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Amyloid formation and depolymerization of tumor suppressor p16<sup>INK4a</sup> are regulated by a thiol-dependent redox mechanism.
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- Nature Communications, 2024, v. 15, n. 1, p. 1, doi. 10.1038/s41467-024-49581-7
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- Article
Amyloid formation and depolymerization of tumor suppressor p16<sup>INK4a</sup> are regulated by a thiol-dependent redox mechanism.
- Published in:
- Nature Communications, 2024, v. 15, n. 1, p. 1, doi. 10.1038/s41467-024-49581-7
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- Article
Taylor Dispersion‐Induced Phase Separation for the Efficient Characterisation of Protein Condensate Formation.
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- Angewandte Chemie, 2024, v. 136, n. 25, p. 1, doi. 10.1002/ange.202404018
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- Article
Taylor Dispersion‐Induced Phase Separation for the Efficient Characterisation of Protein Condensate Formation.
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- Angewandte Chemie International Edition, 2024, v. 63, n. 25, p. 1, doi. 10.1002/anie.202404018
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- Article
Widespread amyloidogenicity potential of multiple myeloma patient-derived immunoglobulin light chains.
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- BMC Biology, 2023, p. 1, doi. 10.1186/s12915-022-01506-w
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- Article
Capillary flow experiments for thermodynamic and kinetic characterization of protein liquid-liquid phase separation.
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- Nature Communications, 2021, v. 12, n. 1, p. 1, doi. 10.1038/s41467-021-27433-y
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- Article
Hydroxy‐Porphyrin as an Effective, Endogenous Molecular Clamp during Early Stages of Amyloid Fibrillization.
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- Chemistry - An Asian Journal, 2021, v. 16, n. 23, p. 3931, doi. 10.1002/asia.202100965
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- Article
Correction to: Reproducibility and accuracy of microscale thermophoresis in the NanoTemper Monolith: a multi laboratory benchmark study.
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- 2021
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- Correction Notice
Reproducibility and accuracy of microscale thermophoresis in the NanoTemper Monolith: a multi laboratory benchmark study.
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- European Biophysics Journal, 2021, v. 50, n. 3/4, p. 411, doi. 10.1007/s00249-021-01532-6
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- Article
The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth.
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- PLoS Computational Biology, 2020, v. 16, n. 5, p. 1, doi. 10.1371/journal.pcbi.1007767
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- Article
The Aggregation Conditions Define Whether EGCG is an Inhibitor or Enhancer of α-Synuclein Amyloid Fibril Formation.
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- International Journal of Molecular Sciences, 2020, v. 21, n. 6, p. 1995, doi. 10.3390/ijms21061995
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- Article
Biochemical and biophysical characterisation of immunoglobulin free light chains derived from an initially unbiased population of patients with light chain disease.
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- PeerJ, 2020, p. 1, doi. 10.7717/peerj.8771
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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
The growth of amyloid fibrils: rates and mechanisms.
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- Biochemical Journal, 2019, v. 476, n. 19, p. 2677, doi. 10.1042/BCJ20160868
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- Article
Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy.
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- Nature Communications, 2019, v. 10, n. 1, p. N.PAG, doi. 10.1038/s41467-019-11320-8
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- Article
Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formation.
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- Communications Biology, 2018, v. 1, n. 1, p. N.PAG, doi. 10.1038/s42003-018-0049-z
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- Article
Nanobodies raised against monomeric α-synuclein inhibit fibril formation and destabilize toxic oligomeric species.
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- BMC Biology, 2017, v. 15, p. 1, doi. 10.1186/s12915-017-0390-6
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- Article
Secondary nucleation of monomers on fibril surface dominates α -synuclein aggregation and provides autocatalytic amyloid amplification.
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- Quarterly Reviews of Biophysics, 2017, v. 50, p. 1, doi. 10.1017/S0033583516000172
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- Article
β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces.
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- Scientific Reports, 2016, p. 36010, doi. 10.1038/srep36010
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- Article
Protein Aggregate-Ligand Binding Assays Based on Microfluidic Diffusional Separation.
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- ChemBioChem, 2016, v. 17, n. 20, p. 1920, doi. 10.1002/cbic.201600384
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- Article
Quantitative thermophoretic study of disease-related protein aggregates.
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- Scientific Reports, 2016, p. 22829, doi. 10.1038/srep22829
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- Article
Mécanismes fondamentaux de formation de fibres amyloïdes par la protéine a-synucléine dans la maladie de Parkinson.
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- Médecine Sciences, 2015, v. 31, n. 6/7, p. 597, doi. 10.1051/medsci/20153106008
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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
Ostwald's rule of stages governs structural transitions and morphology of dipeptide supramolecular polymers.
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- Nature Communications, 2014, v. 5, n. 11, p. 5219, doi. 10.1038/ncomms6219
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- Article
Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein by Small Molecules as a Potential Therapeutic Strategy for Parkinson’s Disease.
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- PLoS ONE, 2014, v. 9, n. 2, p. 1, doi. 10.1371/journal.pone.0087133
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- Article
The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation.
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- Essays in Biochemistry, 2014, v. 56, p. 11, doi. 10.1042/BSE0560011
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- Article
A Label-Free, Quantitative Assay of Amyloid Fibril Growth Based on Intrinsic Fluorescence.
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- ChemBioChem, 2013, v. 14, n. 7, p. 846, doi. 10.1002/cbic.201300103
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- Article
Analyse der Energiebarrieren für das Wachstum von Amyloidfibrillen.
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- Angewandte Chemie, 2012, v. 124, n. 21, p. 5339, doi. 10.1002/ange.201108040
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- Article
Detailed Analysis of the Energy Barriers for Amyloid Fibril Growth.
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- Angewandte Chemie International Edition, 2012, v. 51, n. 21, p. 5247, doi. 10.1002/anie.201108040
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- Article
Nanostructured films from hierarchical self-assembly of amyloidogenic proteins.
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- Nature Nanotechnology, 2010, v. 5, n. 3, p. 204, doi. 10.1038/nnano.2010.26
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- Article
Biosensor-based label-free assays of amyloid growth
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- FEBS Letters, 2009, v. 583, n. 16, p. 2587, doi. 10.1016/j.febslet.2009.06.008
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- Article
Position-Dependent Electrostatic Protection against Protein Aggregation.
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- ChemBioChem, 2009, v. 10, n. 8, p. 1309, doi. 10.1002/cbic.200900144
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- Article