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Journal Abstract Search

183 related items for PubMed ID: 16925522

  • 21. Conformational inhibitors of protein aggregation.
    Fernández Ramírez MDC, Afrin S, Saelices L.
    Curr Opin Struct Biol; 2023 Dec; 83():102700. PubMed ID: 37717490
    [Abstract] [Full Text] [Related]

  • 22. Heterogeneous amyloid-formed ion channels as a common cytotoxic mechanism: implications for therapeutic strategies against amyloidosis.
    Kourie JI, Culverson AL, Farrelly PV, Henry CL, Laohachai KN.
    Cell Biochem Biophys; 2002 Dec; 36(2-3):191-207. PubMed ID: 12139405
    [Abstract] [Full Text] [Related]

  • 23. Molten globule precursor states are conformationally correlated to amyloid fibrils of human beta-2-microglobulin.
    Skora L, Becker S, Zweckstetter M.
    J Am Chem Soc; 2010 Jul 14; 132(27):9223-5. PubMed ID: 20565073
    [Abstract] [Full Text] [Related]

  • 24. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade.
    Chiti F, Dobson CM.
    Annu Rev Biochem; 2017 Jun 20; 86():27-68. PubMed ID: 28498720
    [Abstract] [Full Text] [Related]

  • 25. An emerging concept of prion infections as a form of transmissible cerebral amyloidosis.
    Lupi O, Peryassu MA.
    Prion; 2007 Jun 20; 1(4):223-7. PubMed ID: 19172115
    [Abstract] [Full Text] [Related]

  • 26. [Neurodegenerative conformational disease and its molecular bases].
    Li WW, Cai DF, Ren HM.
    Sheng Li Ke Xue Jin Zhan; 2006 Apr 20; 37(2):97-102. PubMed ID: 16850610
    [Abstract] [Full Text] [Related]

  • 27. The role of β-amyloid peptide in neurodegenerative diseases.
    Maltsev AV, Bystryak S, Galzitskaya OV.
    Ageing Res Rev; 2011 Sep 20; 10(4):440-52. PubMed ID: 21406255
    [Abstract] [Full Text] [Related]

  • 28. Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro.
    McParland VJ, Kad NM, Kalverda AP, Brown A, Kirwin-Jones P, Hunter MG, Sunde M, Radford SE.
    Biochemistry; 2000 Aug 01; 39(30):8735-46. PubMed ID: 10913285
    [Abstract] [Full Text] [Related]

  • 29. Protein conformational misfolding and amyloid formation: characteristics of a new class of disorders that include Alzheimer's and Prion diseases.
    Thompson AJ, Barrow CJ.
    Curr Med Chem; 2002 Oct 01; 9(19):1751-62. PubMed ID: 12369885
    [Abstract] [Full Text] [Related]

  • 30. Conformational changes and aggregation of expanded polyglutamine proteins as therapeutic targets of the polyglutamine diseases: exposed beta-sheet hypothesis.
    Nagai Y, Popiel HA.
    Curr Pharm Des; 2008 Oct 01; 14(30):3267-79. PubMed ID: 19075705
    [Abstract] [Full Text] [Related]

  • 31. [Amyloidosis: a model of misfolded protein disorder].
    Grateau G, Verine J, Delpech M, Ries M.
    Med Sci (Paris); 2005 Oct 01; 21(6-7):627-33. PubMed ID: 15985206
    [Abstract] [Full Text] [Related]

  • 32. Amyloid peptide pores and the beta sheet conformation.
    Kagan BL, Thundimadathil J.
    Adv Exp Med Biol; 2010 Oct 01; 677():150-67. PubMed ID: 20687488
    [Abstract] [Full Text] [Related]

  • 33. A minimal conformational switching-dependent model for amyloid self-assembly.
    Ranganathan S, Ghosh D, Maji SK, Padinhateeri R.
    Sci Rep; 2016 Feb 17; 6():21103. PubMed ID: 26883720
    [Abstract] [Full Text] [Related]

  • 34. Chemical chaperone and inhibitor discovery: potential treatments for protein conformational diseases.
    Zhao JH, Liu HL, Lin HY, Huang CH, Fang HW, Chen SS, Ho Y, Tsai WB, Chen WY.
    Perspect Medicin Chem; 2007 Dec 11; 1():39-48. PubMed ID: 19812735
    [Abstract] [Full Text] [Related]

  • 35. Dissection of conformational conversion events during prion amyloid fibril formation using hydrogen exchange and mass spectrometry.
    Singh J, Udgaonkar JB.
    J Mol Biol; 2013 Sep 23; 425(18):3510-21. PubMed ID: 23811055
    [Abstract] [Full Text] [Related]

  • 36. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways.
    Kelly JW.
    Curr Opin Struct Biol; 1998 Feb 23; 8(1):101-6. PubMed ID: 9519302
    [Abstract] [Full Text] [Related]

  • 37. Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways In Vivo.
    Annamalai K, Liberta F, Vielberg MT, Close W, Lilie H, Gührs KH, Schierhorn A, Koehler R, Schmidt A, Haupt C, Hegenbart U, Schönland S, Schmidt M, Groll M, Fändrich M.
    Angew Chem Int Ed Engl; 2017 Jun 19; 56(26):7510-7514. PubMed ID: 28544119
    [Abstract] [Full Text] [Related]

  • 38. Protein aggregation and its consequences for human disease.
    Dobson CM.
    Protein Pept Lett; 2006 Jun 19; 13(3):219-27. PubMed ID: 16515449
    [Abstract] [Full Text] [Related]

  • 39.
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  • 40. Learnings from Protein Folding Projected onto Amyloid Misfolding.
    Sreenivasan S, Narayan M.
    ACS Chem Neurosci; 2019 Sep 18; 10(9):3911-3913. PubMed ID: 31456389
    [Abstract] [Full Text] [Related]

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