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Kinetic theory of protein filament growth: Self-consistent methods and perturbative techniques.
- Published in:
- International Journal of Modern Physics B: Condensed Matter Physics; Statistical Physics; Applied Physics, 2015, v. 29, n. 2, p. -1, doi. 10.1142/S0217979215300029
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- Article
β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces.
- Published in:
- Scientific Reports, 2016, p. 36010, doi. 10.1038/srep36010
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- Article
Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms.
- Published in:
- Scientific Reports, 2016, p. 28658, doi. 10.1038/srep28658
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- Article
Screening of small molecules using the inhibition of oligomer formation in α-synuclein aggregation as a selection parameter.
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- Communications Chemistry, 2020, v. 3, n. 1, p. 1, doi. 10.1038/s42004-020-00412-y
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- Article
Trodusquemine enhances Aβ<sub>42</sub> aggregation but suppresses its toxicity by displacing oligomers from cell membranes.
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- Nature Communications, 2019, v. 10, n. 1, p. 1, doi. 10.1038/s41467-018-07699-5
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- Article
Aggregation-Prone Amyloid-β⋅Cu<sup>II</sup> Species Formed on the Millisecond Timescale under Mildly Acidic Conditions.
- Published in:
- ChemBioChem, 2015, v. 16, n. 9, p. 1293, doi. 10.1002/cbic.201500080
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- Article
Fabrication of fibrillosomes from droplets stabilized by protein nanofibrils at all-aqueous interfaces.
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- Nature Communications, 2016, v. 7, n. 10, p. 12934, doi. 10.1038/ncomms12934
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- Article
Dynamic microfluidic control of supramolecular peptide self-assembly.
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- Nature Communications, 2016, v. 7, n. 10, p. 13190, doi. 10.1038/ncomms13190
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Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation.
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- Nature Communications, 2016, v. 7, n. 3, p. 10948, doi. 10.1038/ncomms10948
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- Article
A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's disease.
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- Scientific Reports, 2020, v. 10, n. 1, p. N.PAG, doi. 10.1038/s41598-020-69626-3
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- Article
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation.
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- Nature Chemical Biology, 2015, v. 11, n. 3, p. 229, doi. 10.1038/nchembio.1750
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- Article
Deformable and Robust Core–Shell Protein Microcapsules Templated by Liquid–Liquid Phase‐Separated Microdroplets.
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- Advanced Materials Interfaces, 2021, v. 8, n. 19, p. 1, doi. 10.1002/admi.202101071
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- Article
Molecular mechanisms of protein aggregation from global fitting of kinetic models.
- Published in:
- Nature Protocols, 2016, v. 11, n. 2, p. 252, doi. 10.1038/nprot.2016.010
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- Article