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Journal Abstract Search

457 related items for PubMed ID: 29935976

  • 1.
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  • 2. Self-assembly of recombinant prion protein of 106 residues.
    Baskakov IV, Aagaard C, Mehlhorn I, Wille H, Groth D, Baldwin MA, Prusiner SB, Cohen FE.
    Biochemistry; 2000 Mar 14; 39(10):2792-804. PubMed ID: 10704232
    [Abstract] [Full Text] [Related]

  • 3. A valine-to-lysine substitution at position 210 induces structural conversion of prion protein into a β-sheet rich oligomer.
    Kakuda K, Yamaguchi KI, Kuwata K, Honda R.
    Biochem Biophys Res Commun; 2018 Nov 17; 506(1):81-86. PubMed ID: 30336980
    [Abstract] [Full Text] [Related]

  • 4. Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics.
    Viles JH, Donne D, Kroon G, Prusiner SB, Cohen FE, Dyson HJ, Wright PE.
    Biochemistry; 2001 Mar 06; 40(9):2743-53. PubMed ID: 11258885
    [Abstract] [Full Text] [Related]

  • 5. Preventing misfolding of the prion protein by trimethylamine N-oxide.
    Bennion BJ, DeMarco ML, Daggett V.
    Biochemistry; 2004 Oct 19; 43(41):12955-63. PubMed ID: 15476389
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  • 7. Detailed biophysical characterization of the acid-induced PrP(c) to PrP(β) conversion process.
    Bjorndahl TC, Zhou GP, Liu X, Perez-Pineiro R, Semenchenko V, Saleem F, Acharya S, Bujold A, Sobsey CA, Wishart DS.
    Biochemistry; 2011 Feb 22; 50(7):1162-73. PubMed ID: 21189021
    [Abstract] [Full Text] [Related]

  • 8. Aggregation and fibrillization of the recombinant human prion protein huPrP90-231.
    Swietnicki W, Morillas M, Chen SG, Gambetti P, Surewicz WK.
    Biochemistry; 2000 Jan 18; 39(2):424-31. PubMed ID: 10631004
    [Abstract] [Full Text] [Related]

  • 9. Prion protein oligomer and its neurotoxicity.
    Huang P, Lian F, Wen Y, Guo C, Lin D.
    Acta Biochim Biophys Sin (Shanghai); 2013 Jun 18; 45(6):442-51. PubMed ID: 23557632
    [Abstract] [Full Text] [Related]

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  • 11. Disassociation of β1-α1-β2 from the α2-α3 domain of prion protein (PrP) is a prerequisite for the conformational conversion of PrPC into PrPSc: Driven by the free energy landscape.
    Chandrasekaran P, Santosh Kumar C, Rangachari K, Sekar K.
    Int J Biol Macromol; 2019 Sep 01; 136():368-376. PubMed ID: 31207327
    [Abstract] [Full Text] [Related]

  • 12. The pH-triggered conversion of the PrP(c) to PrP(sc.).
    Zhou GP, Huang RB.
    Curr Top Med Chem; 2013 Sep 01; 13(10):1152-63. PubMed ID: 23647538
    [Abstract] [Full Text] [Related]

  • 13. Molecular Mechanism of the Misfolding and Oligomerization of the Prion Protein: Current Understanding and Its Implications.
    Singh J, Udgaonkar JB.
    Biochemistry; 2015 Jul 28; 54(29):4431-42. PubMed ID: 26171558
    [Abstract] [Full Text] [Related]

  • 14. Method for Folding of Recombinant Prion Protein to Soluble β-Sheet Secondary Structure.
    Ellett LJ.
    Methods Mol Biol; 2017 Jul 28; 1658():23-26. PubMed ID: 28861779
    [Abstract] [Full Text] [Related]

  • 15. Molecular architecture of human prion protein amyloid: a parallel, in-register beta-structure.
    Cobb NJ, Sönnichsen FD, McHaourab H, Surewicz WK.
    Proc Natl Acad Sci U S A; 2007 Nov 27; 104(48):18946-51. PubMed ID: 18025469
    [Abstract] [Full Text] [Related]

  • 16. The H187R mutation of the human prion protein induces conversion of recombinant prion protein to the PrP(Sc)-like form.
    Hosszu LL, Tattum MH, Jones S, Trevitt CR, Wells MA, Waltho JP, Collinge J, Jackson GS, Clarke AR.
    Biochemistry; 2010 Oct 12; 49(40):8729-38. PubMed ID: 20718410
    [Abstract] [Full Text] [Related]

  • 17. Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations.
    Jackson GS, Hosszu LL, Power A, Hill AF, Kenney J, Saibil H, Craven CJ, Waltho JP, Clarke AR, Collinge J.
    Science; 1999 Mar 19; 283(5409):1935-7. PubMed ID: 10082469
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  • 19. In Vitro Approach To Identify Key Amino Acids in Low Susceptibility of Rabbit Prion Protein to Misfolding.
    Eraña H, Fernández-Borges N, Elezgarai SR, Harrathi C, Charco JM, Chianini F, Dagleish MP, Ortega G, Millet Ó, Castilla J.
    J Virol; 2017 Dec 15; 91(24):. PubMed ID: 28978705
    [Abstract] [Full Text] [Related]

  • 20. DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation.
    Cordeiro Y, Machado F, Juliano L, Juliano MA, Brentani RR, Foguel D, Silva JL.
    J Biol Chem; 2001 Dec 28; 276(52):49400-9. PubMed ID: 11604397
    [Abstract] [Full Text] [Related]

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