Zweckstetter, Markus

[["dc.bibliographiccitation.artnumber","e2001336"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","PLoS Biology"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Baker, Jeremy D."],["dc.contributor.author","Shelton, Lindsey B."],["dc.contributor.author","Zheng, Dali"],["dc.contributor.author","Favretto, Filippo"],["dc.contributor.author","Nordhues, Bryce A."],["dc.contributor.author","Darling, April"],["dc.contributor.author","Sullivan, Leia E."],["dc.contributor.author","Sun, Zheying"],["dc.contributor.author","Solanki, Parth K."],["dc.contributor.author","Martin, Mackenzie D."],["dc.contributor.author","Suntharalingam, Amirthaa"],["dc.contributor.author","Sabbagh, Jonathan J."],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Mandelkow, Eckhard"],["dc.contributor.author","Uversky, Vladimir N."],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Dickey, Chad A."],["dc.contributor.author","Koren, John, III"],["dc.contributor.author","Blair, Laura J."],["dc.date.accessioned","2018-11-07T10:22:54Z"],["dc.date.available","2018-11-07T10:22:54Z"],["dc.date.issued","2017"],["dc.description.abstract","The accumulation of amyloidogenic proteins is a pathological hallmark of neurodegenerative disorders. The aberrant accumulation of the microtubule associating protein tau (MAPT, tau) into toxic oligomers and amyloid deposits is a primary pathology in tauopathies, the most common of which is Alzheimer's disease (AD). Intrinsically disordered proteins, like tau, are enriched with proline residues that regulate both secondary structure and aggregation propensity. The orientation of proline residues is regulated by cis/trans peptidyl-prolyl isomerases (PPIases). Here we show that cyclophilin 40 (CyP40), a PPIase, dissolves tau amyloids in vitro. Additionally, CyP40 ameliorated silver-positive and oligomeric tau species in a mouse model of tau accumulation, preserving neuronal health and cognition. Nuclear magnetic resonance (NMR) revealed that CyP40 interacts with tau at sites rich in proline residues. CyP40 was also able to interact with and disaggregate other aggregating proteins that contain prolines. Moreover, CyP40 lacking PPIase activity prevented its capacity for disaggregation in vitro. Finally, we describe a unique structural property of CyP40 that may permit disaggregation to occur in an energy-independent manner. This study identifies a novel human protein disaggregase and, for the first time, demonstrates its capacity to dissolve intracellular amyloids."],["dc.identifier.doi","10.1371/journal.pbio.2001336"],["dc.identifier.isi","000404510400007"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14553"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42356"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Public Library Science"],["dc.relation.issn","1545-7885"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Human cyclophilin 40 unravels neurotoxic amyloids"],["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.firstpage","3246"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","3250"],["dc.bibliographiccitation.volume","57"],["dc.contributor.author","Kadavath, Harindranath"],["dc.contributor.author","Cabrales Fontela, Yunior"],["dc.contributor.author","Jaremko, Mariusz"],["dc.contributor.author","Jaremko, Łukasz"],["dc.contributor.author","Overkamp, Kerstin"],["dc.contributor.author","Biernat, Jacek"],["dc.contributor.author","Mandelkow, Eckhard"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2020-12-10T14:08:44Z"],["dc.date.available","2020-12-10T14:08:44Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1002/anie.201712089"],["dc.identifier.issn","1433-7851"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/70538"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The Binding Mode of a Tau Peptide with Tubulin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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","10347"],["dc.bibliographiccitation.issue","35"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","10351"],["dc.bibliographiccitation.volume","54"],["dc.contributor.author","Kadavath, Harindranath"],["dc.contributor.author","Jaremko, Mariusz"],["dc.contributor.author","Jaremko, Lukasz"],["dc.contributor.author","Biernat, Jacek"],["dc.contributor.author","Mandelkow, Eckhard"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2018-11-07T09:53:09Z"],["dc.date.available","2018-11-07T09:53:09Z"],["dc.date.issued","2015"],["dc.description.abstract","Microtubules are regulated by microtubule-associated proteins. However, little is known about the structure of microtubule-associated proteins in complex with microtubules. Herein we show that the microtubule-associated protein Tau, which is intrinsically disordered in solution, locally folds into a stable structure upon binding to microtubules. While Tau is highly flexible in solution and adopts a beta-sheet structure in amyloid fibrils, in complex with microtubules the conserved hexapeptides at the beginning of the Tau repeats two and three convert into a hairpin conformation. Thus, binding to microtubules stabilizes a unique conformation in Tau."],["dc.identifier.doi","10.1002/ange.201501714"],["dc.identifier.isi","000360216800054"],["dc.identifier.pmid","26094605"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36274"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","1521-3773"],["dc.relation.issn","1433-7851"],["dc.title","Folding of the Tau Protein on Microtubules"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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.artnumber","2909"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Ukmar-Godec, Tina"],["dc.contributor.author","Hutten, Saskia"],["dc.contributor.author","Grieshop, Matthew P."],["dc.contributor.author","Rezaei-Ghaleh, Nasrollah"],["dc.contributor.author","Cima-Omori, Maria-Sol"],["dc.contributor.author","Biernat, Jacek"],["dc.contributor.author","Mandelkow, Eckhard"],["dc.contributor.author","Söding, Johannes"],["dc.contributor.author","Dormann, Dorothee"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2019-07-22T12:49:00Z"],["dc.date.available","2019-07-22T12:49:00Z"],["dc.date.issued","2019-07-02"],["dc.description.abstract","Cells form and use biomolecular condensates to execute biochemical reactions. The molecular properties of non-membrane-bound condensates are directly connected to the amino acid content of disordered protein regions. Lysine plays an important role in cellular function, but little is known about its role in biomolecular condensation. Here we show that protein disorder is abundant in protein/RNA granules and lysine is enriched in disordered regions of proteins in P-bodies compared to the entire human disordered proteome. Lysine-rich polypeptides phase separate into lysine/RNA-coacervates that are more dynamic and differ at the molecular level from arginine/RNA-coacervates. Consistent with the ability of lysine to drive phase separation, lysine-rich variants of the Alzheimer's disease-linked protein tau undergo coacervation with RNA in vitro and bind to stress granules in cells. Acetylation of lysine reverses liquid-liquid phase separation and reduces colocalization of tau with stress granules. Our study establishes lysine as an important regulator of cellular condensation."],["dc.identifier.doi","10.1038/s41467-019-10792-y"],["dc.identifier.pmid","31266957"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16293"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61798"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.eissn","2041-1723"],["dc.relation.issn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Lysine/RNA-interactions drive and regulate biomolecular condensation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","963"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","974"],["dc.bibliographiccitation.volume","156"],["dc.contributor.author","Karagoz, G. Elif"],["dc.contributor.author","Duarte, Afonso M. S."],["dc.contributor.author","Akoury, Elias"],["dc.contributor.author","Ippel, Hans"],["dc.contributor.author","Biernat, Jacek"],["dc.contributor.author","Luengo, Tania Moran"],["dc.contributor.author","Radli, Martina"],["dc.contributor.author","Didenko, Tatiana"],["dc.contributor.author","Nordhues, Bryce A."],["dc.contributor.author","Veprintsev, Dmitry B."],["dc.contributor.author","Dickey, Chad A."],["dc.contributor.author","Mandelkow, Eckhard"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Boelens, Rolf"],["dc.contributor.author","Madl, Tobias"],["dc.contributor.author","Rudiger, Stefan G. D."],["dc.date.accessioned","2018-11-07T09:43:36Z"],["dc.date.available","2018-11-07T09:43:36Z"],["dc.date.issued","2014"],["dc.description.abstract","Protein folding in the cell relies on the orchestrated action of conserved families of molecular chaperones, the Hsp70 and Hsp90 systems. Hsp70 acts early and Hsp90 late in the folding path, yet the molecular basis of this timing is enigmatic, mainly because the substrate specificity of Hsp90 is poorly understood. Here, we obtained a structural model of Hsp90 in complex with its natural disease-associated substrate, the intrinsically disordered Tau protein. Hsp90 binds to a broad region in Tau that includes the aggregation-prone repeats. Complementarily, a 106-angstrom-long substrate-binding interface in Hsp90 enables many low-affinity contacts. This allows recognition of scattered hydrophobic residues in late folding intermediates that remain after early burial of the Hsp70 sites. Our model resolves the paradox of how Hsp90 specifically selects for late folding intermediates but also for some intrinsically disordered proteins-through the eyes of Hsp90 they look the same."],["dc.identifier.doi","10.1016/j.cell.2014.01.037"],["dc.identifier.isi","000332083900014"],["dc.identifier.pmid","24581495"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34217"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1097-4172"],["dc.relation.issn","0092-8674"],["dc.title","Hsp90-Tau Complex Reveals Molecular Basis for Specificity in Chaperone Action"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","12230"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","12239"],["dc.bibliographiccitation.volume","282"],["dc.contributor.author","Mukrasch, Marco D."],["dc.contributor.author","von Bergen, Martin"],["dc.contributor.author","Biernat, Jacek"],["dc.contributor.author","Fischer, Daniela"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Mandelkow, Eckhard"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2017-09-07T11:49:48Z"],["dc.date.available","2017-09-07T11:49:48Z"],["dc.date.issued","2007"],["dc.description.abstract","Tau is the major microtubule-associated protein in neuronal axons. It aggregates into \"neurofibrillary tangles\" during the course of Alzheimer disease. Binding to microtubules and microtubule assembly requires the \"repeat domain\" in the C-terminal half of Tau, as well as the two regions flanking the repeats. Here we report the NMR characterization of a 198-residue Tau fragment composed of the four tandem repeats and the flanking domains and containing the full microtubule binding and assembly activity of Tau. NMR secondary chemical shifts and dipolar couplings detect the highest propensity for beta-structure within the four-repeat region, whereas the flanking domains are largely random coil, with an increased rigidity in the proline-rich region. Chemical shift perturbation experiments identify two motifs in the upstream flanking domain, (225)KVAVVRT(231) and (243)LQTA(246), and one downstream of the repeats, (KIETHKTFREN380)-K-370, which strongly contribute to the binding to the acidic outside of microtubules, as well as to the binding of other polyanions such as heparin. This is consistent with the \"jaws\" model of Tau-microtubule interactions and highlights the importance of the regions flanking the repeats for both microtubule binding and pathological Tau aggregation."],["dc.identifier.doi","10.1074/jbc.M607159200"],["dc.identifier.gro","3143510"],["dc.identifier.isi","000245941900066"],["dc.identifier.pmid","17307736"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1032"],["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.issn","0021-9258"],["dc.title","The \"jaws\" of the Tau-microtubule interaction"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","10841"],["dc.bibliographiccitation.issue","41"],["dc.bibliographiccitation.journal","Biochemistry"],["dc.bibliographiccitation.lastpage","10851"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Soragni, Alice"],["dc.contributor.author","Zambelli, Barbara"],["dc.contributor.author","Mukrasch, Marco D."],["dc.contributor.author","Biemat, Jacek"],["dc.contributor.author","Jeganathan, Sadasivam"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Ciurli, Stefano"],["dc.contributor.author","Mandelkow, Eckhard"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2017-09-07T11:48:11Z"],["dc.date.available","2017-09-07T11:48:11Z"],["dc.date.issued","2008"],["dc.description.abstract","Transition metals have been frequently recognized as risk factors in neurodegenerative disorders, and brain lesions associated with Alzheimer's disease are rich in Fe(III), Zn(II), and Cu(II). By using different biophysical techniques (nuclear magnetic resonance, circular dichroism, light scattering, and microcalorimetry), we have structurally characterized the binding of Cu(II) to a 198 amino acid fragment of the protein Tau that can mimic both the aggregation behavior and microtubule binding properties of the full-length protein. We demonstrate that Tau can specifically bind one Cu(II) ion per monomer with a dissociation constant in the micromolar range, an affinity comparable to the binding of Cu(II) to other proteins involved in neurodegenerative diseases. NMR spectroscopy showed that two short stretches of residues, (287)VQSKCGS(293) and (310)YKPVDLSKVTSKCGS(324), are primarily involved in copper binding, in agreement with mutational analysis. According to circular dichroism and NMR spectroscopy, Tau remains largely disordered upon binding to Cu(II), although a limited amount of aggregation is induced."],["dc.identifier.doi","10.1021/bi8008856"],["dc.identifier.gro","3143225"],["dc.identifier.isi","000259868300003"],["dc.identifier.pmid","18803399"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/716"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0006-2960"],["dc.title","Structural characterization of binding of Cu(II) to Tau protein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]