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S100B chaperone multimers suppress the formation of oligomers during Aβ42 aggregation.
Front Neurosci. 2023 Mar 21;17:1162741. doi: 10.3389/fnins.2023.1162741. eCollection 2023.
Front Neurosci. 2023.
PMID: 37025373
Free PMC article.
Tetramerization of the S100B Chaperone Spawns a Ca2+ Independent Regulatory Surface that Enhances Anti-aggregation Activity and Client Specificity.
Figueira AJ, Moreira GG, Saavedra J, Cardoso I, Gomes CM.
Figueira AJ, et al.
J Mol Biol. 2022 Oct 15;434(19):167791. doi: 10.1016/j.jmb.2022.167791. Epub 2022 Aug 12.
J Mol Biol. 2022.
PMID: 35970403
Free article.
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Secondary Modification of S100B Influences Anti Amyloid-β Aggregation Activity and Alzheimer's Disease Pathology.
Coelho R, De Benedictis CA, Sauer AK, Figueira AJ, Faustino H, Grabrucker AM, Gomes CM.
Coelho R, et al. Among authors: figueira aj.
Int J Mol Sci. 2024 Feb 1;25(3):1787. doi: 10.3390/ijms25031787.
Int J Mol Sci. 2024.
PMID: 38339064
Free PMC article.
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Computational Analysis of the Interactions between the S100B Extracellular Chaperone and Its Amyloid β Peptide Client.
Rodrigues FEP, Figueira AJ, Gomes CM, Machuqueiro M.
Rodrigues FEP, et al. Among authors: figueira aj.
Int J Mol Sci. 2021 Mar 31;22(7):3629. doi: 10.3390/ijms22073629.
Int J Mol Sci. 2021.
PMID: 33807304
Free PMC article.
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The S100B Alarmin Is a Dual-Function Chaperone Suppressing Amyloid-β Oligomerization through Combined Zinc Chelation and Inhibition of Protein Aggregation.
Cristóvão JS, Figueira AJ, Carapeto AP, Rodrigues MS, Cardoso I, Gomes CM.
Cristóvão JS, et al. Among authors: figueira aj.
ACS Chem Neurosci. 2020 Sep 2;11(17):2753-2760. doi: 10.1021/acschemneuro.0c00392. Epub 2020 Aug 7.
ACS Chem Neurosci. 2020.
PMID: 32706972
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