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Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6.
- Published in:
- Angewandte Chemie, 2017, v. 129, n. 19, p. 5286, doi. 10.1002/ange.201611750
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Frontispiz: Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6.
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- Angewandte Chemie, 2017, v. 129, n. 19, p. n/a, doi. 10.1002/ange.201781961
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- Article
Pharmacological characterization of mutant huntingtin aggregate-directed PET imaging tracer candidates.
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- Scientific Reports, 2021, v. 11, n. 1, p. 1, doi. 10.1038/s41598-021-97334-z
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Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6.
- Published in:
- Angewandte Chemie International Edition, 2017, v. 56, n. 19, p. 5202, doi. 10.1002/anie.201611750
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- Article
Frontispiece: Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6.
- Published in:
- Angewandte Chemie International Edition, 2017, v. 56, n. 19, p. n/a, doi. 10.1002/anie.201781961
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- Article
TBK1 phosphorylates mutant Huntingtin and suppresses its aggregation and toxicity in Huntington's disease models.
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- EMBO Journal, 2020, v. 39, n. 17, p. 1, doi. 10.15252/embj.2020104671
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Site‐Specific Phosphorylation of Huntingtin Exon 1 Recombinant Proteins Enabled by the Discovery of Novel Kinases.
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- ChemBioChem, 2021, v. 22, n. 1, p. 217, doi. 10.1002/cbic.202000508
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Revisiting the specificity and ability of phospho-S129 antibodies to capture alpha-synuclein biochemical and pathological diversity.
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- NPJ Parkinson's Disease, 2022, v. 8, n. 1, p. 1, doi. 10.1038/s41531-022-00388-7
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A simple, versatile and robust centrifugation‐based filtration protocol for the isolation and quantification of α‐synuclein monomers, oligomers and fibrils: Towards improving experimental reproducibility in α‐synuclein research
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- Journal of Neurochemistry, 2020, v. 153, n. 1, p. 103, doi. 10.1111/jnc.14955
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Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity.
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- Nature Communications, 2020, v. 11, n. 1, p. 1, doi. 10.1038/s41467-020-16564-3
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Exploring the role of post‐translational modifications in regulating α‐synuclein interactions by studying the effects of phosphorylation on nanobody binding.
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- Protein Science: A Publication of the Protein Society, 2018, v. 27, n. 7, p. 1262, doi. 10.1002/pro.3412
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