2005 2004 2003 2002 2001 2000 1999 1998 1997 1996 1995 1994 1993 1992 1991
1990 <1990

 

Reference List:

    2001

     

  1. Mapping the early steps in the pH-induced conformational conversion of the prion protein.
    Alonso DO, DeArmond SJ, Cohen FE, Daggett V.
    Proc Natl Acad Sci U S A 2001, 98: 2985-9   Medline

     

  2. Engineering the prion protein using chemical synthesis.
    Ball HL, King DS, Cohen FE, Prusiner SB, Baldwin MA.
    J Pept Res 2001, 58: 357-74   Medline

     

  3. Folding of prion protein to its native alpha-helical conformation is under kinetic control.
    Baskakov IV, Legname G, Prusiner SB, Cohen FE.
    J Biol Chem 2001, 276: 19687-90   Medline

     

  4. Pairwise sequence alignment below the twilight zone.
    Blake JD, Cohen FE.
    J Mol Biol 2001, 307: 721-35   Medline

     

  5. Conformational propagation with prion-like characteristics in a simple model of protein folding.
    Harrison PM, Chan HS, Prusiner SB, Cohen FE.
    Protein Sci 2001, 10: 819-35   Medline

     

  6. Collecting and harvesting biological data: the GPCRDB and NucleaRDB information systems.
    Horn F, Vriend G, Cohen FE.
    Nucleic Acids Res 2001, 29: 346-9   Medline

     

  7. The impact of whole genome sequence data on drug discovery--a malaria case study.
    Joachimiak MP, Chang C, Rosenthal PJ, Cohen FE.
    Mol Med 2001, 7: 698-710   Medline

     

  8. Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease.
    Korth C, May BC, Cohen FE, Prusiner SB.
    Proc Natl Acad Sci U S A 2001, 98: 9836-41   Medline

     

  9. Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.
    Laws DD, Bitter HM, Liu K, Ball HL, Kaneko K, Wille H, Cohen FE, Prusiner SB, Pines A, Wemmer DE.
    Proc Natl Acad Sci U S A 2001, 98: 11686-90   Medline

     

  10. Cryptic epitopes in N-terminally truncated prion protein are exposed in the full-length molecule: dependence of conformation on pH.
    Matsunaga Y, Peretz D, Williamson A, Burton D, Mehlhorn I, Groth D, Cohen FE, Prusiner SB, Baldwin MA.
    Proteins 2001, 44: 110-8   Medline

     

  11. Two different neurodegenerative diseases caused by proteins with similar structures.
    Mo H, Moore RC, Cohen FE, Westaway D, Prusiner SB, Wright PE, Dyson HJ.
    Proc Natl Acad Sci U S A 2001, 98: 2352-7   Medline

     

  12. Strain-specified relative conformational stability of the scrapie prion protein.
    Peretz D, Scott MR, Groth D, Williamson RA, Burton DR, Cohen FE, Prusiner SB.
    Protein Sci 2001, 10: 854-63   Medline

     

  13. Die Konformation des Prion-Proteins codiert fuer quantitative Charakteristika von Prionstaemmen.
    Safar J,Cohen FE, Prusiner SB.
    In Prionen un Prionkrankheiten ed B Hornlimann D Reisner and H Kretzschmar Walter de Gruyter Berlin New-York 2001 pp. 132-138

     

  14. Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein.
    Schmitt-Ulms G, Legname G, Baldwin MA, Ball HL, Bradon N, Bosque PJ, Crossin KL, Edelman GM, DeArmond SJ, Cohen FE, Prusiner SB.
    J Mol Biol 2001, 314: 1209-25   Medline

     

  15. A protease-resistant 61-residue prion peptide causes neurodegeneration in transgenic mice.
    Supattapone S, Bouzamondo E, Ball HL, Wille H, Nguyen HO, Cohen FE, DeArmond SJ, Prusiner SB, Scott M.
    Mol Cell Biol 2001, 21: 2608-16   Medline

     

  16. Identification of two prion protein regions that modify scrapie incubation time.
    Supattapone S, Muramoto T, Legname G, Mehlhorn I, Cohen FE, DeArmond SJ, Prusiner SB, Scott MR.
    J Virol 2001, 75: 1408-13   Medline

     

  17. Branched polyamines cure prion-infected neuroblastoma cells.
    Supattapone S, Wille H, Uyechi L, Safar J, Tremblay P, Szoka FC, Cohen FE, Prusiner SB, Scott MR.
    J Virol 2001, 75: 3453-61   Medline

     

  18. 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, 40: 2743-53   Medline

     

     


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