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Journal Abstract Search

153 related items for PubMed ID: 17407782

  • 1. The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species.
    Kumita JR, Poon S, Caddy GL, Hagan CL, Dumoulin M, Yerbury JJ, Stewart EM, Robinson CV, Wilson MR, Dobson CM.
    J Mol Biol; 2007 May 25; 369(1):157-67. PubMed ID: 17407782
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  • 2. The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures.
    Yerbury JJ, Poon S, Meehan S, Thompson B, Kumita JR, Dobson CM, Wilson MR.
    FASEB J; 2007 Aug 25; 21(10):2312-22. PubMed ID: 17412999
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  • 3. Clusterin in Alzheimer's disease: An amyloidogenic inhibitor of amyloid formation?
    Spatharas PM, Nasi GI, Tsiolaki PL, Theodoropoulou MK, Papandreou NC, Hoenger A, Trougakos IP, Iconomidou VA.
    Biochim Biophys Acta Mol Basis Dis; 2022 Jul 01; 1868(7):166384. PubMed ID: 35292360
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  • 4. Characterisation of the structural, dynamic and aggregation properties of the W64R amyloidogenic variant of human lysozyme.
    Vettore N, Moray J, Brans A, Herman R, Charlier P, Kumita JR, Kerff F, Dobson CM, Dumoulin M.
    Biophys Chem; 2021 Apr 01; 271():106563. PubMed ID: 33640796
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  • 5. The Extracellular Molecular Chaperone Clusterin Inhibits Amyloid Fibril Formation and Suppresses Cytotoxicity Associated with Semen-Derived Enhancer of Virus Infection (SEVI).
    Elias AK, Wilson MR, Carver JA, Musgrave IF.
    Cells; 2022 Oct 17; 11(20):. PubMed ID: 36291126
    [Abstract] [Full Text] [Related]

  • 6. A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.
    De Genst E, Chan PH, Pardon E, Hsu SD, Kumita JR, Christodoulou J, Menzer L, Chirgadze DY, Robinson CV, Muyldermans S, Matagne A, Wyns L, Dobson CM, Dumoulin M.
    J Phys Chem B; 2013 Oct 24; 117(42):13245-13258. PubMed ID: 23919586
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  • 7. Clusterin Binds to Aβ1-42 Oligomers with High Affinity and Interferes with Peptide Aggregation by Inhibiting Primary and Secondary Nucleation.
    Beeg M, Stravalaci M, Romeo M, Carrá AD, Cagnotto A, Rossi A, Diomede L, Salmona M, Gobbi M.
    J Biol Chem; 2016 Mar 25; 291(13):6958-66. PubMed ID: 26884339
    [Abstract] [Full Text] [Related]

  • 8. Clusterin is an extracellular chaperone that specifically interacts with slowly aggregating proteins on their off-folding pathway.
    Poon S, Treweek TM, Wilson MR, Easterbrook-Smith SB, Carver JA.
    FEBS Lett; 2002 Feb 27; 513(2-3):259-66. PubMed ID: 11904161
    [Abstract] [Full Text] [Related]

  • 9. In silico prediction of novel residues involved in amyloid primary nucleation of human I56T and D67H lysozyme.
    Griffin JWD, Bradshaw PC.
    BMC Struct Biol; 2018 Jul 20; 18(1):9. PubMed ID: 30029603
    [Abstract] [Full Text] [Related]

  • 10. Formation of amyloid aggregates from human lysozyme and its disease-associated variants using hydrostatic pressure.
    De Felice FG, Vieira MN, Meirelles MN, Morozova-Roche LA, Dobson CM, Ferreira ST.
    FASEB J; 2004 Jul 20; 18(10):1099-101. PubMed ID: 15155566
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  • 14. Suppression of apolipoprotein C-II amyloid formation by the extracellular chaperone, clusterin.
    Hatters DM, Wilson MR, Easterbrook-Smith SB, Howlett GJ.
    Eur J Biochem; 2002 Jun 20; 269(11):2789-94. PubMed ID: 12047389
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  • 16. Interaction of nonionic detergents with the specific sites of lysozyme amyloidogenic region - inhibition of amyloid fibrillization.
    Siposova K, Kozar T, Musatov A.
    Colloids Surf B Biointerfaces; 2017 Feb 01; 150():445-455. PubMed ID: 27842932
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  • 17. Insights into Kinetics of Agitation-Induced Aggregation of Hen Lysozyme under Heat and Acidic Conditions from Various Spectroscopic Methods.
    Chaari A, Fahy C, Chevillot-Biraud A, Rholam M.
    PLoS One; 2015 Feb 01; 10(11):e0142095. PubMed ID: 26571264
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