Leonov, Andrei

[["dc.bibliographiccitation.firstpage","779"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Acta Neuropathologica"],["dc.bibliographiccitation.lastpage","780"],["dc.bibliographiccitation.volume","127"],["dc.contributor.author","Levin, Johannes"],["dc.contributor.author","Schmidt, Felix"],["dc.contributor.author","Boehm, Cathrin"],["dc.contributor.author","Prix, Catharina"],["dc.contributor.author","Boetzel, Kai"],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Giese, Armin"],["dc.date.accessioned","2017-09-07T11:46:17Z"],["dc.date.available","2017-09-07T11:46:17Z"],["dc.date.issued","2014"],["dc.identifier.doi","10.1007/s00401-014-1265-3"],["dc.identifier.gro","3142137"],["dc.identifier.isi","000334426300011"],["dc.identifier.pmid","24615514"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12109"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4955"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Springer"],["dc.relation.eissn","1432-0533"],["dc.relation.issn","0001-6322"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","The oligomer modulator anle138b inhibits disease progression in a Parkinson mouse model even with treatment started after disease onset"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","letter_note"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","575"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Acta Neuropathologica"],["dc.bibliographiccitation.lastpage","595"],["dc.bibliographiccitation.volume","138"],["dc.contributor.author","Wegrzynowicz, Michal"],["dc.contributor.author","Bar-On, Dana"],["dc.contributor.author","Calo’, Laura"],["dc.contributor.author","Anichtchik, Oleg"],["dc.contributor.author","Iovino, Mariangela"],["dc.contributor.author","Xia, Jing"],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Giese, Armin"],["dc.contributor.author","Dalley, Jeffrey W."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Ashery, Uri"],["dc.contributor.author","Spillantini, Maria Grazia"],["dc.date.accessioned","2020-12-10T14:10:27Z"],["dc.date.available","2020-12-10T14:10:27Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1007/s00401-019-02023-x"],["dc.identifier.pmid","31165254"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16591"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/70765"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/28"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.workinggroup","RG Griesinger"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Depopulation of dense α-synuclein aggregates is associated with rescue of dopamine neuron dysfunction and death in a new Parkinson’s disease model"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Journal of Nuclear Medicine and Molecular Imaging"],["dc.contributor.author","Kuebler, Laura"],["dc.contributor.author","Buss, Sabrina"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Schmidt, Felix"],["dc.contributor.author","Maurer, Andreas"],["dc.contributor.author","Weckbecker, Daniel"],["dc.contributor.author","Landau, Anne M."],["dc.contributor.author","Lillethorup, Thea P."],["dc.contributor.author","Bleher, Daniel"],["dc.contributor.author","Saw, Ran Sing"],["dc.contributor.author","Pichler, Bernd J."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Giese, Armin"],["dc.contributor.author","Herfert, Kristina"],["dc.date.accessioned","2021-04-14T08:30:50Z"],["dc.date.available","2021-04-14T08:30:50Z"],["dc.date.issued","2020"],["dc.description.abstract","Purpose\r\n\r\nDeposition of misfolded alpha-synuclein (αSYN) aggregates in the human brain is one of the major hallmarks of synucleinopathies. However, a target-specific tracer to detect pathological aggregates of αSYN remains lacking. Here, we report the development of a positron emission tomography (PET) tracer based on anle138b, a compound shown to have therapeutic activity in animal models of neurodegenerative diseases.\r\nMethods\r\n\r\nSpecificity and selectivity of [3H]MODAG-001 were tested in in vitro binding assays using recombinant fibrils. After carbon-11 radiolabeling, the pharmacokinetic and metabolic profile was determined in mice. Specific binding was quantified in rats, inoculated with αSYN fibrils and using in vitro autoradiography in human brain sections of Lewy body dementia (LBD) cases provided by the Neurobiobank Munich (NBM).\r\nResults\r\n\r\n[3H]MODAG-001 revealed a very high affinity towards pure αSYN fibrils (Kd = 0.6 ± 0.1 nM) and only a moderate affinity to hTau46 fibrils (Kd = 19 ± 6.4 nM) as well as amyloid-β1–42 fibrils (Kd = 20 ± 10 nM). [11C]MODAG-001 showed an excellent ability to penetrate the mouse brain. Metabolic degradation was present, but the stability of the parent compound improved after selective deuteration of the precursor. (d3)-[11C]MODAG-001 binding was confirmed in fibril-inoculated rat striata using in vivo PET imaging. In vitro autoradiography showed no detectable binding to aggregated αSYN in human brain sections of LBD cases, most likely, because of the low abundance of aggregated αSYN against background protein.\r\nConclusion\r\n\r\nMODAG-001 provides a promising lead structure for future compound development as it combines a high affinity and good selectivity in fibril-binding assays with suitable pharmacokinetics and biodistribution properties."],["dc.identifier.doi","10.1007/s00259-020-05133-x"],["dc.identifier.pmid","33369690"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83387"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/101"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1619-7089"],["dc.relation.issn","1619-7070"],["dc.relation.workinggroup","RG Griesinger"],["dc.rights","CC BY 4.0"],["dc.title","[11C]MODAG-001—towards a PET tracer targeting α-synuclein aggregates"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","14893"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Jaipuria, Garima"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Vasa, Suresh Kumar"],["dc.contributor.author","Jaremko, Lukasz"],["dc.contributor.author","Jaremko, Mariusz"],["dc.contributor.author","Linser, Rasmus"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2018-11-07T10:26:01Z"],["dc.date.available","2018-11-07T10:26:01Z"],["dc.date.issued","2017"],["dc.description.abstract","Cholesterol is an important regulator of membrane protein function. However, the exact mechanisms involved in this process are still not fully understood. Here we study how the tertiary and quaternary structure of the mitochondrial translocator protein TSPO, which binds cholesterol with nanomolar affinity, is affected by this sterol. Residue-specific analysis of TSPO by solid-state NMR spectroscopy reveals a dynamic monomer-dimer equilibrium of TSPO in the membrane. Binding of cholesterol to TSPO's cholesterol-recognition motif leads to structural changes across the protein that shifts the dynamic equilibrium towards the translocator monomer. Consistent with an allosteric mechanism, a mutation within the oligomerization interface perturbs transmembrane regions located up to 35 angstrom away from the interface, reaching TSPO's cholesterol-binding motif. The lower structural stability of the intervening transmembrane regions provides a mechanistic basis for signal transmission. Our study thus reveals an allosteric signal pathway that connects membrane protein tertiary and quaternary structure with cholesterol binding."],["dc.identifier.doi","10.1038/ncomms14893"],["dc.identifier.isi","000397799000001"],["dc.identifier.pmid","28358007"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14416"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42959"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Cholesterol-mediated allosteric regulation of the mitochondrial translocator protein structure"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Bartels, Martin"],["dc.contributor.author","Weckbecker, Daniel"],["dc.contributor.author","Kuhn, Peer-Hendrik"],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Lichtenthaler, Stefan F."],["dc.contributor.author","Bötzel, Kai"],["dc.contributor.author","Giese, Armin"],["dc.date.accessioned","2020-12-10T18:10:13Z"],["dc.date.available","2020-12-10T18:10:13Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1038/s41598-019-45298-6"],["dc.identifier.eissn","2045-2322"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16341"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73892"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Iron-mediated aggregation and toxicity in a novel neuronal cell culture model with inducible alpha-synuclein expression"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","99"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","Frontiers in Neuroscience"],["dc.bibliographiccitation.lastpage","9"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Fellner, Lisa"],["dc.contributor.author","Kuzdas-Wood, Daniela"],["dc.contributor.author","Levin, Johannes"],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Giese, Armin"],["dc.contributor.author","Wenning, Gregor K."],["dc.contributor.author","Stefanova, Nadia"],["dc.date.accessioned","2017-09-07T11:54:34Z"],["dc.date.available","2017-09-07T11:54:34Z"],["dc.date.issued","2016"],["dc.description.abstract","The neurodegenerative disorder multiple system atrophy (MSA) is characterized by autonomic failure, cerebellar ataxia and parkinsonism in any combination associated with predominantly oligodendroglial alpha-synuclein (alpha-syn) aggregates (glial cytoplasmic inclusions = GCls). To date, there is no effective disease modifying therapy. Previous experiments have shown that the aggregation inhibitor anle138b reduces neurodegeneration, as well as behavioral deficits in both transgenic and toxin mouse models of Parkinson's disease (PD). Here we analyzed whether anle138b improves motor skills and reduces neuronal loss, as well as oligodendroglial alpha-syn aggregation in the PLP-alpha-syn transgenic mouse challenged with the mitochondria' toxin 3-nitropropionic acid (3-NP) to model full-blown MSA. Following 1 month of treatment with anle138b, MSA mice showed signs of motor improvement affecting stride length, but not pole, grip strength, and beam test performance. Loss of dopaminergic nigral neurons and Purkinje cells was not attenuated and GCI density remained unchanged. These data suggest that the pathology in transgenic PLP-alpha-syn mice receiving 3-NP might be too advanced to detect significant effects of anle138b treatment on neuronal loss and intracytoplasmic alpha-syn inclusion bodies. However, the partial motor amelioration may indicate potential efficacy of anle138b treatment that may be mediated by its actions on alpha-syn oligomers or may reflect improvement of neuronal dysfunction in neural at risk populations. Further studies are required to address the efficacy of anle138b in transgenic alpha-syn models of early-stage MSA and in the absence of additional toxin application."],["dc.identifier.doi","10.3389/fnins.2016.00099"],["dc.identifier.gro","3141710"],["dc.identifier.isi","000371761400001"],["dc.identifier.pmid","27013960"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13156"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/213"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1662-453X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Anle138b Partly Ameliorates Motor Deficits Despite Failure of Neuroprotection in a Model of Advanced Multiple System Atrophy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","32"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","EMBO molecular medicine"],["dc.bibliographiccitation.lastpage","47"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Martinez-Hernandez, Ana"],["dc.contributor.author","Urbanke, Hendrik"],["dc.contributor.author","Gillman, Alan L."],["dc.contributor.author","Lee, Joon"],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Agbemenyah, Hope Y."],["dc.contributor.author","Benito, Eva"],["dc.contributor.author","Jain, Gaurav"],["dc.contributor.author","Kaurani, Lalit"],["dc.contributor.author","Grigorian, Gayane"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Rezaei-Ghaleh, Nasrollah"],["dc.contributor.author","Wilken, Petra"],["dc.contributor.author","Teran Arce, Fernando"],["dc.contributor.author","Wagner, Jens"],["dc.contributor.author","Fuhrman, Martin"],["dc.contributor.author","Caruana, Mario"],["dc.contributor.author","Camilleri, Angelique"],["dc.contributor.author","Vassallo, Neville"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Benz, Roland"],["dc.contributor.author","Giese, Armin"],["dc.contributor.author","Schneider, Anja"],["dc.contributor.author","Korte, Martin"],["dc.contributor.author","Lal, Ratnesh"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Eichele, Gregor"],["dc.contributor.author","Fischer, Andre"],["dc.date.accessioned","2018-01-09T14:58:18Z"],["dc.date.available","2018-01-09T14:58:18Z"],["dc.date.issued","2017-12-05"],["dc.description.abstract","Alzheimer's disease is a devastating neurodegenerative disease eventually leading to dementia. An effective treatment does not yet exist. Here we show that oral application of the compound anle138b restores hippocampal synaptic and transcriptional plasticity as well as spatial memory in a mouse model for Alzheimer's disease, when given orally before or after the onset of pathology. At the mechanistic level, we provide evidence that anle138b blocks the activity of conducting Aβ pores without changing the membrane embedded Aβ-oligomer structure. In conclusion, our data suggest that anle138b is a novel and promising compound to treat AD-related pathology that should be investigated further."],["dc.identifier.doi","10.15252/emmm.201707825"],["dc.identifier.pmid","29208638"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15064"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11613"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","1757-4684"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The diphenylpyrazole compound anle138b blocks Aβ channels and rescues disease phenotypes in a mouse model for amyloid pathology"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Saravanan, Manikam S."],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Nicolai, Janine"],["dc.contributor.author","Praest, Patrique"],["dc.contributor.author","Giese, Armin"],["dc.contributor.author","Winter, Roland"],["dc.contributor.author","Khemtemourian, Lucie"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Killian, J. Antoinette"],["dc.date.accessioned","2020-12-10T18:11:10Z"],["dc.date.available","2020-12-10T18:11:10Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1038/s41598-019-54919-z"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17084"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73911"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/18"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.workinggroup","RG Griesinger"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The small molecule inhibitor anle145c thermodynamically traps human islet amyloid peptide in the form of non-cytotoxic oligomers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","795"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Acta Neuropathologica"],["dc.bibliographiccitation.lastpage","813"],["dc.bibliographiccitation.volume","125"],["dc.contributor.author","Wagner, J."],["dc.contributor.author","Ryazanov, S."],["dc.contributor.author","Leonov, A."],["dc.contributor.author","Levin, J."],["dc.contributor.author","Shi, S."],["dc.contributor.author","Schmidt, F."],["dc.contributor.author","Prix, C."],["dc.contributor.author","Pan-Montojo, F."],["dc.contributor.author","Bertsch, U."],["dc.contributor.author","Mitteregger-Kretzschmar, G."],["dc.contributor.author","Geissen, M."],["dc.contributor.author","Eiden, M."],["dc.contributor.author","Leidel, F."],["dc.contributor.author","Hirschberger, T."],["dc.contributor.author","Deeg, A. A."],["dc.contributor.author","Krauth, J. J."],["dc.contributor.author","Zinth, W."],["dc.contributor.author","Tavan, P."],["dc.contributor.author","Pilger, J."],["dc.contributor.author","Zweckstetter, M."],["dc.contributor.author","Frank, T."],["dc.contributor.author","Bähr, M."],["dc.contributor.author","Weishaupt, J. H."],["dc.contributor.author","Uhr, M."],["dc.contributor.author","Urlaub, H."],["dc.contributor.author","Teichmann, U."],["dc.contributor.author","Samwer, M."],["dc.contributor.author","Bötzel, K."],["dc.contributor.author","Groschup, M."],["dc.contributor.author","Kretzschmar, Hans"],["dc.contributor.author","Griesinger, C."],["dc.contributor.author","Giese, A."],["dc.date.accessioned","2017-09-07T11:47:41Z"],["dc.date.available","2017-09-07T11:47:41Z"],["dc.date.issued","2013"],["dc.description.abstract","In neurodegenerative diseases such as Alzheimer's disease (AD), Parkinson's disease (PD) and prion diseases, deposits of aggregated disease-specific proteins are found. Oligomeric aggregates are presumed to be the key neurotoxic agent. Here we describe the novel oligomer modulator anle138b [3-(1,3-benzodioxol-5-yl)-5-(3-bromophenyl)-1H-pyrazole], an aggregation inhibitor we developed based on a systematic high-throughput screening campaign combined with medicinal chemistry optimization. In vitro, anle138b blocked the formation of pathological aggregates of prion protein (PrPSc) and of alpha-synuclein (alpha-syn), which is deposited in PD and other synucleinopathies such as dementia with Lewy bodies (DLB) and multiple system atrophy (MSA). Notably, anle138b strongly inhibited all prion strains tested including BSE-derived and human prions. Anle138b showed structure-dependent binding to pathological aggregates and strongly inhibited formation of pathological oligomers in vitro and in vivo both for prion protein and alpha-synuclein. Both in mouse models of prion disease and in three different PD mouse models, anle138b strongly inhibited oligomer accumulation, neuronal degeneration, and disease progression in vivo. Anle138b had no detectable toxicity at therapeutic doses and an excellent oral bioavailability and blood-brain-barrier penetration. Our findings indicate that oligomer modulators provide a new approach for disease-modifying therapy in these diseases, for which only symptomatic treatment is available so far. Moreover, our findings suggest that pathological oligomers in neurodegenerative diseases share structural features, although the main protein component is disease-specific, indicating that compounds such as anle138b that modulate oligomer formation by targeting structure-dependent epitopes can have a broad spectrum of activity in the treatment of different protein aggregation diseases."],["dc.identifier.doi","10.1007/s00401-013-1114-9"],["dc.identifier.gro","3142347"],["dc.identifier.isi","000319357900002"],["dc.identifier.pmid","23604588"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10301"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7275"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0001-6322"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Anle138b: a novel oligomer modulator for disease-modifying therapy of neurodegenerative diseases such as prion and Parkinson's disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Dominguez-Meijide, Antonio"],["dc.contributor.author","Vasili, Eftychia"],["dc.contributor.author","König, Annekatrin"],["dc.contributor.author","Cima-Omori, Maria-Sol"],["dc.contributor.author","Ibáñez de Opakua, Alain"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Outeiro, Tiago F."],["dc.date.accessioned","2021-04-14T08:24:26Z"],["dc.date.available","2021-04-14T08:24:26Z"],["dc.date.issued","2020"],["dc.description.abstract","Parkinson's disease (PD) and Alzheimer's disease (AD) are common neurodegenerative disorders of the elderly and, therefore, affect a growing number of patients worldwide. Both diseases share, as a common hallmark, the accumulation of characteristic protein aggregates, known as Lewy bodies (LB) in PD, and neurofibrillary tangles in AD. LBs are primarily composed of misfolded α-synuclein (aSyn), and neurofibrillary tangles are primarily composed of tau protein. Importantly, upon pathological evaluation, most AD and PD/Lewy body dementia cases exhibit mixed pathology, with the co-occurrence of both LB and neurofibrillary tangles, among other protein inclusions. Recent studies suggest that both aSyn and tau pathology can spread and propagate through neuronal connections. Therefore, it is important to investigate the mechanisms underlying aggregation and propagation of these proteins for the development of novel therapeutic strategies. Here, we assessed the effects of different pharmacological interventions on the aggregation and internalization of tau and aSyn. We found that anle138b and fulvic acid decrease aSyn and tau aggregation, that epigallocatechin gallate decreases aSyn aggregation, and that dynasore reduces tau internalization. Establishing the effects of small molecules with different chemical properties on the aggregation and spreading of aSyn and tau will be important for the development of future therapeutic interventions."],["dc.identifier.doi","10.1038/s41598-020-69744-y"],["dc.identifier.pmid","32732936"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81282"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/167"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","2045-2322"],["dc.relation.workinggroup","RG Griesinger"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.rights","CC BY 4.0"],["dc.title","Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]