are unfortunately expensive as they require field experts to create them, and often cannot be shared outside the lab due to medical regulations. We propose AnnotatorJ, an ImageJ plugin for the semiautomatic annotation of cells (or generally, objects of interest) on (not only) microscopy images in 2D that helps find the true contour of individual objects by applying U-Net-based presegmentation. The manual labor of hand annotating cells can be significantly accelerated by using our tool. Thus, it enables users to create such datasets that could potentially increase the accuracy of state-of-the-art solutions, DL or otherwise, when used as training data.},
	year = {2020},
	eissn = {1939-4586},
	pages = {2179-2186},
	orcid-numbers = {Diósdi, Ákos/0000-0002-3118-5576; Moshkov, Nikita/0000-0002-5823-4884}
}

@article{MTMT:30784321,
	title = {Heat-shock proteins in neuroinflammation},
	url = {https://m2.mtmt.hu/api/publication/30784321},
	author = {Dukay, Brigitta and Csoboz, Bálint and Tóth, Erzsébet Melinda},
	doi = {10.3389/fphar.2019.00920},
	journal-iso = {FRONT PHARMACOL},
	journal = {FRONTIERS IN PHARMACOLOGY},
	volume = {10},
	unique-id = {30784321},
	year = {2019},
	eissn = {1663-9812}
}

@article{MTMT:3371756,
	title = {Protection of cultured brain endothelial cells from cytokine-induced damage by α-melanocyte stimulating hormone},
	url = {https://m2.mtmt.hu/api/publication/3371756},
	author = {Harazin, András and Bocsik, Alexandra and Barna, Lilla and Kincses, András and Váradi, Judit and Fenyvesi, Ferenc and Tubak, Vilmos and Deli, Mária Anna and Vecsernyés, Miklós},
	doi = {10.7717/peerj.4774},
	journal-iso = {PEERJ},
	journal = {PEERJ},
	volume = {6},
	unique-id = {3371756},
	issn = {2167-8359},
	year = {2018},
	eissn = {2167-8359},
	orcid-numbers = {Harazin, András/0000-0002-0904-5606; Tubak, Vilmos/0000-0002-6141-3920; Deli, Mária Anna/0000-0001-6084-6524}
}

@article{MTMT:3326952,
	title = {Heat shock proteins and autophagy pathways in neuroprotection: From molecular bases to pharmacological interventions},
	url = {https://m2.mtmt.hu/api/publication/3326952},
	author = {Penke, Botond and Bogár, Ferenc and Crul, Tim and Sántha, Miklós and Tóth, Erzsébet Melinda and Vigh, László},
	doi = {10.3390/ijms19010325},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {19},
	unique-id = {3326952},
	issn = {1661-6596},
	abstract = {Neurodegenerative diseases (NDDs) such as Alzheimer’s disease, Parkinson’s disease and Huntington’s disease (HD), amyotrophic lateral sclerosis, and prion diseases are all characterized by the accumulation of protein aggregates (amyloids) into inclusions and/or plaques. The ubiquitous presence of amyloids in NDDs suggests the involvement of disturbed protein homeostasis (proteostasis) in the underlying pathomechanisms. This review summarizes specific mechanisms that maintain proteostasis, including molecular chaperons, the ubiquitin-proteasome system (UPS), endoplasmic reticulum associated degradation (ERAD), and different autophagic pathways (chaperon mediated-, micro-, and macro-autophagy). The role of heat shock proteins (Hsps) in cellular quality control and degradation of pathogenic proteins is reviewed. Finally, putative therapeutic strategies for efficient removal of cytotoxic proteins from neurons and design of new therapeutic targets against the progression of NDDs are discussed. © 2018 by the authors.},
	keywords = {neurodegenerative diseases; neuroprotection; UBIQUITIN-PROTEASOME SYSTEM; Heat shock proteins; Autophagy; endoplasmic reticulum associated degradation; Hsp-inducers; Autophagy modulating drugs},
	year = {2018},
	eissn = {1422-0067},
	orcid-numbers = {Penke, Botond/0000-0003-0938-0567; Bogár, Ferenc/0000-0002-0611-1452; Crul, Tim/0000-0002-6053-7016}
}

@article{MTMT:3060238,
	title = {Microglia protect against brain injury and their selective elimination dysregulates neuronal network activity after stroke},
	url = {https://m2.mtmt.hu/api/publication/3060238},
	author = {Szalay, Gergely and Martinecz, Bernadett and Lénárt, Nikolett and Környei, Zsuzsanna and Orsolits, Barbara and Judák, Linda and Császár, Eszter and Fekete, Rebeka and West, BL and Katona, Gergely and Rózsa J., Balázs and Dénes, Ádám},
	doi = {10.1038/ncomms11499},
	journal-iso = {NAT COMMUN},
	journal = {NATURE COMMUNICATIONS},
	volume = {7},
	unique-id = {3060238},
	issn = {2041-1723},
	abstract = {Microglia are the main immune cells of the brain and contribute to common brain diseases. However, it is unclear how microglia influence neuronal activity and survival in the injured brain in vivo. Here we develop a precisely controlled model of brain injury induced by cerebral ischaemia combined with fast in vivo two-photon calcium imaging and selective microglial manipulation. We show that selective elimination of microglia leads to a striking, 60% increase in infarct size, which is reversed by microglial repopulation. Microglia-mediated protection includes reduction of excitotoxic injury, since an absence of microglia leads to dysregulated neuronal calcium responses, calcium overload and increased neuronal death. Furthermore, the incidence of spreading depolarization (SD) is markedly reduced in the absence of microglia. Thus, microglia are involved in changes in neuronal network activity and SD after brain injury in vivo that could have important implications for common brain diseases.},
	year = {2016},
	eissn = {2041-1723},
	orcid-numbers = {Lénárt, Nikolett/0000-0002-7456-949X; Császár, Eszter/0000-0002-5543-4100; Katona, Gergely/0000-0002-4173-0355}
}

@article{MTMT:2920970,
	title = {Cultured cells of the blood-brain barrier from apolipoprotein B-100 transgenic mice: effects of oxidized low-density lipoprotein treatment},
	url = {https://m2.mtmt.hu/api/publication/2920970},
	author = {Lénárt, Nikolett and Walter, Fruzsina and Bocsik, Alexandra and Sántha, Petra and Tóth, Erzsébet Melinda and Harazin, András and Tóth, Andrea and Vizler, Csaba and Török, Zsolt and Pilbat, Ana Maria and Vigh, László and Puskás, László and Sántha, Miklós and Deli, Mária Anna},
	doi = {10.1186/s12987-015-0013-y},
	journal-iso = {FLUIDS BARRIERS CNS},
	journal = {FLUIDS AND BARRIERS OF THE CNS},
	volume = {12},
	unique-id = {2920970},
	issn = {2045-8118},
	year = {2015},
	eissn = {2045-8118},
	orcid-numbers = {Lénárt, Nikolett/0000-0002-7456-949X; Walter, Fruzsina/0000-0001-8145-2823; Harazin, András/0000-0002-0904-5606; Deli, Mária Anna/0000-0001-6084-6524}
}

@article{MTMT:2365063,
	title = {Overexpression of Hsp27 ameliorates symptoms of Alzheimer's disease in APP/PS1 mice},
	url = {https://m2.mtmt.hu/api/publication/2365063},
	author = {Tóth, Erzsébet Melinda and Szegedi, Viktor and Varga, Edina and Juhász, Gábor and Horváth, János and Borbély, Emőke and Csibrány, Balázs and Alföldi, Róbert and Lénárt, Nikolett and Penke, Botond and Sántha, Miklós},
	doi = {10.1007/s12192-013-0428-9},
	journal-iso = {CELL STRESS CHAPERON},
	journal = {CELL STRESS & CHAPERONES},
	volume = {18},
	unique-id = {2365063},
	issn = {1355-8145},
	abstract = {Hsp27 belongs to the small heat shock protein family, which are ATP-independent chaperones. The most important function of Hsp27 is based on its ability to bind non-native proteins and inhibit the aggregation of incorrectly folded proteins maintaining them in a refolding-competent state. Additionally, it has anti-apoptotic and antioxidant activities. To study the effect of Hsp27 on memory and synaptic functions, amyloid-β (Aβ) accumulation, and neurodegeneration, we generated transgenic mice overexpressing human Hsp27 protein and crossed with APPswe/PS1dE9 mouse strain, a mouse model of Alzheimer's disease (AD). Using different behavioral tests, we found that spatial learning was impaired in AD model mice and was rescued by Hsp27 overexpression. Electrophysiological recordings have revealed that excitability of neurons was significantly increased, and long-term potentiation (LTP) was impaired in AD model mice, whereas they were normalized in Hsp27 overexpressing AD model mice. Using anti-amyloid antibody, we counted significantly less amyloid plaques in the brain of APPswe/PS1dE9/Hsp27 animals compared to AD model mice. These results suggest that overexpression of Hsp27 protein might ameliorate certain symptoms of AD. © 2013 Cell Stress Society International.},
	keywords = {TRANSGENIC MICE; Alzheimer's disease; MOUSE MODEL; Heat shock proteins; Electrophysiological recordings; Real-time Q-PCR; Behavior tests; Amyloid plaques},
	year = {2013},
	eissn = {1466-1268},
	pages = {759-771},
	orcid-numbers = {Szegedi, Viktor/0000-0003-4191-379X; Lénárt, Nikolett/0000-0002-7456-949X; Penke, Botond/0000-0003-0938-0567}
}

@article{MTMT:1921491,
	title = {Neuroprotective effect of small heat shock protein, Hsp27, after acute and chronic alcohol administration.},
	url = {https://m2.mtmt.hu/api/publication/1921491},
	author = {Tóth, Erzsébet Melinda and Gonda, Szilvia and Vigh, László and Sántha, Miklós},
	doi = {10.1007/s12192-010-0188-8},
	journal-iso = {CELL STRESS CHAPERON},
	journal = {CELL STRESS & CHAPERONES},
	volume = {15},
	unique-id = {1921491},
	issn = {1355-8145},
	year = {2010},
	eissn = {1466-1268},
	pages = {807-817}
}

@article{MTMT:1915070,
	title = {The Small Heat Shock Proteins And Their Clients},
	url = {https://m2.mtmt.hu/api/publication/1915070},
	author = {Nakamoto, H and Vigh, László},
	doi = {10.1007/s00018-006-6321-2},
	journal-iso = {CELL MOL LIFE SCI},
	journal = {CELLULAR AND MOLECULAR LIFE SCIENCES},
	volume = {64},
	unique-id = {1915070},
	issn = {1420-682X},
	year = {2007},
	eissn = {1420-9071},
	pages = {294-306}
}