Griesinger, Christian

[["dc.bibliographiccitation.firstpage","17968"],["dc.bibliographiccitation.issue","51"],["dc.bibliographiccitation.journal","Journal of the American Chemical Society"],["dc.bibliographiccitation.lastpage","17969"],["dc.bibliographiccitation.volume","127"],["dc.contributor.author","Bernado, Pau"],["dc.contributor.author","Bertoncini, Carlos W."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Blackledge, Martin"],["dc.date.accessioned","2017-09-07T11:53:35Z"],["dc.date.available","2017-09-07T11:53:35Z"],["dc.date.issued","2005"],["dc.identifier.doi","10.1021/ja055538p"],["dc.identifier.gro","3143768"],["dc.identifier.isi","000234258700002"],["dc.identifier.pmid","16366524"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1318"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0002-7863"],["dc.title","Defining long-range order and local disorder in native alpha-synuclein using residual dipolar couplings"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","21057"],["dc.bibliographiccitation.issue","50"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","21062"],["dc.bibliographiccitation.volume","106"],["dc.contributor.author","Lamberto, Gonzalo R."],["dc.contributor.author","Binolfi, Andres"],["dc.contributor.author","Orcellet, Maria L."],["dc.contributor.author","Bertoncini, Carlos W."],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Fernandez, Claudio O."],["dc.date.accessioned","2017-09-07T11:46:44Z"],["dc.date.available","2017-09-07T11:46:44Z"],["dc.date.issued","2009"],["dc.description.abstract","The identification of aggregation inhibitors and the investigation of their mechanism of action are fundamental in the quest to mitigate the pathological consequences of amyloid formation. Here, characterization of the structural and mechanistic basis for the antiamyloidogenic effect of phthalocyanine tetrasulfonate (PcTS) on alpha-synuclein (AS) allowed us to demonstrate that specific aromatic interactions are central for ligand-mediated inhibition of amyloid formation. We provide evidence indicating that the mechanism behind the antiamyloidogenic effect of PcTS is correlated with the trapping of prefibrillar AS species during the early stages of the assembly process. By using NMR spectroscopy, we have located the primary binding region for PcTS to a specific site in the N terminus of AS, involving the amino acid Tyr-39 as the anchoring residue. Moreover, the residue-specific structural characterization of the AS-PcTS complex provided the basis for the rational design of nonamyloidogenic species of AS, highlighting the role of aromatic interactions in driving AS amyloid assembly. A comparative analysis with other proteins involved in neurodegenerative disorders reveals that aromatic recognition interfaces might constitute a key structural element to target their aggregation pathways. These findings emphasize the use of aggregation inhibitors as molecular probes to assess structural and toxic mechanisms related to amyloid formation and the potential of small molecules as therapeutics for amyloid-related pathologies."],["dc.identifier.doi","10.1073/pnas.0902603106"],["dc.identifier.gro","3143010"],["dc.identifier.isi","000272795300011"],["dc.identifier.pmid","19948969"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/477"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Structural and mechanistic basis behind the inhibitory interaction of PcTS on alpha-synuclein amyloid fibril formation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5235"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Journal of the American Chemical Society"],["dc.bibliographiccitation.lastpage","5243"],["dc.bibliographiccitation.volume","129"],["dc.contributor.author","Mukrasch, Marco D."],["dc.contributor.author","Markwick, Phineus"],["dc.contributor.author","Biernat, Jacek"],["dc.contributor.author","von Bergen, Martin"],["dc.contributor.author","Bernado, Pau"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Mandelkow, Eckhard"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Blackledge, Martin"],["dc.date.accessioned","2017-09-07T11:49:48Z"],["dc.date.available","2017-09-07T11:49:48Z"],["dc.date.issued","2007"],["dc.description.abstract","Tau, a natively unstructured protein that regulates the organization of neuronal microtubules, is also found in high concentrations in neurofibrillary tangles of Alzheimer's disease and other neurodegenerative disorders. The conformational transition between these vastly different healthy and pathological forms remains poorly understood. We have measured residual dipolar couplings (RDCs), J-couplings, and nuclear Overhauser enhancement (NOE) in construct K18 of tau, containing all four repeat domains R1-R4. NHN RDCs were compared with prediction on the basis of a statistical model describing the intrinsic conformational sampling of unfolded proteins in solution. While local variation and relative amplitude of RDCs agrees with propensity-based prediction for most of the protein, homologous sequences in each repeat domain (DLKN, DLSN, DLSK, and DKFD in repeats R1-R4) show strong disagreement characterized by inversion of the sign of the central couplings. Accelerated molecular dynamic simulations (AMD) in explicit solvent revealed strong tendencies to form turns, identified as type I beta-turns for repeats R1-R3. Incorporation of the backbone dihedral sampling resulting from AMD into the statistical coil model closely reproduces experimental RDC values. These localized sequence-dependent conformational tendencies interrupt the propensity to sample more extended conformations in adjacent strands and are remarkably resistant to local environmental factors, as demonstrated by the persistence of the RDC signature even under harsh denaturing conditions (8 M urea). The role that this specific conformational behavior may play in the transition to the pathological form is discussed."],["dc.identifier.doi","10.1021/ja0690159"],["dc.identifier.gro","3143509"],["dc.identifier.isi","000245782800062"],["dc.identifier.pmid","17385861"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1031"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0002-7863"],["dc.title","Highly populated turn conformations in natively unfolded Tau protein identified from residual dipolar couplings and molecular simulation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1430"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","1435"],["dc.bibliographiccitation.volume","102"],["dc.contributor.author","Bertoncini, Carlos W."],["dc.contributor.author","Jung, Y. S."],["dc.contributor.author","Fernandez, Claudio O."],["dc.contributor.author","Hoyer, W."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Jovin, Thomas M."],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2017-09-07T11:43:01Z"],["dc.date.available","2017-09-07T11:43:01Z"],["dc.date.issued","2005"],["dc.description.abstract","In idiopathic Parkinson's disease, intracytoplasmic neuronal inclusions (Lewy bodies) containing aggregates of the protein a-synuclein (alphaS) are deposited in the pigmented nuclei of the brainstem. The mechanisms underlying the structural transition of innocuous, presumably natively unfolded, aS to neurotoxic forms are largely unknown. Using paramagnetic relaxation enhancement and NMR dipolar couplings, we show that monomeric aS assumes conformations that are stabilized by long-range interactions and act to inhibit oligomerization and aggregation. The autoinhibitory conformations fluctuate in the range of nanoseconds to microseconds corresponding to the time scale of secondary structure formation during folding. Polyamine binding and/or temperature increase, conditions that induce aggregation in vitro, release this inherent tertiary structure, leading to a completely unfolded conformation that associates readily. Stabilization of the native, autoinhibitory structure of alphaS constitutes a potential strategy for reducing or inhibiting oligomerization and aggregation in Parkinson's disease."],["dc.identifier.doi","10.1073/pnas.0407146102"],["dc.identifier.gro","3143902"],["dc.identifier.isi","000226877300034"],["dc.identifier.pmid","15671169"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1467"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","512"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","523"],["dc.bibliographiccitation.volume","377"],["dc.contributor.author","Sevvana, Madhumati"],["dc.contributor.author","Vijayan, Vinesh"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Reinelt, Stefan"],["dc.contributor.author","Madden, Dean R."],["dc.contributor.author","Herbst-Irmer, Regine"],["dc.contributor.author","Sheldrick, George M."],["dc.contributor.author","Bott, Michael"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Becker, Stefan"],["dc.date.accessioned","2017-09-07T11:48:46Z"],["dc.date.available","2017-09-07T11:48:46Z"],["dc.date.issued","2008"],["dc.description.abstract","Sensor histidine kinases of two-component signal-transduction systems are essential for bacteria to adapt to variable environmental conditions. However, despite their prevalence, it is not well understood how extracellular signals such as ligand binding regulate the activity of these sensor kinases. CitA is the sensor histidine kinase in Klebsiella pneumoniae that regulates the transport and anaerobic metabolism of citrate in response to its extracellular concentration. We report here the X-ray structures of the periplasmic sensor domain of CitA in the citrate-free and citrate-bound states. A comparison of the two structures shows that ligand binding causes a considerable contraction of the sensor domain. This contraction may represent the molecular switch that activates transmembrane signaling in the receptor. (C) 2008 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.jmb.2008.01.024"],["dc.identifier.gro","3143331"],["dc.identifier.isi","000254586100018"],["dc.identifier.pmid","18258261"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/833"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Academic Press Ltd- Elsevier Science Ltd"],["dc.relation.issn","0022-2836"],["dc.title","A ligand-induced switch in the periplasmic domain of sensor histidine kinase CitA"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","11520"],["dc.bibliographiccitation.issue","48"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","11524"],["dc.bibliographiccitation.volume","50"],["dc.contributor.author","Bibow, Stefan"],["dc.contributor.author","Mukrasch, Marco D."],["dc.contributor.author","Chinnathambi, Subashchandrabose"],["dc.contributor.author","Biernat, Jacek"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Mandelkow, Eckhard"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2017-09-07T11:45:04Z"],["dc.date.available","2017-09-07T11:45:04Z"],["dc.date.issued","2011"],["dc.identifier.doi","10.1002/anie.201105493"],["dc.identifier.gro","3142795"],["dc.identifier.isi","000297863900044"],["dc.identifier.pmid","21990182"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/239"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Max Planck Society; DFG [71/2-2, 3-2, 7-1]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","1433-7851"],["dc.title","The Dynamic Structure of Filamentous Tau"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1000034"],["dc.bibliographiccitation.firstpage","399"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","PLoS Biology"],["dc.bibliographiccitation.lastpage","414"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Mukrasch, Marco D."],["dc.contributor.author","Bibow, Stefan"],["dc.contributor.author","Korukottu, Jegannath"],["dc.contributor.author","Jeganathan, Sadasivam"],["dc.contributor.author","Biernat, Jacek"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Mandelkow, Eckhard"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2017-09-07T11:47:34Z"],["dc.date.available","2017-09-07T11:47:34Z"],["dc.date.issued","2009"],["dc.description.abstract","Alzheimer disease is characterized by abnormal protein deposits in the brain, such as extracellular amyloid plaques and intracellular neurofibrillary tangles. The tangles are made of a protein called tau comprising 441 residues in its longest isoform. Tau belongs to the class of natively unfolded proteins, binds to and stabilizes microtubules, and partially folds into an ordered beta-structure during aggregation to Alzheimer paired helical filaments (PHFs). Here we show that it is possible to overcome the size limitations that have traditionally hampered detailed nuclear magnetic resonance (NMR) spectroscopy studies of such large nonglobular proteins. This is achieved using optimal NMR pulse sequences and matching of chemical shifts from smaller segments in a divide and conquer strategy. The methodology reveals that 441-residue tau is highly dynamic in solution with a distinct domain character and an intricate network of transient long-range contacts important for pathogenic aggregation. Moreover, the single-residue view provided by the NMR analysis reveals unique insights into the interaction of tau with microtubules. Our results establish that NMR spectroscopy can provide detailed insight into the structural polymorphism of very large nonglobular proteins."],["dc.identifier.doi","10.1371/journal.pbio.1000034"],["dc.identifier.gro","3143159"],["dc.identifier.isi","000263599900018"],["dc.identifier.pmid","19226187"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8445"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/642"],["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","Public Library Science"],["dc.relation.issn","1544-9173"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Structural Polymorphism of 441-Residue Tau at Single Residue Resolution"],["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","6444"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Journal of the American Chemical Society"],["dc.bibliographiccitation.lastpage","6447"],["dc.bibliographiccitation.volume","137"],["dc.contributor.author","Miotto, Marco C."],["dc.contributor.author","Valiente-Gabioud, Ariel A."],["dc.contributor.author","Rossetti, Giulia"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Carloni, Paolo"],["dc.contributor.author","Selenko, Philipp"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Binolfi, Andres"],["dc.contributor.author","Fernandez, Claudio O."],["dc.date.accessioned","2017-09-07T11:44:23Z"],["dc.date.available","2017-09-07T11:44:23Z"],["dc.date.issued","2015"],["dc.description.abstract","Growing evidence supports a link between brain copper homeostasis; the formation of alpha-synuclein (AS)-copper complexes, and the development of Parkinson disease (PD). Recently it was demonstrated that the physiological form of AS is N-terminally acetylated (AcAS). Here we used NMR spectroscopy to structurally characterize the interaction between Cu(I) and AcAS. We found that the formation of an AcAS Cu(I) complex at the N-terminal region stabilizes local conformations with alpha-helical secondary structure and restricted motility. Our work provides new evidence into the metallo-biology of PD and opens new lines of research as the formation of AcAS Cu(I) complex might impact on AcAS Membrane binding and aggregation."],["dc.identifier.doi","10.1021/jacs.5b01911"],["dc.identifier.gro","3141896"],["dc.identifier.isi","000355383500006"],["dc.identifier.pmid","25939020"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2278"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0002-7863"],["dc.title","Copper Binding to the N-Terminally Acetylated, Naturally Occurring Form of Alpha-Synuclein Induces Local Helical Folding"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e24701"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Balija, Madhu Babu Gajula"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Herzig, Alf"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Jaeckle, Herbert"],["dc.date.accessioned","2017-09-07T11:43:24Z"],["dc.date.available","2017-09-07T11:43:24Z"],["dc.date.issued","2011"],["dc.description.abstract","Parkinson's disease (PD) is linked to the formation of insoluble fibrillar aggregates of the presynaptic protein alpha-Synuclein (alpha S) in neurons. The appearance of such aggregates coincides with severe motor deficits in human patients. These deficits are often preceded by non-motor symptoms such as sleep-related problems in the patients. PD-like motor deficits can be recapitulated in model organisms such as Drosophila melanogaster when alpha S is pan-neurally expressed. Interestingly, both these deficits are more severe when alpha S mutants with reduced aggregation properties are expressed in flies. This indicates that that alpha S aggregation is not the primary cause of the PD-like motor symptoms. Here we describe a model for PD in Drosophila which utilizes the targeted expression of alpha S mutants in a subset of dopadecarboxylase expressing serotonergic and dopaminergic (DA) neurons. Our results show that targeted expression of pre-fibrillar alpha S mutants not only recapitulates PD-like motor symptoms but also the preceding non-motor symptoms such as an abnormal sleep-like behavior, altered locomotor activity and abnormal circadian periodicity. Further, the results suggest that the observed non-motor symptoms in flies are caused by an early impairment of neuronal functions rather than by the loss of neurons due to cell death."],["dc.identifier.doi","10.1371/journal.pone.0024701"],["dc.identifier.gro","3142669"],["dc.identifier.isi","000294802800085"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/98"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Max-Planck-Society"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.title","Pre-Fibrillar alpha-Synuclein Mutants Cause Parkinson's Disease-Like Non-Motor Symptoms in Drosophila"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","32036"],["dc.bibliographiccitation.issue","37"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","32044"],["dc.bibliographiccitation.volume","286"],["dc.contributor.author","Lamberto, Gonzalo R."],["dc.contributor.author","Torres-Monserrat, Valentina"],["dc.contributor.author","Bertoncini, Carlos W."],["dc.contributor.author","Salvatella, Xavier"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Fernandez, Claudio O."],["dc.date.accessioned","2017-09-07T11:43:24Z"],["dc.date.available","2017-09-07T11:43:24Z"],["dc.date.issued","2011"],["dc.description.abstract","The fibrillation of amyloidogenic proteins is a critical step in the etiology of neurodegenerative disorders such as Alzheimer and Parkinson diseases. There is major interest in the therapeutic intervention on such aberrant aggregation phenomena, and the utilization of polyaromatic scaffolds has lately received considerable attention. In this regard, the molecular and structural basis of the anti-amyloidogenicity of polyaromatic compounds, required to evolve this molecular scaffold toward therapeutic drugs, is not known in detail. We present here biophysical and biochemical studies that have enabled us to characterize the interaction of metal-substituted, tetrasulfonated phthalocyanines (PcTS) with alpha-synuclein (AS), the major protein component of amyloid-like deposits in Parkinson disease. The inhibitory activity of the assayed compounds on AS amyloid fibril formation decreases in the order PcTS[Ni(II)] similar to PcTS > PcTS[Zn(II)] >> PcTS[Al(III)] approximate to 0. Using NMR and electronic absorption spectroscopies we demonstrated conclusively that the differences in binding capacity and anti-amyloid activity of phthalocyanines on AS are attributed to their relative ability to self-stack through pi-pi interactions, modulated by the nature of the metal ion bound at the molecule. Low order stacked aggregates of phthalocyanines were identified as the active amyloid inhibitory species, whose effects are mediated by residue specific interactions. Such sequence-specific anti-amyloid behavior of self-stacked phthalocyanines contrasts strongly with promiscuous amyloid inhibitors with self-association capabilities that act via nonspecific sequestration of AS molecules. The new findings reported here constitute an important contribution for future drug discovery efforts targeting amyloid formation."],["dc.identifier.doi","10.1074/jbc.M111.242958"],["dc.identifier.gro","3142668"],["dc.identifier.isi","000294726800013"],["dc.identifier.pmid","21795682"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/97"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.eissn","1083-351X"],["dc.relation.issn","0021-9258"],["dc.title","Toward the Discovery of Effective Polycyclic Inhibitors of alpha-Synuclein Amyloid Assembly"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]