Found: 24
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Hidden Aggregation Hot-Spots on Human Apolipoprotein E: A Structural Study.
- Published in:
- International Journal of Molecular Sciences, 2019, v. 20, n. 9, p. 2274, doi. 10.3390/ijms20092274
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- Article
Mapping the sequence specificity of heterotypic amyloid interactions enables the identification of aggregation modifiers.
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- Nature Communications, 2022, v. 13, n. 1, p. 1, doi. 10.1038/s41467-022-28955-9
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- Article
Enhanced therapeutic window for antimicrobial Pept-ins by investigating their structure-activity relationship.
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- PLoS ONE, 2023, v. 17, n. 3, p. 1, doi. 10.1371/journal.pone.0283674
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- Article
Heterotypic Amyloid β interactions facilitate amyloid assembly and modify amyloid structure.
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- EMBO Journal, 2022, v. 41, n. 2, p. 1, doi. 10.15252/embj.2021108591
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- Article
Autonomous aggregation suppression by acidic residues explains why chaperones favour basic residues.
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- EMBO Journal, 2020, v. 39, n. 11, p. 1, doi. 10.15252/embj.2019102864
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- Article
CORDAX web server: an online platform for the prediction and 3D visualization of aggregation motifs in protein sequences.
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- Bioinformatics, 2024, v. 40, n. 5, p. 1, doi. 10.1093/bioinformatics/btae279
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- Article
StAmP-DB: a platform for structures of polymorphic amyloid fibril cores.
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- Bioinformatics, 2022, v. 38, n. 9, p. 2636, doi. 10.1093/bioinformatics/btac126
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- Article
Local structural preferences in shaping tau amyloid polymorphism.
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- Nature Communications, 2024, v. 15, n. 1, p. 1, doi. 10.1038/s41467-024-45429-2
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- Article
Author Correction: Reverse engineering synthetic antiviral amyloids.
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- 2023
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- Correction Notice
Structural Analysis of Peptide-Analogues of Human <i>Zona Pellucida</i> ZP1 Protein with Amyloidogenic Properties: Insights into Mammalian <i>Zona Pellucida</i> Formation.
- Published in:
- PLoS ONE, 2013, v. 8, n. 9, p. 1, doi. 10.1371/journal.pone.0073258
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- Article
Heterotypic interactions in amyloid function and disease.
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- FEBS Journal, 2022, v. 289, n. 8, p. 2025, doi. 10.1111/febs.15719
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- Article
A β-solenoid model of the Pmel17 repeat domain: insights to the formation of functional amyloid fibrils.
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- Journal of Computer-Aided Molecular Design, 2016, v. 30, n. 2, p. 153, doi. 10.1007/s10822-015-9892-x
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- Article
Exposure of a cryptic Hsp70 binding site determines the cytotoxicity of the ALS-associated SOD1-mutant A4V.
- Published in:
- PEDS: Protein Engineering, Design & Selection, 2019, v. 32, n. 10, p. 443, doi. 10.1093/protein/gzaa008
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- Article
WALTZ-DB 2.0: an updated database containing structural information of experimentally determined amyloid-forming peptides.
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- Nucleic Acids Research, 2020, v. 48, n. D1, p. D389, doi. 10.1093/nar/gkz758
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- Article
Aggregating sequences that occur in many proteins constitute weak spots of bacterial proteostasis.
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- Nature Communications, 2018, v. 9, n. 1, p. 1, doi. 10.1038/s41467-018-03131-0
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- Article
A common 'aggregation-prone' interface possibly participates in the self-assembly of human zona pellucida proteins.
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- FEBS Letters, 2016, v. 590, n. 5, p. 619, doi. 10.1002/1873-3468.12099
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- Article
An N-terminal pro-atrial natriuretic peptide (NT-proANP) ‘aggregation-prone’ segment involved in isolated atrial amyloidosis.
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- FEBS Letters, 2014, v. 588, n. 1, p. 52, doi. 10.1016/j.febslet.2013.10.049
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- Article
Arabidopsis thaliana Plant Natriuretic Peptide Active Domain Forms Amyloid-like Fibrils in a pH-Dependent Manner.
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- Plants (2223-7747), 2022, v. 11, n. 1, p. 9, doi. 10.3390/plants11010009
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- Article
Unraveling the Aggregation Propensity of Human Insulin C-Peptide.
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- Biopolymers, 2017, v. 108, n. 2, p. 1, doi. 10.1002/bip.22882
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- Article
Identification of an amyloid fibril forming segment of human Pmel17 repeat domain ( RPT domain).
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- Biopolymers, 2016, v. 106, n. 1, p. 133, doi. 10.1002/bip.22746
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- Article
Structural studies and cytotoxicity assays of 'aggregation-prone' IAPP<sub>8-16</sub> and its non-amyloidogenic variants suggest its important role in fibrillogenesis and cytotoxicity of human amylin.
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- Biopolymers, 2015, v. 104, n. 3, p. 196, doi. 10.1002/bip.22650
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- Article
Structural studies of 'aggregation-prone' peptide-analogues of teleostean egg chorion ZPB proteins.
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- Biopolymers, 2014, v. 102, n. 6, p. 427, doi. 10.1002/bip.22563
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- Article
Structure-based machine-guided mapping of amyloid sequence space reveals uncharted sequence clusters with higher solubilities.
- Published in:
- Nature Communications, 2020, v. 11, n. 1, p. 1, doi. 10.1038/s41467-020-17207-3
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- Article
Reverse engineering synthetic antiviral amyloids.
- Published in:
- Nature Communications, 2020, v. 11, n. 1, p. 1, doi. 10.1038/s41467-020-16721-8
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- Publication type:
- Article