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Conformation-Specific Association of Prion Protein Amyloid Aggregates with Tau Protein Monomers.
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- International Journal of Molecular Sciences, 2023, v. 24, n. 11, p. 9277, doi. 10.3390/ijms24119277
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- Article
The Major Components of Cerebrospinal Fluid Dictate the Characteristics of Inhibitors against Amyloid-Beta Aggregation.
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- International Journal of Molecular Sciences, 2023, v. 24, n. 6, p. 5991, doi. 10.3390/ijms24065991
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- Article
Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy.
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- International Journal of Molecular Sciences, 2022, v. 23, n. 12, p. 6781, doi. 10.3390/ijms23126781
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- Article
Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State.
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- International Journal of Molecular Sciences, 2022, v. 23, n. 10, p. 5421, doi. 10.3390/ijms23105421
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- Article
Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration.
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- International Journal of Molecular Sciences, 2021, v. 22, n. 22, p. 12382, doi. 10.3390/ijms222212382
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- Article
Aggregation Condition–Structure Relationship of Mouse Prion Protein Fibrils.
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- International Journal of Molecular Sciences, 2021, v. 22, n. 17, p. 9635, doi. 10.3390/ijms22179635
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- Article
Co-Aggregation of S100A9 with DOPA and Cyclen-Based Compounds Manifested in Amyloid Fibril Thickening without Altering Rates of Self-Assembly.
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- International Journal of Molecular Sciences, 2021, v. 22, n. 16, p. 8556, doi. 10.3390/ijms22168556
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- Article
S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation.
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- International Journal of Molecular Sciences, 2021, v. 22, n. 15, p. 7972, doi. 10.3390/ijms22157972
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- Article
Human Polymerase δ-Interacting Protein 2 (PolDIP2) Inhibits the Formation of Human Tau Oligomers and Fibrils.
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- International Journal of Molecular Sciences, 2021, v. 22, n. 11, p. 5768, doi. 10.3390/ijms22115768
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- Article
Variability of Amyloid Propensity in Imperfect Repeats of CsgA Protein of Salmonella enterica and Escherichia coli.
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- International Journal of Molecular Sciences, 2021, v. 22, n. 10, p. 5127, doi. 10.3390/ijms22105127
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- Article
Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils.
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- International Journal of Molecular Sciences, 2021, v. 22, n. 10, p. 5075, doi. 10.3390/ijms22105075
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- Article
Amyloid Structural Changes Studied by Infrared Microspectroscopy in Bigenic Cellular Models of Alzheimer's Disease.
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- International Journal of Molecular Sciences, 2021, v. 22, n. 7, p. 3430, doi. 10.3390/ijms22073430
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- Article
Lysozyme Fibrils Alter the Mechanism of Insulin Amyloid Aggregation.
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- International Journal of Molecular Sciences, 2021, v. 22, n. 4, p. 1775, doi. 10.3390/ijms22041775
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- Article
Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates.
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- International Journal of Molecular Sciences, 2020, v. 21, n. 19, p. 7410, doi. 10.3390/ijms21197410
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- Article
Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange.
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- Nature Structural & Molecular Biology, 2011, v. 18, n. 4, p. 504, doi. 10.1038/nsmb.2035
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- Article
Protein Amyloidogenesis in the Context of Volume Fluctuations: A Case Study on Insulin.
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- ChemPhysChem, 2006, v. 7, n. 5, p. 1046, doi. 10.1002/cphc.200500717
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- Article
Structure‐Activity Relationship of Fluorinated Benzenesulfonamides as Inhibitors of Amyloid‐β Aggregation.
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- Chemistry - A European Journal, 2024, v. 30, n. 58, p. 1, doi. 10.1002/chem.202402330
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- Article
Cover Feature: Structure‐Activity Relationship of Fluorinated Benzenesulfonamides as Inhibitors of Amyloid‐β Aggregation (Chem. Eur. J. 58/2024).
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- Chemistry - A European Journal, 2024, v. 30, n. 58, p. 1, doi. 10.1002/chem.202485804
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- Article
pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils.
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- PLoS ONE, 2015, v. 10, n. 8, p. 1, doi. 10.1371/journal.pone.0136602
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- Article
Flavone Derivatives as Inhibitors of Insulin Amyloid-Like Fibril Formation.
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- PLoS ONE, 2015, v. 10, n. 3, p. 1, doi. 10.1371/journal.pone.0121231
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- Article
Elongation of Mouse Prion Protein Amyloid-Like Fibrils: Effect of Temperature and Denaturant Concentration.
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- PLoS ONE, 2014, v. 9, n. 4, p. 1, doi. 10.1371/journal.pone.0094469
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- Article
Amyloid-Like Fibril Elongation Follows Michaelis-Menten Kinetics.
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- PLoS ONE, 2013, v. 8, n. 7, p. 1, doi. 10.1371/journal.pone.0068684
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- Article
The Environment Is a Key Factor in Determining the Anti-Amyloid Efficacy of EGCG.
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- Biomolecules (2218-273X), 2019, v. 9, n. 12, p. 855, doi. 10.3390/biom9120855
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- Article
Liquid–liquid phase separation of alpha‐synuclein increases the structural variability of fibrils formed during amyloid aggregation.
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- FEBS Journal, 2024, v. 291, n. 20, p. 4522, doi. 10.1111/febs.17244
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- Article
Formation of distinct prion protein amyloid fibrils under identical experimental conditions.
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- Scientific Reports, 2020, v. 10, n. 1, p. 1, doi. 10.1038/s41598-020-61663-2
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- Article
Effects of Pulsed Electric Fields on Yeast with Prions and the Structure of Amyloid Fibrils.
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- Applied Sciences (2076-3417), 2021, v. 11, n. 6, p. 2684, doi. 10.3390/app11062684
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- Article
Extracellular tau induces microglial phagocytosis of living neurons in cell cultures.
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- Journal of Neurochemistry, 2020, v. 154, n. 3, p. 316, doi. 10.1111/jnc.14940
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- Article
Exploring Epigallocatechin-3-Gallate Autoxidation Products: Specific Incubation Times Required for Emergence of Anti-Amyloid Properties.
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- Antioxidants, 2022, v. 11, n. 10, p. N.PAG, doi. 10.3390/antiox11101887
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- Article
Exploring the Formation of Polymers with Anti-Amyloid Properties within the 2′3′-Dihydroxyflavone Autoxidation Process.
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- Antioxidants, 2022, v. 11, n. 9, p. 1711, doi. 10.3390/antiox11091711
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- Article
Autoxidation Enhances Anti-Amyloid Potential of Flavone Derivatives.
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- Antioxidants, 2021, v. 10, n. 9, p. 1428, doi. 10.3390/antiox10091428
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- Article
Bioinformatics methods for identification of amyloidogenic peptides show robustness to misannotated training data.
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- Scientific Reports, 2021, v. 11, n. 1, p. 1, doi. 10.1038/s41598-021-86530-6
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- Article
Gallic acid oxidation products alter the formation pathway of insulin amyloid fibrils.
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- Scientific Reports, 2020, v. 10, n. 1, p. N.PAG, doi. 10.1038/s41598-020-70982-3
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- Article
Rapid restructurization of conformationally-distinct alpha-synuclein amyloid fibrils at an elevated temperature.
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- PeerJ, 2022, p. 1, doi. 10.7717/peerj.14137
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- Article
Interplay between epigallocatechin-3-gallate and ionic strength during amyloid aggregation.
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- PeerJ, 2021, p. 1, doi. 10.7717/peerj.12381
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- Article
Exploring the occurrence of thioflavin-T-positive insulin amyloid aggregation intermediates.
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- PeerJ, 2021, p. 1, doi. 10.7717/peerj.10918
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- Article
Methylene blue inhibits nucleation and elongation of SOD1 amyloid fibrils.
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- PeerJ, 2020, p. 1, doi. 10.7717/peerj.9719
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- Article
Concentration-dependent polymorphism of insulin amyloid fibrils.
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- PeerJ, 2019, p. 1, doi. 10.7717/peerj.8208
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- Article
Exploring the potential of deep-blue autofluorescence for monitoring amyloid fibril formation and dissociation.
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- PeerJ, 2019, p. 1, doi. 10.7717/peerj.7554
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- Article
Emergence of visible light optical properties of L-phenylalanine aggregates.
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- PeerJ, 2019, p. 1, doi. 10.7717/peerj.6518
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- Publication type:
- Article
Solid-state NMR backbone chemical shift assignments of α-synuclein amyloid fibrils at fast MAS regime.
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- Biomolecular NMR Assignments, 2024, v. 18, n. 2, p. 181, doi. 10.1007/s12104-024-10186-2
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- Article
Using lysozyme amyloid fibrils as a means of scavenging aggregation‐inhibiting compounds.
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- Biotechnology Journal, 2021, v. 16, n. 9, p. 1, doi. 10.1002/biot.202100138
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- Article
PROTEIN AGGREGATION AND NEURONAL LOSS IN EXPERIMENTAL MODELS OF NEURODEGENERATIVE DISORDERS.
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- Neurologijos Seminarai, 2018, v. 22, n. 3, p. 238
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- Article
Insulin forms amyloid in a strain-dependent manner: An FT-IR spectroscopic study.
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- Protein Science: A Publication of the Protein Society, 2004, v. 13, n. 7, p. 1927, doi. 10.1110/ps.03607204
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- Article
Study of Insulin Aggregation and Fibril Structure under Different Environmental Conditions.
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- International Journal of Molecular Sciences, 2024, v. 25, n. 17, p. 9406, doi. 10.3390/ijms25179406
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- Article
ApoE Isoforms Inhibit Amyloid Aggregation of Proinflammatory Protein S100A9.
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- International Journal of Molecular Sciences, 2024, v. 25, n. 4, p. 2114, doi. 10.3390/ijms25042114
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- Article
The Stabilization of S100A9 Structure by Calcium Inhibits the Formation of Amyloid Fibrils.
- Published in:
- International Journal of Molecular Sciences, 2023, v. 24, n. 17, p. 13200, doi. 10.3390/ijms241713200
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- Article
Distinct Neurotoxic Effects of Extracellular Tau Species in Primary Neuronal-Glial Cultures.
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- Molecular Neurobiology, 2021, v. 58, n. 2, p. 658, doi. 10.1007/s12035-020-02150-7
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- Article
Extracellular tau stimulates phagocytosis of living neurons by activated microglia via Toll-like 4 receptor–NLRP3 inflammasome–caspase-1 signalling axis.
- Published in:
- Scientific Reports, 2023, v. 13, n. 1, p. 1, doi. 10.1038/s41598-023-37887-3
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- Article
Investigating lysozyme amyloid fibril formation and structural variability dependence on its initial folding state under different pH conditions.
- Published in:
- Protein Science: A Publication of the Protein Society, 2024, v. 33, n. 2, p. 1, doi. 10.1002/pro.4888
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- Article