TY - JOUR AU - Szalay, Gergely AU - Judák, Linda AU - Katona, Gergely AU - Ocsai, K AU - Juhász, Gábor AU - Veress, Máté AU - Szadai, Zoltán AU - Fehér, András AU - Tompa, Tamás AU - Chiovini, Balázs AU - Maák, Pál AU - Rózsa J., Balázs TI - Fast 3D Imaging of Spine, Dendritic, and Neuronal Assemblies in Behaving Animals. JF - NEURON J2 - NEURON VL - 92 PY - 2016 IS - 4 SP - 723 EP - 738 PG - 16 SN - 0896-6273 DO - 10.1016/j.neuron.2016.10.002 UR - https://m2.mtmt.hu/api/publication/3144889 ID - 3144889 N1 - Laboratory of 3D Functional Network and Dendritic Imaging, Institute of Experimental Medicine, Hungarian Academy of SciencesBudapest 1083, Hungary MTA-PPKE ITK-NAP B–2p Measurement Technology Group, Faculty of Information Technology, Pázmány Péter Catholic UniversityBudapest 1083, Hungary Two-Photon Laboratory, Faculty of Information Technology, Pázmány Péter Catholic UniversityBudapest 1083, Hungary Department of Atomic Physics, Budapest University of Technology and EconomicsBudapest 1111, Hungary Cited By :33 Export Date: 17 March 2021 CODEN: NERNE Correspondence Address: Rózsa, B.; Laboratory of 3D Functional Network and Dendritic Imaging, Hungary; email: rozsabal@koki.hu Funding details: /7/2/8, FP7-ICT-2011-C 323945, KMR_12-1-2012-0214, KTIA_NAP_12-2-2015-0006, VKSZ_14-1-2015-0155 Funding details: Horizon 2020 Framework Programme, H2020 Funding details: Seventh Framework Programme, FP7, 323945 Funding details: European Research Council, ERC, 682426 Funding details: Hungarian Scientific Research Fund, OTKA, K105997 Funding text 1: We thank Botond Roska and David Fitzpatrick for their helpful comments. This work was supported by the Hungarian-French grant, Swiss-Hungarian grant /7/2/8, KMR_12-1-2012-0214, FP7-ICT-2011-C 323945 (3x3D imaging), KTIA_NAP_12-2-2015-0006, VKSZ_14-1-2015-0155, OTKA ( K105997 ), and ERC 682426. G.K. and B.R. are founders of Femtonics Kft. B.R. is a member of its scientific advisory board. Laboratory of 3D Functional Network and Dendritic Imaging, Institute of Experimental Medicine, Hungarian Academy of SciencesBudapest 1083, Hungary MTA-PPKE ITK-NAP B–2p Measurement Technology Group, Faculty of Information Technology, Pázmány Péter Catholic UniversityBudapest 1083, Hungary Two-Photon Laboratory, Faculty of Information Technology, Pázmány Péter Catholic UniversityBudapest 1083, Hungary Department of Atomic Physics, Budapest University of Technology and EconomicsBudapest 1111, Hungary Cited By :33 Export Date: 18 March 2021 CODEN: NERNE Correspondence Address: Rózsa, B.; Laboratory of 3D Functional Network and Dendritic Imaging, Hungary; email: rozsabal@koki.hu Funding details: /7/2/8, FP7-ICT-2011-C 323945, KMR_12-1-2012-0214, KTIA_NAP_12-2-2015-0006, VKSZ_14-1-2015-0155 Funding details: Horizon 2020 Framework Programme, H2020 Funding details: Seventh Framework Programme, FP7, 323945 Funding details: European Research Council, ERC, 682426 Funding details: Hungarian Scientific Research Fund, OTKA, K105997 Funding text 1: We thank Botond Roska and David Fitzpatrick for their helpful comments. This work was supported by the Hungarian-French grant, Swiss-Hungarian grant /7/2/8, KMR_12-1-2012-0214, FP7-ICT-2011-C 323945 (3x3D imaging), KTIA_NAP_12-2-2015-0006, VKSZ_14-1-2015-0155, OTKA ( K105997 ), and ERC 682426. G.K. and B.R. are founders of Femtonics Kft. B.R. is a member of its scientific advisory board. Laboratory of 3D Functional Network and Dendritic Imaging, Institute of Experimental Medicine, Hungarian Academy of SciencesBudapest 1083, Hungary MTA-PPKE ITK-NAP B–2p Measurement Technology Group, Faculty of Information Technology, Pázmány Péter Catholic UniversityBudapest 1083, Hungary Two-Photon Laboratory, Faculty of Information Technology, Pázmány Péter Catholic UniversityBudapest 1083, Hungary Department of Atomic Physics, Budapest University of Technology and EconomicsBudapest 1111, Hungary Cited By :34 Export Date: 7 April 2021 CODEN: NERNE Correspondence Address: Rózsa, B.; Laboratory of 3D Functional Network and Dendritic Imaging, Hungary; email: rozsabal@koki.hu Funding details: /7/2/8, FP7-ICT-2011-C 323945, KMR_12-1-2012-0214, KTIA_NAP_12-2-2015-0006, VKSZ_14-1-2015-0155 Funding details: Horizon 2020 Framework Programme, H2020 Funding details: Seventh Framework Programme, FP7, 323945 Funding details: European Research Council, ERC, 682426 Funding details: Hungarian Scientific Research Fund, OTKA, K105997 Funding text 1: We thank Botond Roska and David Fitzpatrick for their helpful comments. This work was supported by the Hungarian-French grant, Swiss-Hungarian grant /7/2/8, KMR_12-1-2012-0214, FP7-ICT-2011-C 323945 (3x3D imaging), KTIA_NAP_12-2-2015-0006, VKSZ_14-1-2015-0155, OTKA ( K105997 ), and ERC 682426. G.K. and B.R. are founders of Femtonics Kft. B.R. is a member of its scientific advisory board. Laboratory of 3D Functional Network and Dendritic Imaging, Institute of Experimental Medicine, Hungarian Academy of SciencesBudapest 1083, Hungary MTA-PPKE ITK-NAP B–2p Measurement Technology Group, Faculty of Information Technology, Pázmány Péter Catholic UniversityBudapest 1083, Hungary Two-Photon Laboratory, Faculty of Information Technology, Pázmány Péter Catholic UniversityBudapest 1083, Hungary Department of Atomic Physics, Budapest University of Technology and EconomicsBudapest 1111, Hungary Cited By :35 Export Date: 20 April 2021 CODEN: NERNE Correspondence Address: Rózsa, B.; Laboratory of 3D Functional Network and Dendritic Imaging, Hungary; email: rozsabal@koki.hu Funding details: /7/2/8, FP7-ICT-2011-C 323945, KMR_12-1-2012-0214, KTIA_NAP_12-2-2015-0006, VKSZ_14-1-2015-0155 Funding details: Horizon 2020 Framework Programme, H2020 Funding details: Seventh Framework Programme, FP7, 323945 Funding details: European Research Council, ERC, 682426 Funding details: Hungarian Scientific Research Fund, OTKA, K105997 Funding text 1: We thank Botond Roska and David Fitzpatrick for their helpful comments. This work was supported by the Hungarian-French grant, Swiss-Hungarian grant /7/2/8, KMR_12-1-2012-0214, FP7-ICT-2011-C 323945 (3x3D imaging), KTIA_NAP_12-2-2015-0006, VKSZ_14-1-2015-0155, OTKA ( K105997 ), and ERC 682426. G.K. and B.R. are founders of Femtonics Kft. B.R. is a member of its scientific advisory board. Laboratory of 3D Functional Network and Dendritic Imaging, Institute of Experimental Medicine, Hungarian Academy of SciencesBudapest 1083, Hungary MTA-PPKE ITK-NAP B–2p Measurement Technology Group, Faculty of Information Technology, Pázmány Péter Catholic UniversityBudapest 1083, Hungary Two-Photon Laboratory, Faculty of Information Technology, Pázmány Péter Catholic UniversityBudapest 1083, Hungary Department of Atomic Physics, Budapest University of Technology and EconomicsBudapest 1111, Hungary Cited By :35 Export Date: 23 April 2021 CODEN: NERNE Correspondence Address: Rózsa, B.; Laboratory of 3D Functional Network and Dendritic Imaging, Hungary; email: rozsabal@koki.hu Funding details: /7/2/8, FP7-ICT-2011-C 323945, KMR_12-1-2012-0214, KTIA_NAP_12-2-2015-0006, VKSZ_14-1-2015-0155 Funding details: Horizon 2020 Framework Programme, H2020 Funding details: Seventh Framework Programme, FP7, 323945 Funding details: European Research Council, ERC, 682426 Funding details: Hungarian Scientific Research Fund, OTKA, K105997 Funding text 1: We thank Botond Roska and David Fitzpatrick for their helpful comments. This work was supported by the Hungarian-French grant, Swiss-Hungarian grant /7/2/8, KMR_12-1-2012-0214, FP7-ICT-2011-C 323945 (3x3D imaging), KTIA_NAP_12-2-2015-0006, VKSZ_14-1-2015-0155, OTKA ( K105997 ), and ERC 682426. G.K. and B.R. are founders of Femtonics Kft. B.R. is a member of its scientific advisory board. AB - Understanding neural computation requires methods such as 3D acousto-optical (AO) scanning that can simultaneously read out neural activity on both the somatic and dendritic scales. AO point scanning can increase measurement speed and signal- to-noise ratio (SNR) by several orders of magnitude, but high optical resolution requires long point-to-point switching time, which limits imaging capability. Here we present a novel technology, 3D DRIFT AO scanning, which can extend each scanning point to small 3D lines, surfaces, or volume elements for flexible and fast imaging of complex structures simultaneously in multiple locations. Our method was demonstrated by fast 3D recording of over 150 dendritic spines with 3D lines, over 100 somata with squares and cubes, or multiple spiny dendritic segments with surface and volume elements, including in behaving animals. Finally, a 4-fold improvement in total excitation efficiency resulted in about 500 x 500 x 650 mum scanning volume with genetically encoded calcium indicators (GECIs). LA - English DB - MTMT ER - TY - JOUR AU - Varga, Edina AU - Juhász, Gábor AU - Bozsó, Zsolt AU - Penke, Botond AU - Fülöp, Lívia AU - Szegedi, Viktor TI - Amyloid-β1-42 disrupts synaptic plasticity by altering glutamate recycling at the synapse JF - JOURNAL OF ALZHEIMER'S DISEASE J2 - J ALZHEIMERS DIS VL - 45 PY - 2015 IS - 2 SP - 449 EP - 456 PG - 8 SN - 1387-2877 DO - 10.3233/JAD-142367 UR - https://m2.mtmt.hu/api/publication/2812783 ID - 2812783 AB - Alzheimer's disease (AD) is the most prevalent form of neurodegenerative disorders characterized by neuritic plaques containing amyloid-beta peptide (Abeta) and neurofibrillary tangles. Evidence has been reported that Abeta1-42 plays an essential pathogenic role in decreased spine density, impairment of synaptic plasticity, and neuronal loss with disruption of memory-related synapse function, all associated with AD. Experimentally, Abeta1-42 oligomers perturb hippocampal long-term potentiation (LTP), an electrophysiological correlate of learning and memory. Abeta was also reported to perturb synaptic glutamate (Glu)-recycling by inhibiting excitatory-amino-acid-transporters. Elevated level of extracellular Glu leads to activation of perisynaptic receptors, including NR2B subunit containing NMDARs. These receptors were shown to induce impaired LTP and enhanced long-term depression and proapoptotic pathways, all central features of AD. In the present study, we investigated the role of Glu-recycling on Abeta1-42-induced LTP deficit in the CA1. We found that Abeta-induced LTP damage, which was mimicked by the Glu-reuptake inhibitor TBOA, could be rescued by blocking the NR2B subunit of NMDA receptors. Furthermore, decreasing the level of extracellular Glu using a Glu scavenger also restores TBOA or Abeta induces LTP damage. Overall, these results suggest that reducing ambient Glu in the brain can be protective against Abeta-induced synaptic disruption. LA - English DB - MTMT ER - TY - JOUR AU - Varga, Edina AU - Juhász, Gábor AU - Bozsó, Zsolt AU - Penke, Botond AU - Fülöp, Lívia AU - Szegedi, Viktor TI - Abeta(1-42) Enhances Neuronal Excitability in the CA1 via NR2B Subunit-Containing NMDA Receptors JF - NEURAL PLASTICITY J2 - NEURAL PLAST VL - 2014 PY - 2014 PG - 12 SN - 2090-5904 DO - 10.1155/2014/584314 UR - https://m2.mtmt.hu/api/publication/2755870 ID - 2755870 AB - Neuronal hyperexcitability is a phenomenon associated with early Alzheimer's disease. The underlying mechanism is considered to involve excessive activation of glutamate receptors; however, the exact molecular pathway remains to be determined. Extracellular recording from the CA1 of hippocampal slices is a long-standing standard for a range of studies both in basic research and in neuropharmacology. Evoked field potentials (fEPSPs) are regarded as the input, while spiking rate is regarded as the output of the neuronal network; however, the relationship between these two phenomena is not fully clear. We investigated the relationship between spontaneous spiking and evoked fEPSPs using mouse hippocampal slices. Blocking AMPA receptors (AMPARs) with CNQX abolished fEPSPs, but left firing rate unchanged. NMDA receptor (NMDAR) blockade with MK801 decreased neuronal spiking dose dependently without altering fEPSPs. Activating NMDARs by small concentration of NMDA induced a trend of increased firing. These results suggest that fEPSPs are mediated by synaptic activation of AMPARs, while spontaneous firing is regulated by the activation of extrasynaptic NMDARs. Synaptotoxic Abeta(1-42) increased firing activity without modifying evoked fEPSPs. This hyperexcitation was prevented by ifenprodil, an antagonist of the NR2B NMDARs. Overall, these results suggest that Abeta(1-42) induced neuronal overactivity is not dependent on AMPARs but requires NR2B. LA - English DB - MTMT ER - TY - JOUR AU - Tóth, Erzsébet Melinda AU - Szegedi, Viktor AU - Varga, Edina AU - Juhász, Gábor AU - Horváth, János AU - Borbély, Emőke AU - Csibrány, Balázs AU - Alföldi, Róbert AU - Lénárt, Nikolett AU - Penke, Botond AU - Sántha, Miklós TI - Overexpression of Hsp27 ameliorates symptoms of Alzheimer's disease in APP/PS1 mice JF - CELL STRESS & CHAPERONES J2 - CELL STRESS CHAPERON VL - 18 PY - 2013 IS - 6 SP - 759 EP - 771 PG - 13 SN - 1355-8145 DO - 10.1007/s12192-013-0428-9 UR - https://m2.mtmt.hu/api/publication/2365063 ID - 2365063 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Lénárt, Nikolett AU - Szegedi, Viktor AU - Juhász, Gábor AU - Kasztner, Anikó AU - Horváth, János AU - Bereczki, Erika AU - Tóth, Erzsébet Melinda AU - Penke, Botond AU - Sántha, Miklós TI - Increased Tau Phosphorylation and Impaired Presynaptic Function in Hypertriglyceridemic ApoB-100 Transgenic Mice JF - PLOS ONE J2 - PLOS ONE VL - 7 PY - 2012 IS - 9 PG - 12 SN - 1932-6203 DO - 10.1371/journal.pone.0046007 UR - https://m2.mtmt.hu/api/publication/2101104 ID - 2101104 AB - Aims: ApoB-100 is the major protein component of cholesterol- and triglyceride-rich LDL and VLDL lipoproteins in the serum. Previously, we generated and partially described transgenic mice overexpressing the human ApoB-100 protein. Here, we further characterize this transgenic strain in order to reveal a possible link between hypeprlipidemia and neurodegeneration. Methods and Results: We analyzed the serum and cerebral lipid profiles, tau phosphorylation patterns, amyloid plaque-formation, neuronal apoptosis and synaptic plasticity of young (3 month old), adult (6 month old) and aging (10-11 month old) transgenic mice. We show that ApoB-100 transgenic animals present i) elevated serum and cerebral levels of triglycerides and ApoB-100, ii) increased cerebral tau phosphorylation at phosphosites Ser 199, Ser 199/202, Ser 396 and Ser 404. Furthermore, we demonstrate, that tau hyperphosphorylation is accompanied by impaired presynaptic function, long-term potentiation and widespread hippocampal neuronal apoptosis. Conclusions: The results presented here indicate that elevated ApoB-100 level and the consequent chronic hypertriglyceridemia may lead to impaired neuronal function and neurodegeneration, possibly via hyperphosphorylation of tau protein. On account of their specific phenotype, ApoB-100 transgenic mice may be considered a versatile model of hyperlipidemia-induced age-related neurodegeneration. © 2012 Lénárt et al. LA - English DB - MTMT ER - TY - JOUR AU - Fülöp, Lívia AU - Mándity, István AU - Juhász, Gábor AU - Szegedi, Viktor AU - Hetényi, Anasztázia AU - Wéber, Edit AU - Bozsó, Zsolt AU - Simon, Dóra AU - Benkő, Mária AU - Király, Zoltán AU - Martinek, Tamás TI - A Foldamer-Dendrimer Conjugate Neutralizes Synaptotoxic Beta-Amyloid Oligomers JF - PLOS ONE J2 - PLOS ONE VL - 7 PY - 2012 IS - 7 PG - 17 SN - 1932-6203 DO - 10.1371/journal.pone.0039485 UR - https://m2.mtmt.hu/api/publication/2034805 ID - 2034805 N1 - Funding Agency and Grant Number: EU FP7 [HEALTH-F2-2007-201159, HEALTH-F2-2007-211696]; COST [CM0803]; Hungarian Research Foundation [NK81371, PD83581, PD83600, K68152]; Hungarian Academy of Sciences, Lendulet programme\n Funding text: This work was supported by the EU FP7 (HEALTH-F2-2007-201159, HEALTH-F2-2007-211696 and COST CM0803) (http://cordis.europa.eu/fp7/home_en.html); the Hungarian Research Foundation (NK81371, PD83581, PD83600 and K68152) (http://www.otka.hu/); and the Hungarian Academy of Sciences, Lendulet programme (http://mta.hu/). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.\n Department of Medical Chemistry, University of Szeged, Szeged, Hungary Institute of Pharmaceutical Chemistry, University of Szeged, Szeged, Hungary Bay Zoltán Foundation for Applied Research - BAYGEN, Szeged, Hungary Department of Physical Chemistry and Materials Science, University of Szeged, Szeged, Hungary Cited By :31 Export Date: 24 April 2020 Correspondence Address: Martinek, T. A.; Institute of Pharmaceutical Chemistry, University of Szeged, Szeged, Hungary; email: martinek@pharm.u-szeged.hu Chemicals/CAS: amyloid beta protein, 109770-29-8; Amyloid beta-Peptides; Dendrimers CAplus AN 2012:1144372; MEDLINE PMID: 22859942 (Journal; Article; Research Support, Non-U.S. Gov't); AB - Background and Aims

Unnatural self-organizing biomimetic polymers (foldamers) emerged as promising materials for biomolecule recognition and inhibition. Our goal was to construct multivalent foldamer-dendrimer conjugates which wrap the synaptotoxic β-amyloid (Aβ) oligomers with high affinity through their helical foldamer tentacles. Oligomeric Aβ species play pivotal role in Alzheimer's disease, therefore recognition and direct inhibition of this undruggable target is a great current challenge.

Methods and Results

Short helical β-peptide foldamers with designed secondary structures and side chain chemistry patterns were applied as potential recognition segments and their binding to the target was tested with NMR methods (saturation transfer difference and transferred-nuclear Overhauser effect). Helices exhibiting binding in the µM region were coupled to a tetravalent G0-PAMAM dendrimer. In vitro biophysical (isothermal titration calorimetry, dynamic light scattering, transmission electron microscopy and size-exclusion chromatography) and biochemical tests (ELISA and dot blot) indicated the tight binding between the foldamer conjugates and the Aβ oligomers. Moreover, a selective low nM interaction with the low molecular weight fraction of the Aβ oligomers was found. Ex vivo electrophysiological experiments revealed that the new material rescues the long-term potentiation from the toxic Aβ oligomers in mouse hippocampal slices at submicromolar concentration.

Conclusions

The combination of the foldamer methodology, the fragment-based approach and the multivalent design offers a pathway to unnatural protein mimetics that are capable of specific molecular recognition, and has already resulted in an inhibitor for an extremely difficult target.

 LA - English DB - MTMT ER - TY - JOUR AU - Barkóczi, Balázs Zoltán AU - Juhász, Gábor AU - Averkin, Róbert AU - Voros, Imre AU - Vertes, Petra AU - Penke, Botond AU - Szegedi, Viktor TI - GluA1 phosphorylation alters evoked firing pattern in vivo JF - NEURAL PLASTICITY J2 - NEURAL PLAST VL - 2012 PY - 2012 PG - 8 SN - 2090-5904 DO - 10.1155/2012/286215 UR - https://m2.mtmt.hu/api/publication/1848719 ID - 1848719 LA - English DB - MTMT ER - TY - JOUR AU - Szegedi, Viktor AU - Juhász, Gábor AU - Zhang, XQ AU - Barkóczi, Balázs Zoltán AU - Qi, HS AU - Madeira, A AU - Kapus, G AU - Svenningsson, P AU - Spedding, M AU - Penke, Botond TI - Tianeptine potentiates AMPA receptors by activating CaMKII and PKA via the p38, p42/44 MAPK and JNK pathways JF - NEUROCHEMISTRY INTERNATIONAL J2 - NEUROCHEM INT VL - 59 PY - 2011 IS - 8 SP - 1109 EP - 1122 PG - 14 SN - 0197-0186 DO - 10.1016/j.neuint.2011.10.008 UR - https://m2.mtmt.hu/api/publication/1842703 ID - 1842703 AB - Impairments of cellular plasticity appear to underlie the pathophysiology of major depression. Recently, elevated levels of phosphorylated AMPA receptor were implicated in the antidepressant effect of various drugs. Here, we investigated the effects of an antidepressant, Tianeptine, on synaptic function and GluA1 phosphorylation using murine hippocampal slices and in vivo single-unit recordings. Tianeptine, but not imipramine, increased AMPA receptor-mediated neuronal responses both in vitro and in vivo, in a stauro-sporine-sensitive manner. Paired-pulse ratio was unaltered by Tianeptine, suggesting a postsynaptic site of action. Tianeptine, 10 mu M, enhanced the GluA1-dependent initial phase of LIP, whereas 100 mu M impaired the latter phases, indicating a critical role of GluA1 subunit phosphorylation in the excitation. Tianeptine rapidly increased the phosphorylation level of Ser(831)-GluA1 and Ser(845)-GluA1. Using H-89 and KN-93, we show that the activation of both PKA and CaMKII is critical in the effect of Tianeptine on AMPA responses. Moreover, the phosphorylation states of Ser(217/221)-MEK and Thr(183)/Tyr(185)-p42MAPK were increased by Tianeptine and specific kinase blockers of the MAPK pathways (PD 98095, SB 203580 and SP600125) prevented the effects of Tianeptine. Overall these data suggest that Tianeptine potentiates several signaling cascades associated with synaptic plasticity and provide further evidence that a major mechanism of action for Tianeptine is to act as an enhancer of glutamate neurotransmission via AMPA receptors. (C) 2011 Elsevier B.V. All rights reserved. LA - English DB - MTMT ER - TY - JOUR AU - Virók, Dezső AU - Kis, Z AU - Szegedi, Viktor AU - Juhász, Gábor AU - Zvara, Ágnes AU - Muller, G AU - Lévay, György István AU - Hársing, László Gábor AU - Rajkó, Róbert AU - Penke, Botond AU - Janka, Zoltán AU - Janáky, Tamás AU - Puskás, László TI - Functional changes in transcriptomes of the prefrontal cortex and hippocampus in a mouse model of anxiety JF - PHARMACOLOGICAL REPORTS J2 - PHARMACOL REP VL - 63 PY - 2011 IS - 2 SP - 348 EP - 361 PG - 14 SN - 1734-1140 DO - 10.1016/S1734-1140(11)70501-1 UR - https://m2.mtmt.hu/api/publication/1627330 ID - 1627330 LA - English DB - MTMT ER - TY - CHAP AU - Kasza, Ágnes AU - Szegedi, Viktor AU - Juhász, Gábor AU - Frank, Zsuzsanna AU - Penke, Zsuzsa AU - Penke, Botond ED - Marija, Abramić ED - Zvonimir, Maksić ED - Branka, Salopek-Sondi ED - Sanja, Tomić ED - Robert, Vianello TI - ICV injected Aβ-peptide induces dysfunctions in hippocampus and in spatial memory: model for Alzheimer's disease T2 - The 5th Central European Conference "Chemistry towards Biology" PB - Ruder Boskovic Institute CY - Zagreb SN - 9789536690 PY - 2010 SP - 98 UR - https://m2.mtmt.hu/api/publication/1878910 ID - 1878910 LA - English DB - MTMT ER -