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Journal Abstract Search

326 related items for PubMed ID: 15377534

  • 1. Oligomerization of amyloid Abeta16-22 peptides using hydrogen bonds and hydrophobicity forces.
    Favrin G, Irbäck A, Mohanty S.
    Biophys J; 2004 Dec; 87(6):3657-64. PubMed ID: 15377534
    [Abstract] [Full Text] [Related]

  • 2. Stability and structure of oligomers of the Alzheimer peptide Abeta16-22: from the dimer to the 32-mer.
    Röhrig UF, Laio A, Tantalo N, Parrinello M, Petronzio R.
    Biophys J; 2006 Nov 01; 91(9):3217-29. PubMed ID: 16920832
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  • 3. Mechanistic insight into E22Q-mutation-induced antiparallel-to-parallel β-sheet transition of Aβ16-22 fibrils: an all-atom simulation study.
    Li X, Lei J, Qi R, Xie L, Wei G.
    Phys Chem Chem Phys; 2019 Jul 17; 21(28):15686-15694. PubMed ID: 31271401
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  • 4. Dissecting the assembly of Abeta16-22 amyloid peptides into antiparallel beta sheets.
    Klimov DK, Thirumalai D.
    Structure; 2003 Mar 17; 11(3):295-307. PubMed ID: 12623017
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  • 5. Effects of hydrophobic macromolecular crowders on amyloid β (16-22) aggregation.
    Latshaw DC, Hall CK.
    Biophys J; 2015 Jul 07; 109(1):124-34. PubMed ID: 26153709
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  • 6. Aggregation of beta-amyloid fragments.
    Meinke JH, Hansmann UH.
    J Chem Phys; 2007 Jan 07; 126(1):014706. PubMed ID: 17212510
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  • 7. Probing the role of backbone hydrogen bonding in beta-amyloid fibrils with inhibitor peptides containing ester bonds at alternate positions.
    Gordon DJ, Meredith SC.
    Biochemistry; 2003 Jan 21; 42(2):475-85. PubMed ID: 12525175
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  • 8. Molecular dynamics simulation of amyloid beta dimer formation.
    Urbanc B, Cruz L, Ding F, Sammond D, Khare S, Buldyrev SV, Stanley HE, Dokholyan NV.
    Biophys J; 2004 Oct 21; 87(4):2310-21. PubMed ID: 15454432
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  • 10. Beta2-microglobulin amyloid fragment organization and morphology and its comparison to Abeta suggests that amyloid aggregation pathways are sequence specific.
    Zheng J, Jang H, Nussinov R.
    Biochemistry; 2008 Feb 26; 47(8):2497-509. PubMed ID: 18215070
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  • 14. The role of phenolic OH groups of flavonoid compounds with H-bond formation ability to suppress amyloid mature fibrils by destabilizing β-sheet conformation of monomeric Aβ17-42.
    Andarzi Gargari S, Barzegar A, Tarinejad A.
    PLoS One; 2018 Feb 26; 13(6):e0199541. PubMed ID: 29953467
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  • 15. Simulation of molecular crowding effects on an Alzheimer's beta-amyloid peptide.
    Li X, Mehler EL.
    Cell Biochem Biophys; 2006 Feb 26; 46(2):123-41. PubMed ID: 17012754
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  • 17. Polymorphic fibril formation by residues 10-40 of the Alzheimer's beta-amyloid peptide.
    Paravastu AK, Petkova AT, Tycko R.
    Biophys J; 2006 Jun 15; 90(12):4618-29. PubMed ID: 16565054
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