Ryazanov, Sergey

[["dc.bibliographiccitation.firstpage","E4971"],["dc.bibliographiccitation.issue","25"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","E4977"],["dc.bibliographiccitation.volume","114"],["dc.contributor.author","Turriani, Elisa"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Giese, Armin"],["dc.contributor.author","Schön, Margarete"],["dc.contributor.author","Schön, Michael P."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Arndt-Jovin, Donna J."],["dc.contributor.author","Becker, Dorothea"],["dc.date.accessioned","2018-04-23T11:47:36Z"],["dc.date.available","2018-04-23T11:47:36Z"],["dc.date.issued","2017"],["dc.description.abstract","Recent epidemiological and clinical studies have reported a significantly increased risk for melanoma in people with Parkinson’s disease. Because no evidence could be obtained that genetic factors are the reason for the association between these two diseases, we hypothesized that of the three major Parkinson’s disease-related proteins—α-synuclein, LRRK2, and Parkin—α-synuclein might be a major link. Our data, presented here, demonstrate that α-synuclein promotes the survival of primary and metastatic melanoma cells, which is the exact opposite of the effect that α-synuclein has on dopaminergic neurons, where its accumulation causes neuronal dysfunction and death. Because this detrimental effect of α-synuclein on neurons can be rescued by the small molecule anle138b, we explored its effect on melanoma cells. We found that treatment with anle138b leads to massive melanoma cell death due to a major dysregulation of autophagy, suggesting that α-synuclein is highly beneficial to advanced melanoma because it ensures that autophagy is maintained at a homeostatic level that promotes and ensures the cell’s survival."],["dc.identifier.doi","10.1073/pnas.1700200114"],["dc.identifier.gro","3142238"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13362"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0027-8424"],["dc.title","Treatment with diphenyl–pyrazole compound anle138b/c reveals that α-synuclein protects melanoma cells from autophagic cell death"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","S2352396422002055"],["dc.bibliographiccitation.firstpage","104021"],["dc.bibliographiccitation.journal","eBioMedicine"],["dc.bibliographiccitation.volume","80"],["dc.contributor.author","Levin, Johannes"],["dc.contributor.author","Sing, Nand"],["dc.contributor.author","Melbourne, Sue"],["dc.contributor.author","Morgan, Amber"],["dc.contributor.author","Mariner, Carla"],["dc.contributor.author","Spillantini, Maria Grazia"],["dc.contributor.author","Wegrzynowicz, Michal"],["dc.contributor.author","Dalley, Jeffrey W."],["dc.contributor.author","Langer, Simon"],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Giese, Armin"],["dc.date.accessioned","2022-06-01T09:40:14Z"],["dc.date.available","2022-06-01T09:40:14Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1016/j.ebiom.2022.104021"],["dc.identifier.pii","S2352396422002055"],["dc.identifier.pmid","35500536"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/108672"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/513"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-572"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.issn","2352-3964"],["dc.relation.workinggroup","RG Griesinger"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","Safety, tolerability and pharmacokinetics of the oligomer modulator anle138b with exposure levels sufficient for therapeutic efficacy in a murine Parkinson model: A randomised, double-blind, placebo-controlled phase 1a trial"],["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","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.firstpage","924"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Journal of Neuropathology and Experimental Neurology"],["dc.bibliographiccitation.lastpage","933"],["dc.bibliographiccitation.volume","74"],["dc.contributor.author","Shi, Song"],["dc.contributor.author","Wagner, Jens"],["dc.contributor.author","Mitteregger-Kretzschmar, Gerda"],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Giese, Armin"],["dc.date.accessioned","2017-09-07T11:43:35Z"],["dc.date.available","2017-09-07T11:43:35Z"],["dc.date.issued","2015"],["dc.description.abstract","Prion diseases are fatal neurodegenerative diseases characterized by accumulation of the pathogenic prion protein PrPSc in the brain. We established quantitative real-time quaking-induced conversion for the measurement of minute amounts of PrPSc in body fluids such as urine. Using this approach, we monitored the efficacy of antiprion therapy by quantifying the seeding activity of PrPSc from the brain and urine of mice after prion infection. We found that the aggregation inhibitor anle138b decreased the levels of PrPSc in the brain and urine. Importantly, variations of PrPSc levels in the urine closely corresponded to those in the brain. Our findings indicate that quantification of urinary PrPSc enables measurement of prion disease progression in body fluids and can substitute for immunodetection in brain tissue. We expect PrPSc quantification biologic fluids (such as urine and cerebrospinal fluid) with quantitative real-time quaking-induced conversion to emerge as a valuable noninvasive diagnostic tool for monitoring disease progression and the efficacy of therapeutic approaches in animal studies and human clinical trials of prion diseases. Moreover, highly sensitive methods for quantifying pathologic aggregate seeds might provide novel molecular biomarkers for other neurodegenerative diseases that may involve prion-like mechanisms (protein aggregation and spreading), such as Alzheimer disease and Parkinson disease."],["dc.identifier.doi","10.1097/NEN.0000000000000233"],["dc.identifier.gro","3141840"],["dc.identifier.isi","000360142900007"],["dc.identifier.pmid","26247395"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1656"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0022-3069"],["dc.title","Quantitative Real-Time Quaking-Induced Conversion Allows Monitoring of Disease-Modifying Therapy in the Urine of Prion-Infected Mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","800"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - General Subjects"],["dc.bibliographiccitation.lastpage","807"],["dc.bibliographiccitation.volume","1862"],["dc.contributor.author","Reiner, Anne M."],["dc.contributor.author","Schmidt, Felix"],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Weckbecker, Daniel"],["dc.contributor.author","Deeg, Andreas A."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Giese, Armin"],["dc.contributor.author","Zinth, Wolfgang"],["dc.date.accessioned","2018-01-17T11:27:13Z"],["dc.date.available","2018-01-17T11:27:13Z"],["dc.date.issued","2017"],["dc.description.abstract","Recently diphenyl-pyrazole (DPP) compounds and especially anle138b were found to reduce the aggregation of α-synuclein or Tau protein in vitro as well as in a mouse model of neurodegenerative diseases . Direct interaction of the DPPs with the fibrillar structure was identified by fluorescence spectroscopy. Thereby a strong dependence of the fluorescence on the surroundings could be identified ."],["dc.identifier.doi","10.1016/j.bbagen.2017.12.007"],["dc.identifier.pmid","29273222"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11675"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.title","Photophysics of diphenyl-pyrazole compounds in solutions and α-synuclein aggregates"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1884"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - General Subjects"],["dc.bibliographiccitation.lastpage","1890"],["dc.bibliographiccitation.volume","1850"],["dc.contributor.author","Deeg, Andreas A."],["dc.contributor.author","Reiner, Anne M."],["dc.contributor.author","Schmidt, Felix"],["dc.contributor.author","Schueder, Florian"],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Ruf, Viktoria C."],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Giese, Armin"],["dc.contributor.author","Zinth, Wolfgang"],["dc.date.accessioned","2017-09-07T11:43:35Z"],["dc.date.available","2017-09-07T11:43:35Z"],["dc.date.issued","2015"],["dc.description.abstract","Background: Special diphenyl-pyrazole compounds and in particular anle138b were found to reduce the progression of prion and Parkinson's disease in animal models. The therapeutic impact of these compounds was attributed to the modulation of a-synuclein and prion-protein aggregation related to these diseases. Methods: Photophysical and photochemical properties of the diphenyl-pyrazole compounds anle138b, anle186b and sery313b and their interaction with monomeric and aggregated a-synuclein were studied by fluorescence techniques. Results: The fluorescence emission of diphenyl-pyrazole is strongly increased upon incubation with a-synuclein fibrils, while no change in fluorescence emission is found when brought in contact with monomeric a-synuclein. This points to a distinct interaction between diphenyl-pyrazole and the fibrillar structure with a high binding affinity (K-d = 190 +/- 120 nM) for anle138b. Several a-synuclein proteins form a hydrophobic binding pocket for the diphenyl-pyrazole compound. A UV-induced dehalogenation reaction was observed for anle138b which is modulated by the hydrophobic environment of the fibrils. Conclusion: Fluorescence of the investigated diphenyl-pyrazole compounds strongly increases upon binding to fibrillar a-synuclein structures. Binding at high affinity occurs to hydrophobic pockets in the fibrils. General significance: The observed particular fluorescence properties of the diphenyl-pyrazole molecules open new possibilities for the investigation of the mode of action of these compounds in neurodegenerative diseases. The high binding affinity to aggregates and the strong increase in fluorescence upon binding make the compounds promising fluorescence markers for the analysis of aggregation-dependent epitopes. (C) 2015 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbagen.2015.05.021"],["dc.identifier.gro","3141841"],["dc.identifier.isi","000359173900026"],["dc.identifier.pmid","26028294"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1667"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1872-8006"],["dc.relation.issn","0304-4165"],["dc.title","Anle138b and related compounds are aggregation specific fluorescence markers and reveal high affinity binding to ot-synuclein aggregates"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["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.firstpage","560a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","114"],["dc.contributor.author","Antonschmidt, Leif"],["dc.contributor.author","Dervisoglu, Riza"],["dc.contributor.author","Ryazanov, Sergey"],["dc.contributor.author","Leonov, Andrei"],["dc.contributor.author","Wegstroth, Melanie"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Lee, Joon"],["dc.contributor.author","Lal, Ratneshwar"],["dc.contributor.author","Eichele, Gregor"],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2022-03-01T11:44:59Z"],["dc.date.available","2022-03-01T11:44:59Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.bpj.2017.11.3064"],["dc.identifier.pii","S0006349517342960"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103181"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0006-3495"],["dc.title","The Small Molecule anle138b Shows Interaction with α-Synuclein Oligomers in Phospholipid Membranes"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]