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Journal Abstract Search

271 related items for PubMed ID: 32706972

  • 1. 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.
    ACS Chem Neurosci; 2020 Sep 02; 11(17):2753-2760. PubMed ID: 32706972
    [Abstract] [Full Text] [Related]

  • 2. The neuronal S100B protein is a calcium-tuned suppressor of amyloid-β aggregation.
    Cristóvão JS, Morris VK, Cardoso I, Leal SS, Martínez J, Botelho HM, Göbl C, David R, Kierdorf K, Alemi M, Madl T, Fritz G, Reif B, Gomes CM.
    Sci Adv; 2018 Jun 02; 4(6):eaaq1702. PubMed ID: 29963623
    [Abstract] [Full Text] [Related]

  • 3. 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.
    J Mol Biol; 2022 Oct 15; 434(19):167791. PubMed ID: 35970403
    [Abstract] [Full Text] [Related]

  • 4. Computational Analysis of the Interactions between the S100B Extracellular Chaperone and Its Amyloid β Peptide Client.
    Rodrigues FEP, Figueira AJ, Gomes CM, Machuqueiro M.
    Int J Mol Sci; 2021 Mar 31; 22(7):. PubMed ID: 33807304
    [Abstract] [Full Text] [Related]

  • 5. S100B chaperone multimers suppress the formation of oligomers during Aβ42 aggregation.
    Figueira AJ, Saavedra J, Cardoso I, Gomes CM.
    Front Neurosci; 2023 Mar 31; 17():1162741. PubMed ID: 37025373
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  • 7. Identification of a Novel Multifunctional Ligand for Simultaneous Inhibition of Amyloid-Beta (Aβ42) and Chelation of Zinc Metal Ion.
    Asadbegi M, Shamloo A.
    ACS Chem Neurosci; 2019 Nov 20; 10(11):4619-4632. PubMed ID: 31566950
    [Abstract] [Full Text] [Related]

  • 8. d-Enantiomeric RTHLVFFARK-NH2: A Potent Multifunctional Decapeptide Inhibiting Cu2+-Mediated Amyloid β-Protein Aggregation and Remodeling Cu2+-Mediated Amyloid β Aggregates.
    Liu W, Dong X, Sun Y.
    ACS Chem Neurosci; 2019 Mar 20; 10(3):1390-1401. PubMed ID: 30650306
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  • 10. Quantitative NMR analysis of the mechanism and kinetics of chaperone Hsp104 action on amyloid-β42 aggregation and fibril formation.
    Ghosh S, Tugarinov V, Clore GM.
    Proc Natl Acad Sci U S A; 2023 May 23; 120(21):e2305823120. PubMed ID: 37186848
    [Abstract] [Full Text] [Related]

  • 11. Metal Binding of Alzheimer's Amyloid-β and Its Effect on Peptide Self-Assembly.
    Abelein A.
    Acc Chem Res; 2023 Oct 03; 56(19):2653-2663. PubMed ID: 37733746
    [Abstract] [Full Text] [Related]

  • 12. Stoichiometric Zn2+ interferes with the self-association of Aβ42: Insights from size distribution analysis.
    Zhang T, Pauly T, Nagel-Steger L.
    Int J Biol Macromol; 2018 Jul 01; 113():631-639. PubMed ID: 29476859
    [Abstract] [Full Text] [Related]

  • 13. Dynamic interactions and Ca2+-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding.
    Moreira GG, Cantrelle FX, Quezada A, Carvalho FS, Cristóvão JS, Sengupta U, Puangmalai N, Carapeto AP, Rodrigues MS, Cardoso I, Fritz G, Herrera F, Kayed R, Landrieu I, Gomes CM.
    Nat Commun; 2021 Nov 01; 12(1):6292. PubMed ID: 34725360
    [Abstract] [Full Text] [Related]

  • 14. Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.
    Abelein A, Gräslund A, Danielsson J.
    Proc Natl Acad Sci U S A; 2015 Apr 28; 112(17):5407-12. PubMed ID: 25825723
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  • 16. Metal ions differentially influence the aggregation and deposition of Alzheimer's beta-amyloid on a solid template.
    Ha C, Ryu J, Park CB.
    Biochemistry; 2007 May 22; 46(20):6118-25. PubMed ID: 17455909
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  • 19. Dynamics of Inter-Molecular Interactions Between Single Aβ42 Oligomeric and Aggregate Species by High-Speed Atomic Force Microscopy.
    Feng L, Watanabe H, Molino P, Wallace GG, Phung SL, Uchihashi T, Higgins MJ.
    J Mol Biol; 2019 Jul 12; 431(15):2687-2699. PubMed ID: 31075274
    [Abstract] [Full Text] [Related]

  • 20. The coexistence of an equal amount of Alzheimer's amyloid-β 40 and 42 forms structurally stable and toxic oligomers through a distinct pathway.
    Chang YJ, Chen YR.
    FEBS J; 2014 Jun 12; 281(11):2674-87. PubMed ID: 24720730
    [Abstract] [Full Text] [Related]

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