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Corrigendum: Direct Correlation Between Ligand-Induced α-Synuclein Oligomers and Amyloid-like Fibril Growth.
- Published in:
- Scientific Reports, 2015, p. 15692, doi. 10.1038/srep15692
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- Article
Considerably Unfolded Transthyretin Monomers Precede and Exchange with Dynamically Structured Amyloid Protofibrils.
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- Scientific Reports, 2015, p. 11443, doi. 10.1038/srep11443
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- Publication type:
- Article
Direct Correlation Between Ligand-Induced α-Synuclein Oligomers and Amyloid-like Fibril Growth.
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- Scientific Reports, 2015, p. 10422, doi. 10.1038/srep10422
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- Article
Cholesterol facilitates interactions between α-synuclein oligomers and charge-neutral membranes.
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- FEBS Letters, 2015, v. 589, n. 19PartB, p. 2661, doi. 10.1016/j.febslet.2015.08.013
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- Article
Avidity within the N‐terminal anchor drives α‐synuclein membrane interaction and insertion.
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- FASEB Journal, 2020, v. 34, n. 6, p. 7462, doi. 10.1096/fj.202000107R
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- Article
A cryo-electron microscopic study of ribosome-bound termination factor RF2.
- Published in:
- Nature, 2003, v. 421, n. 6918, p. 87, doi. 10.1038/nature01224
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- Article
Structure of the Escherichia coli ribosomal termination complex with release factor 2.
- Published in:
- Nature, 2003, v. 421, n. 6918, p. 90, doi. 10.1038/nature01225
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- Article
Early Stage Alpha-Synuclein Amyloid Fibrils are Reservoirs of Membrane-Binding Species.
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- Scientific Reports, 2019, v. 9, n. 1, p. 1, doi. 10.1038/s41598-018-38271-2
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- Article
Time-resolved SAXS measurements facilitated by online HPLC buffer exchange.
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- Journal of Synchrotron Radiation, 2010, v. 17, n. 6, p. 769, doi. 10.1107/S0909049510030372
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- Article
Monoclonal Antibodies Follow Distinct Aggregation Pathways During Production-Relevant Acidic Incubation and Neutralization.
- Published in:
- Pharmaceutical Research, 2016, v. 33, n. 3, p. 716, doi. 10.1007/s11095-015-1821-0
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- Article
High Concentration Formulation Studies of an IgG2 Antibody Using Small Angle X-ray Scattering.
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- Pharmaceutical Research, 2012, v. 29, n. 8, p. 2225, doi. 10.1007/s11095-012-0751-3
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- Article
Small Angle X-Ray Scattering Studies of Mitochondrial Glutaminase C Reveal Extended Flexible Regions, and Link Oligomeric State with Enzyme Activity.
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- PLoS ONE, 2013, v. 8, n. 9, p. 1, doi. 10.1371/journal.pone.0074783
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- Article
Unlocked Concanavalin A Forms Amyloid-like Fibrils from Coagulation of Long-lived “Crinkled” Intermediates.
- Published in:
- PLoS ONE, 2013, v. 8, n. 7, p. 1, doi. 10.1371/journal.pone.0068912
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- Article
Wildtype and A30P Mutant Alpha-Synuclein Form Different Fibril Structures.
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- PLoS ONE, 2013, v. 8, n. 7, p. 1, doi. 10.1371/journal.pone.0067713
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- Article
A Helical Structural Nucleus Is the Primary Elongating Unit of Insulin Amyloid Fibrils.
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- PLoS Biology, 2007, v. 5, n. 5, p. e134, doi. 10.1371/journal.pbio.0050134
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- Publication type:
- Article
The Non-Fibrillating N-Terminal of α-Synuclein Binds and Co-Fibrillates with Heparin.
- Published in:
- Biomolecules (2218-273X), 2020, v. 10, n. 8, p. 1192, doi. 10.3390/biom10081192
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- Article
Size‐exclusion chromatography small‐angle X‐ray scattering of water soluble proteins on a laboratory instrument.
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- Journal of Applied Crystallography, 2018, v. 51, n. 6, p. 1623, doi. 10.1107/S1600576718014462
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- Article
In situ microfluidic dialysis for biological smallangle X-ray scattering.
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- Journal of Applied Crystallography, 2014, v. 47, n. 4, p. 1355, doi. 10.1107/S1600576714012618
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- Article
Application of Bayesian analysis to indirect Fourier transformation in small-angle scattering.
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- 2006
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- Publication type:
- Other
Methods for structural characterization of prefibrillar intermediates and amyloid fibrils
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- FEBS Letters, 2009, v. 583, n. 16, p. 2600, doi. 10.1016/j.febslet.2009.05.040
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- Article
Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate
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- FEBS Letters, 2005, v. 579, n. 5, p. 1154, doi. 10.1016/j.febslet.2005.01.012
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- Publication type:
- Article