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NMR of a-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation.
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- EMBO Journal, 2004, v. 23, n. 10, p. 2039, doi. 10.1038/sj.emboj.7600211
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- Article
Role of Tyr-39 for the Structural Features of α-Synuclein and for the Interaction with a Strong Modulator of Its Amyloid Assembly.
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- International Journal of Molecular Sciences, 2020, v. 21, n. 14, p. 5061, doi. 10.3390/ijms21145061
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- Article
Repurposing doxycycline for synucleinopathies: remodelling of α-synuclein oligomers towards non-toxic parallel beta-sheet structured species.
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- Scientific Reports, 2017, p. 41755, doi. 10.1038/srep41755
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- Article
Recognition between a short unstructured peptide and a partially folded fragment leads to the thioredoxin fold sharing native-like dynamics.
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- Proteins, 2012, v. 80, n. 5, p. 1448, doi. 10.1002/prot.24043
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- Article
Metal-ligand interactions in perturbed blue copper sites: a paramagnetic <sup>1</sup>H NMR study of Co(II)-pseudoazurin.
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- Journal of Biological Inorganic Chemistry (JBIC), 2003, v. 8, n. 1/2, p. 75, doi. 10.1007/s00775-002-0390-y
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- Article
Membrane binding, internalization, and sorting of alpha-synuclein in the cell.
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- Acta Neuropathologica Communications, 2018, v. 6, n. 1, p. N.PAG, doi. 10.1186/s40478-018-0578-1
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- Article
Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts.
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- Nature Communications, 2019, v. 10, n. 1, p. 1, doi. 10.1038/s41467-019-13564-w
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- Article
Phosphorylation at S87 Is Enhanced in Synucleinopathies, Inhibits α-Synuclein Oligomerization, and Influences Synuclein-Membrane Interactions.
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- Journal of Neuroscience, 2010, v. 30, n. 9, p. 3184, doi. 10.1523/JNEUROSCI.5922-09.2010
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- Article
Small-Molecule-Induced Soluble Oligomers of α-Synuclein with Helical Structure.
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- Chemistry - A European Journal, 2017, v. 23, n. 53, p. 13010, doi. 10.1002/chem.201703001
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- Article
Small molecule-mediated stabilization of vesicle-associated helical α-synuclein inhibits pathogenic misfolding and aggregation.
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- Nature Communications, 2014, v. 5, n. 12, p. 5857, doi. 10.1038/ncomms6857
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- Article
Interaction of Cu(i) with the Met-X<sub>3</sub>-Met motif of alpha-synuclein: binding ligands, affinity and structural features.
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- Metallomics, 2018, v. 10, n. 10, p. 1383, doi. 10.1039/c8mt00232k
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- Article
Effects of alpha‐synuclein post‐translational modifications on metal binding.
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- Journal of Neurochemistry, 2019, v. 150, n. 5, p. 507, doi. 10.1111/jnc.14721
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Ladungsinduzierte molekulare Ausrichtung von intrinsisch ungeordneten ProteinenL.S. erhält ein Marie-Curie-Stipendium (MEST-CT-2004-504193), M.-K.C. ein Stipendium des DFG-Graduiertenkollegs und M.Z. ein Emmy Noether-Stipendium (ZW 71/1-5)....
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- Angewandte Chemie, 2006, v. 118, n. 42, p. 7173, doi. 10.1002/ange.200602317
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Charge-Induced Molecular Alignment of Intrinsically Disordered Proteins.
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- Angewandte Chemie International Edition, 2006, v. 45, n. 42, p. 7012, doi. 10.1002/anie.200602317
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- Article
Conserved core of amyloid fibrils of wild type and A30P mutant α-synuclein.
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- Protein Science: A Publication of the Protein Society, 2011, v. 20, n. 2, p. 387, doi. 10.1002/pro.570
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- Article
Structural characterization of α-synuclein in an aggregation prone state.
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- Protein Science: A Publication of the Protein Society, 2009, v. 18, n. 9, p. 1840, doi. 10.1002/pro.194
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- Article
Correlation of Amyloid Fibril β-Structure with the Unfolded State of α-Synuclein.
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- ChemBioChem, 2007, v. 8, n. 14, p. 1671, doi. 10.1002/cbic.200700366
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- Article
Metal coordination and peripheral substitution modulate the activity of cyclic tetrapyrroles on αS aggregation: a structural and cell-based study.
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- Journal of Biological Inorganic Chemistry (JBIC), 2019, v. 24, n. 8, p. 1269, doi. 10.1007/s00775-019-01711-z
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Aroylhydrazones constitute a promising class of 'metal-protein attenuating compounds' for the treatment of Alzheimer's disease: a proof-of-concept based on the study of the interactions between zinc(II) and pyridine-2-carboxaldehyde isonicotinoyl hydrazone
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- Journal of Biological Inorganic Chemistry (JBIC), 2018, v. 23, n. 8, p. 1227, doi. 10.1007/s00775-018-1606-0
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Cover Picture: Dissociation of Amyloid Fibrils of α-Synuclein in Supercooled Water (Angew. Chem. Int. Ed. 27/2008).
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- Angewandte Chemie International Edition, 2008, v. 47, n. 27, p. 4939, doi. 10.1002/anie.200890127
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- Article
Dissociation of Amyloid Fibrils of α-Synuclein in Supercooled Water.
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- Angewandte Chemie International Edition, 2008, v. 47, n. 27, p. 5046, doi. 10.1002/anie.200800342
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- Article
Aromaticity at position 39 in α‐synuclein: A modulator of amyloid fibril assembly and membrane‐bound conformations.
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- Protein Science: A Publication of the Protein Society, 2022, v. 31, n. 7, p. 1, doi. 10.1002/pro.4360
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- Article