Publikationen Chemische Biologie der Proteinaggregation

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Structural basis for the inhibition of IAPP fibril formation by the co-chaperonin prefoldin.
Nature Communications 13(1), 2363 () [10.1038/s41467-022-30042-y] OpenAccess  Download fulltext Files  Download fulltextFulltext by Pubmed Central Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Alpha-Synuclein-Specific Naturally Occurring Antibodies Inhibit Aggregation In Vitro and In Vivo
Biomolecules 12(3), 469 - () [10.3390/biom12030469] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Editorial: The Biochemistry of Amyloids in Neurodegenerative Diseases, Volume I.
Frontiers in neuroscience 15, 819481 () [10.3389/fnins.2021.819481] OpenAccess  Download fulltext Files  Download fulltextFulltext by Pubmed Central Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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A β-Wrapin Targeting the N-Terminus of α-Synuclein Monomers Reduces Fibril-Induced Aggregation in Neurons.
Frontiers in neuroscience 15, 696440 () [10.3389/fnins.2021.696440] OpenAccess  Download fulltext Files  Download fulltextFulltext by Pubmed Central Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Endo-lysosomal Aβ concentration and pH trigger formation of Aβ oligomers that potently induce Tau missorting
Nature Communications 12(1), 4634 () [10.1038/s41467-021-24900-4] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids
Chemical reviews 121(13), 8285 - 8307 () [10.1021/acs.chemrev.1c00196] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Structural details of amyloid β oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy
The journal of biological chemistry 296, 100499 - () [10.1016/j.jbc.2021.100499] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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β-Turn exchanges in the α-synuclein segment 44-TKEG-47 reveal high sequence fidelity requirements of amyloid fibril elongation
Biophysical chemistry 269, 106519 - () [10.1016/j.bpc.2020.106519] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Protofibril‐Fibril Interactions Inhibit Amyloid Fibril Assembly by Obstructing Secondary Nucleation
Angewandte Chemie / International edition 60(6), 3016-3021 () [10.1002/anie.202010098] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Sub-stoichiometric inhibition of IAPP aggregation: a peptidomimetic approach to anti-amyloid agents
RSC chemical biology 1(4), 225-232 () [10.1039/D0CB00086H] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Inhibitor and substrate cooperate to inhibit amyloid fibril elongation of α-synuclein
Chemical science 11(41), 11331 - 11337 () [10.1039/D0SC04051G] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils
Nature structural & molecular biology 27(7), 660 - 667 () [10.1038/s41594-020-0442-4] Embargoed OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Clustering of human prion protein and α-synuclein oligomers requires the prion protein N-terminus
Communications biology 3(1), 365 () [10.1038/s42003-020-1085-z] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Mechanism of Fibril and Soluble Oligomer Formation in Amyloid Beta and Hen Egg White Lysozyme Proteins
The journal of physical chemistry <Washington, DC> / B B, Condensed matter, materials, surfaces, interfaces & biophysical 123(27), 5678 - 5689 () [10.1021/acs.jpcb.9b02338] Embargoed OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy
Nature Communications 10(1), 3754 () [10.1038/s41467-019-11320-8] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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α-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formation
Chemistry and physics of lipids 220, 57 - 65 () [10.1016/j.chemphyslip.2019.02.009] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils
eLife 8, e46112 () [10.7554/eLife.46112] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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α-Synuclein Aggregation Monitored by Thioflavin T Fluorescence Assay
Bio-protocol 8(14), PMC6066150 () [10.21769/BioProtoc.2941] BibTeX | EndNote: XML, Text | RIS

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Elucidating the multi-targeted anti-amyloid activity and enhanced islet amyloid polypeptide binding of β-wrapins
Computers & chemical engineering 116, 322 - 332 () [10.1016/j.compchemeng.2018.02.013] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Transcriptome-wide analysis uncovers the targets of the RNA-binding protein MSI2 and effects of MSI2's RNA-binding activity on IL-6 signaling
The journal of biological chemistry 293(40), 15359 - 15369 () [10.1074/jbc.RA118.002243] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Origin of metastable oligomers and their effects on amyloid fibril self-assembly
Chemical science 9(27), 5937 - 5948 () [10.1039/C8SC01479E] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formation
Communications biology 1(1), 44 () [10.1038/s42003-018-0049-z] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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A D-enantiomeric peptide interferes with hetero-association of amyloid-β oligomers and prion protein
The journal of biological chemistry 293, jbc.RA118.003116 - () [10.1074/jbc.RA118.003116] Embargoed OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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DNP-Enhanced MAS NMR: A Tool to Snapshot Conformational Ensembles of α -Synuclein in Different States
Biophysical journal 114(7), 1614 - 1623 () [10.1016/j.bpj.2018.02.011] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Opposed effects of dityrosine formation in soluble and aggregated alpha-synuclein on fibril growth
Journal of molecular biology 429, 3018-3030 () [10.1016/j.jmb.2017.09.005] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Fibril structure of amyloid-ß(1-42) by cryoelectron microscopy
Science 358, 116-119 () [10.1126/science.aao2825]  Download fulltext Files BibTeX | EndNote: XML, Text | RIS

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Uncovering the Binding and Specificity of β-Wrapins for Amyloid-β and α-Synuclein
The journal of physical chemistry <Washington, DC> / B 120(50), 12781-12794 () [10.1021/acs.jpcb.6b08485]  Download fulltext Files BibTeX | EndNote: XML, Text | RIS

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β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor
Scientific reports 6, 33474 - () [10.1038/srep33474] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Structural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the β-Sheet Core
PLoS one 11(9), e0161243 () [10.1371/journal.pone.0161243] OpenAccess  Download fulltext Files  Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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Structural characterization of alpha-Synuclein amyloids
The Prion Phenomena in Neurodegenerative Diseases Hauppauge NY; USA : Nova Science Publishers 111-128 () BibTeX | EndNote: XML, Text | RIS

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Contact between the β1 and β2 Segments of α-Synuclein that Inhibits Amyloid Formation
Angewandte Chemie / International edition 54(30), 8837 - 8840 () [10.1002/anie.201503018]  Download fulltext Files BibTeX | EndNote: XML, Text | RIS

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QIAD assay for quantitating a compound’s efficacy in elimination of toxic Aβ oligomers
Scientific reports 5, 13222 () [10.1038/srep13222] OpenAccess  Download fulltext Files  Download fulltextFulltext Download fulltextFulltext by OpenAccess repository BibTeX | EndNote: XML, Text | RIS

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A β-Hairpin-Binding Protein for Three Different Disease-Related Amyloidogenic Proteins
ChemBioChem 16(3), 411 - 414 () [10.1002/cbic.201402552]  Download fulltext Files BibTeX | EndNote: XML, Text | RIS

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What does solid-state NMR tell us about Amyloid structures?
Amyloid fibrils and prefibrillar aggregates Weinheim : Wiley-VCH 39-62 ()   Download fulltextFulltext BibTeX | EndNote: XML, Text | RIS

Letzte Änderung: 10.06.2022