Riedel, Dietmar

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Strohäker, Timo"],["dc.contributor.author","Jung, Byung Chul"],["dc.contributor.author","Liou, Shu-Hao"],["dc.contributor.author","Fernandez, Claudio O."],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Halliday, Glenda M."],["dc.contributor.author","Bennati, Marina"],["dc.contributor.author","Kim, Woojin S."],["dc.contributor.author","Lee, Seung-Jae"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2020-12-10T18:09:52Z"],["dc.date.available","2020-12-10T18:09:52Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1038/s41467-019-13564-w"],["dc.identifier.eissn","2041-1723"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17027"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73784"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5046"],["dc.bibliographiccitation.issue","27"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","5048"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Kim, Hai-Young"],["dc.contributor.author","Cho, Min-Kyu"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Fernandez, Claudio O."],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2021-06-01T10:49:25Z"],["dc.date.available","2021-06-01T10:49:25Z"],["dc.date.issued","2008"],["dc.identifier.doi","10.1002/anie.200800342"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86282"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1521-3773"],["dc.relation.issn","1433-7851"],["dc.title","Dissociation of Amyloid Fibrils of α-Synuclein in Supercooled Water"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5017"],["dc.bibliographiccitation.issue","27"],["dc.bibliographiccitation.journal","Angewandte Chemie"],["dc.bibliographiccitation.lastpage","5017"],["dc.bibliographiccitation.volume","120"],["dc.contributor.author","Kim, Hai-Young"],["dc.contributor.author","Cho, Min-Kyu"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Fernandez, Claudio O."],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2021-12-08T12:30:02Z"],["dc.date.available","2021-12-08T12:30:02Z"],["dc.date.issued","2008"],["dc.identifier.doi","10.1002/ange.200890181"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/96298"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-476"],["dc.relation.eissn","1521-3757"],["dc.relation.issn","0044-8249"],["dc.rights.uri","http://doi.wiley.com/10.1002/tdm_license_1.1"],["dc.title","Titelbild: Dissociation of Amyloid Fibrils of α-Synuclein in Supercooled Water (Angew. Chem. 27/2008)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5124"],["dc.bibliographiccitation.issue","27"],["dc.bibliographiccitation.journal","Angewandte Chemie"],["dc.bibliographiccitation.lastpage","5126"],["dc.bibliographiccitation.volume","120"],["dc.contributor.author","Kim, Hai-Young"],["dc.contributor.author","Cho, Min-Kyu"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Fernandez, Claudio O."],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2021-12-08T12:30:00Z"],["dc.date.available","2021-12-08T12:30:00Z"],["dc.date.issued","2008"],["dc.identifier.doi","10.1002/ange.200800342"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/96287"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-476"],["dc.relation.eissn","1521-3757"],["dc.relation.issn","0044-8249"],["dc.rights.uri","http://doi.wiley.com/10.1002/tdm_license_1.1"],["dc.title","Dissociation of Amyloid Fibrils of α-Synuclein in Supercooled Water"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","Journal of Parkinson's Disease"],["dc.bibliographiccitation.lastpage","26"],["dc.contributor.author","Brás, Inês C."],["dc.contributor.author","Khani, Mohammad H."],["dc.contributor.author","Vasili, Eftychia"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Parfentev, Iwan"],["dc.contributor.author","Gerhardt, Ellen"],["dc.contributor.author","Fahlbusch, Christiane"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Outeiro, Tiago F."],["dc.date.accessioned","2022-11-01T10:17:15Z"],["dc.date.available","2022-11-01T10:17:15Z"],["dc.date.issued","2022"],["dc.description.abstract","Background: Various cellular pathways have been implicated in the transfer of disease-related proteins between cells, contributing to disease progression and neurodegeneration. However, the overall effects of protein transfer are still unclear. Objective: Here, we performed a systematic comparison of basic molecular mechanisms involved in the release of alpha-synuclein, Tau, and huntingtin, and evaluated functional effects upon internalization by receiving cells. Methods: Evaluation of protein release to the extracellular space in a free form and in extracellular vesicles using an optimized ultracentrifugation protocol. The extracellular effects of the proteins and extracellular vesicles in primary neuronal cultures were assessed using multi-channel electrophysiological recordings combined with a customized spike sorting framework. Results: We demonstrate cells differentially release free-forms of each protein to the extracellular space. Importantly, neuronal activity is distinctly modulated upon protein internalization in primary cortical cultures. In addition, these disease-related proteins also occur in extracellular vesicles, and are enriched in ectosomes. Internalization of ectosomes and exosomes by primary microglial or astrocytic cells elicits the production of pro-inflammatory cytokines, and modifies spontaneous electrical activity in neurons. Objective: Overall, our study demonstrates that released proteins can have detrimental effects for surrounding cells, and suggests protein release pathways may be exploited as therapeutic targets in different neurodegenerative diseases."],["dc.identifier.doi","10.3233/JPD-223516"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/116767"],["dc.notes.intern","DOI-Import GROB-605"],["dc.relation.eissn","1877-718X"],["dc.relation.issn","1877-7171"],["dc.title","Molecular Mechanisms Mediating the Transfer of Disease-Associated Proteins and Effects on Neuronal Activity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Ambadipudi, Susmitha"],["dc.contributor.author","Biernat, Jacek"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Mandelkow, Eckhard"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2019-07-09T11:43:48Z"],["dc.date.available","2019-07-09T11:43:48Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1038/s41467-017-00480-0"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14684"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58973"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3256"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","3268"],["dc.bibliographiccitation.volume","28"],["dc.contributor.author","Karpinar, Damla Pinar"],["dc.contributor.author","Balija, Madhu Babu Gajula"],["dc.contributor.author","Kügler, Sebastian"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Rezaei-Ghaleh, Nasrollah"],["dc.contributor.author","Wender, Nora"],["dc.contributor.author","Kim, Hai-Young"],["dc.contributor.author","Taschenberger, Grit"],["dc.contributor.author","Falkenburger, Bjoern H."],["dc.contributor.author","Heise, Henrike"],["dc.contributor.author","Kumar, Ashutosh"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Fichtner, Lars"],["dc.contributor.author","Voigt, Aaron"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Herzig, Alf"],["dc.contributor.author","Baldus, Marc"],["dc.contributor.author","Jaeckle, Herbert"],["dc.contributor.author","Eimer, Stefan"],["dc.contributor.author","Schulz, Joerg B."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2017-09-07T11:46:48Z"],["dc.date.available","2017-09-07T11:46:48Z"],["dc.date.issued","2009"],["dc.description.abstract","The relation of alpha-synuclein (alpha S) aggregation to Parkinson's disease (PD) has long been recognized, but the mechanism of toxicity, the pathogenic species and its molecular properties are yet to be identified. To obtain insight into the function different aggregated alpha S species have in neurotoxicity in vivo, we generated alpha S variants by a structure-based rational design. Biophysical analysis revealed that the alpha S mutants have a reduced fibrillization propensity, but form increased amounts of soluble oligomers. To assess their biological response in vivo, we studied the effects of the biophysically defined pre-fibrillar alpha S mutants after expression in tissue culture cells, in mammalian neurons and in PD model organisms, such as Caenorhabditis elegans and Drosophila melanogaster. The results show a striking correlation between alpha S aggregates with impaired beta-structure, neuronal toxicity and behavioural defects, and they establish a tight link between the biophysical properties of multimeric aS species and their in vivo function. The EMBO Journal (2009) 28, 3256-3268. doi:10.1038/emboj.2009.257; Published online 10 September 2009"],["dc.identifier.doi","10.1038/emboj.2009.257"],["dc.identifier.gro","3143038"],["dc.identifier.isi","000271008200017"],["dc.identifier.pmid","19745811"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/508"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.title","Pre‐fibrillar α‐synuclein variants with impaired β‐structure increase neurotoxicity in Parkinson's disease models"],["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","Nature Communications"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Cabrales Fontela, Yunior"],["dc.contributor.author","Kadavath, Harindranath"],["dc.contributor.author","Biernat, Jacek"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Mandelkow, Eckhard"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2020-12-10T18:09:44Z"],["dc.date.available","2020-12-10T18:09:44Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1038/s41467-017-02230-8"],["dc.identifier.eissn","2041-1723"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16721"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73745"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4939"],["dc.bibliographiccitation.issue","27"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","4939"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Kim, Hai-Young"],["dc.contributor.author","Cho, Min-Kyu"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Fernandez, Claudio O."],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2021-12-08T12:30:17Z"],["dc.date.available","2021-12-08T12:30:17Z"],["dc.date.issued","2008"],["dc.identifier.doi","10.1002/anie.200890127"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/96387"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-476"],["dc.relation.eissn","1521-3773"],["dc.relation.issn","1433-7851"],["dc.rights.uri","http://doi.wiley.com/10.1002/tdm_license_1.1"],["dc.title","Cover Picture: Dissociation of Amyloid Fibrils of α-Synuclein in Supercooled Water (Angew. Chem. Int. Ed. 27/2008)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2994"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","3002"],["dc.bibliographiccitation.volume","288"],["dc.contributor.author","Skora, Lukasz"],["dc.contributor.author","Fonseca-Ornelas, Luis"],["dc.contributor.author","Hofele, Romina V."],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Watzlawik, Jens"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2018-11-07T09:28:39Z"],["dc.date.available","2018-11-07T09:28:39Z"],["dc.date.issued","2013"],["dc.description.abstract","Misfolding of the natively alpha-helical prion protein into a beta-sheet rich isoform is related to various human diseases such as Creutzfeldt-Jakob disease and Gerstmann-Straussler-Scheinker syndrome. In humans, the disease phenotype is modified by a methionine/valine polymorphism at codon 129 of the prion protein gene. Using a combination of hydrogen/deuterium exchange coupled to NMR spectroscopy, hydroxyl radical probing detected by mass spectrometry, and site-directed mutagenesis, we demonstrate that stop mutants of the human prion protein have a conserved amyloid core. The 129 residue is deeply buried in the amyloid core structure, and its mutation strongly impacts aggregation. Taken together the data support a critical role of the polymorphic residue 129 of the human prion protein in aggregation and disease."],["dc.identifier.doi","10.1074/jbc.M112.423715"],["dc.identifier.isi","000314397900010"],["dc.identifier.pmid","23209282"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30832"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","0021-9258"],["dc.title","Burial of the Polymorphic Residue 129 in Amyloid Fibrils of Prion Stop Mutants"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]