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Journal Abstract Search

245 related items for PubMed ID: 24920162

  • 1. Cold denaturation of α-synuclein amyloid fibrils.
    Ikenoue T, Lee YH, Kardos J, Saiki M, Yagi H, Kawata Y, Goto Y.
    Angew Chem Int Ed Engl; 2014 Jul 21; 53(30):7799-804. PubMed ID: 24920162
    [Abstract] [Full Text] [Related]

  • 2. Protein denaturation and aggregation: Cellular responses to denatured and aggregated proteins.
    Meredith SC.
    Ann N Y Acad Sci; 2005 Dec 21; 1066():181-221. PubMed ID: 16533927
    [Abstract] [Full Text] [Related]

  • 3. Kinetically controlled thermal response of beta2-microglobulin amyloid fibrils.
    Sasahara K, Naiki H, Goto Y.
    J Mol Biol; 2005 Sep 23; 352(3):700-11. PubMed ID: 16098535
    [Abstract] [Full Text] [Related]

  • 4. Dissociation of amyloid fibrils of alpha-synuclein in supercooled water.
    Kim HY, Cho MK, Riedel D, Fernandez CO, Zweckstetter M.
    Angew Chem Int Ed Engl; 2008 Sep 23; 47(27):5046-8. PubMed ID: 18521826
    [No Abstract] [Full Text] [Related]

  • 5. The thermodynamic stability of amyloid fibrils studied by differential scanning calorimetry.
    Morel B, Varela L, Conejero-Lara F.
    J Phys Chem B; 2010 Mar 25; 114(11):4010-9. PubMed ID: 20199038
    [Abstract] [Full Text] [Related]

  • 6. Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry.
    Kardos J, Yamamoto K, Hasegawa K, Naiki H, Goto Y.
    J Biol Chem; 2004 Dec 31; 279(53):55308-14. PubMed ID: 15494406
    [Abstract] [Full Text] [Related]

  • 7. Reversible heat-induced dissociation of β2-microglobulin amyloid fibrils.
    Kardos J, Micsonai A, Pál-Gábor H, Petrik É, Gráf L, Kovács J, Lee YH, Naiki H, Goto Y.
    Biochemistry; 2011 Apr 19; 50(15):3211-20. PubMed ID: 21388222
    [Abstract] [Full Text] [Related]

  • 8. Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.
    Kim HY, Heise H, Fernandez CO, Baldus M, Zweckstetter M.
    Chembiochem; 2007 Sep 24; 8(14):1671-4. PubMed ID: 17722123
    [No Abstract] [Full Text] [Related]

  • 9. Thioflavin T-Silent Denaturation Intermediates Support the Main-Chain-Dominated Architecture of Amyloid Fibrils.
    Noda S, So M, Adachi M, Kardos J, Akazawa-Ogawa Y, Hagihara Y, Goto Y.
    Biochemistry; 2016 Jul 19; 55(28):3937-48. PubMed ID: 27345358
    [Abstract] [Full Text] [Related]

  • 10. The fold preference and thermodynamic stability of α-synuclein fibrils is encoded in the non-amyloid-β component region.
    Xu L, Bhattacharya S, Thompson D.
    Phys Chem Chem Phys; 2018 Feb 07; 20(6):4502-4512. PubMed ID: 29372732
    [Abstract] [Full Text] [Related]

  • 11. Main-chain dominated amyloid structures demonstrated by the effect of high pressure.
    Chatani E, Kato M, Kawai T, Naiki H, Goto Y.
    J Mol Biol; 2005 Sep 30; 352(4):941-51. PubMed ID: 16122756
    [Abstract] [Full Text] [Related]

  • 12. Studies of the aggregation of an amyloidogenic alpha-synuclein peptide fragment.
    Madine J, Doig AJ, Kitmitto A, Middleton DA.
    Biochem Soc Trans; 2005 Nov 30; 33(Pt 5):1113-5. PubMed ID: 16246058
    [Abstract] [Full Text] [Related]

  • 13. Structural stability of amyloid fibrils of beta(2)-microglobulin in comparison with its native fold.
    Chatani E, Goto Y.
    Biochim Biophys Acta; 2005 Nov 10; 1753(1):64-75. PubMed ID: 16213801
    [Abstract] [Full Text] [Related]

  • 14. The fold of alpha-synuclein fibrils.
    Vilar M, Chou HT, Lührs T, Maji SK, Riek-Loher D, Verel R, Manning G, Stahlberg H, Riek R.
    Proc Natl Acad Sci U S A; 2008 Jun 24; 105(25):8637-42. PubMed ID: 18550842
    [Abstract] [Full Text] [Related]

  • 15. AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin.
    Raman B, Ban T, Sakai M, Pasta SY, Ramakrishna T, Naiki H, Goto Y, Rao ChM.
    Biochem J; 2005 Dec 15; 392(Pt 3):573-81. PubMed ID: 16053447
    [Abstract] [Full Text] [Related]

  • 16. Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity.
    Rekas A, Adda CG, Andrew Aquilina J, Barnham KJ, Sunde M, Galatis D, Williamson NA, Masters CL, Anders RF, Robinson CV, Cappai R, Carver JA.
    J Mol Biol; 2004 Jul 23; 340(5):1167-83. PubMed ID: 15236975
    [Abstract] [Full Text] [Related]

  • 17. The role of the acidic domain of α-synuclein in amyloid fibril formation: a molecular dynamics study.
    Park S, Yoon J, Jang S, Lee K, Shin S.
    J Biomol Struct Dyn; 2016 Jul 23; 34(2):376-83. PubMed ID: 25869255
    [Abstract] [Full Text] [Related]

  • 18. Fibrils with parallel in-register structure constitute a major class of amyloid fibrils: molecular insights from electron paramagnetic resonance spectroscopy.
    Margittai M, Langen R.
    Q Rev Biophys; 2008 Jul 23; 41(3-4):265-97. PubMed ID: 19079806
    [Abstract] [Full Text] [Related]

  • 19. Role of different regions of alpha-synuclein in the assembly of fibrils.
    Qin Z, Hu D, Han S, Hong DP, Fink AL.
    Biochemistry; 2007 Nov 20; 46(46):13322-30. PubMed ID: 17963364
    [Abstract] [Full Text] [Related]

  • 20. The monomer-seed interaction mechanism in the formation of the β2-microglobulin amyloid fibril clarified by solution NMR techniques.
    Yanagi K, Sakurai K, Yoshimura Y, Konuma T, Lee YH, Sugase K, Ikegami T, Naiki H, Goto Y.
    J Mol Biol; 2012 Sep 21; 422(3):390-402. PubMed ID: 22683352
    [Abstract] [Full Text] [Related]

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