@article{MTMT:1746145,
	title = {Kainate postconditioning restores LTP in ischemic hippocampal CA1: Onset-dependent second pathophysiological stress},
	url = {https://m2.mtmt.hu/api/publication/1746145},
	author = {Nagy, D and Kocsis, Kitti and Fuzik, J and Marosi, Máté Gábor and Kis, Zsolt and Teichberg, V I and Toldi, József and Farkas, Tamás},
	doi = {10.1016/j.neuropharm.2011.07.005},
	journal-iso = {NEUROPHARMACOLOGY},
	journal = {NEUROPHARMACOLOGY},
	volume = {61},
	unique-id = {1746145},
	issn = {0028-3908},
	abstract = {Postconditioning can be induced by a broad range of stimuli within minutes to days after an ischemic cerebral insult. A special form is elicited by pharmacological intervention called second pathophysiological stress. The present study aimed to evaluate the effects of low-dose (5 mg/kg) kainate postconditioning with onsets 0, 24 and 48 h after the ischemic insult on the hippocampal synaptic plasticity in a 2-vessel occlusion model in rat. The hippocampal function was tested by LTP measurements of Schaffer collateral-CA1 pyramidal cell synapses in acute slices and the changes in density of Golgi-Cox-stained apical dendritic spines. Postconditioning 0 and 24 h after ischemia was not protective, whereas 48-h-onset postconditioning resulted in the reappearance of a normal spine density (>100,000 spines) 3 days after ischemia, in parallel with the long-term restoration of the damaged LTP function. Similar, but somewhat less effects were observed after 10 days. Our data clearly demonstrate the onset dependence of postconditioning elicited by a subconvulsant dose of kainate treatment in global ischemia, with restoration of the structural plasticity and hippocampal function. © 2011 Elsevier Ltd. All rights reserved.},
	keywords = {Male; KAINIC ACID; ARTICLE; priority journal; controlled study; nonhuman; animal tissue; animal experiment; animal cell; brain ischemia; CA1; synapse; neuroprotection; LTP; drug dose reduction; Postconditioning; brain function; nerve cell plasticity; low drug dose; pyramidal nerve cell; blood vessel occlusion; brain slice; dendritic spine; brain blood vessel; second pathophysiological stress; pharmacological procedures; pharmacological postconditioning; long term potentiation; hippocampal CA1 region; Golgi stain; Spine density; 2-vessel occlusion; rat},
	year = {2011},
	eissn = {1873-7064},
	pages = {1026-1032},
	orcid-numbers = {Kis, Zsolt/0000-0002-6896-5883; Toldi, József/0000-0001-7355-0503}
}

@article{MTMT:1329681,
	title = {Controlled in situ preparation of Aβ(1-42) oligomers from the isopeptide "iso-Aβ(1-42)", physicochemical and biological characterization},
	url = {https://m2.mtmt.hu/api/publication/1329681},
	author = {Bozsó, Zsolt and Penke, Botond and Simon, Dóra and Laczkó, Ilona and Juhász, Gábor and Szegedi, Viktor and Kasza, Ágnes and Soós, Katalin and Hetényi, Anasztázia and Wéber, Edit and Tóháti, Hajnalka-Mária and Czirjákné Csete, Mária and Zarándi, Márta and Fülöp, Lívia},
	doi = {10.1016/j.peptides.2009.12.001},
	journal-iso = {PEPTIDES},
	journal = {PEPTIDES},
	volume = {31},
	unique-id = {1329681},
	issn = {0196-9781},
	abstract = {beta-Amyloid (A beta) peptides play a crucial role in the pathology of the neurodegeneration in Alzheimer's disease (AD). Biological experiments (both in vitro and animal model studies of AD) require synthetic A beta peptides of standard quality, aggregation grade, neurotoxicity and water solubility. The synthesis of A beta peptides has been difficult, owing to their hydrophobic character, poor solubility and high tendency for aggregation. Recently an isopeptide precursor (iso-A beta(1-42)) was synthesized by Fmoc-chemistry and transformed at neutral pH to A beta(1-42) by O -> N acyl migration in a short period of time. We prepared the same precursor peptide using Boc-chemistry and studied the transformation to A beta(1-42) by acyl migration. The peptide conformation and aggregation processes were studied by several methods (circular dichroism, atomic force and transmission electron microscopy, dynamic light scattering). The biological activity of the synthetic A beta(1-42) was measured by ex vivo (long-term potentiation studies in rat hippocampal slices) and in vivo experiments (spatial learning of rats). It was proven that O -> N acyl migration of the precursor isopeptide results in a water soluble oligomeric mixture of neurotoxic A beta(1-42). These oligomers; are formed in situ just before the biological experiments and their aggregation grade could be standardized. (C) 2009 Elsevier Inc. All rights reserved.},
	keywords = {AGGREGATION; ALZHEIMERS-DISEASE; PROTEIN; SOLID-PHASE SYNTHESIS; AMYLOID-BETA; OLIGOMERS; Alzheimer's disease; DEPROTECTION; PEPTIDE-SYNTHESIS; beta-Amyloid; Endocrinology & Metabolism; Biochemistry & Molecular Biology; DIFFICULT SEQUENCES; A-BETA-1-42 ISOPEPTIDE; PSEUDO-PROLINES},
	year = {2010},
	eissn = {1873-5169},
	pages = {248-256},
	orcid-numbers = {Bozsó, Zsolt/0000-0002-5713-3096; Penke, Botond/0000-0003-0938-0567; Szegedi, Viktor/0000-0003-4191-379X; Hetényi, Anasztázia/0000-0001-8080-6992; Wéber, Edit/0000-0002-5904-0619; Czirjákné Csete, Mária/0000-0002-3755-714X; Zarándi, Márta/0000-0002-2136-2946; Fülöp, Lívia/0000-0002-8010-0129}
}