AAAAAA

   
Results: 1-25 | 26-50 | 51-62
Results: 1-25/62
Structural intermediates in the putative pathway from the cellular prion protein to the pathogenic form
Authors: Jansen, K Schafer, O Birkmann, E Post, K Serban, H Prusiner, SB Riesner, D
Citation: K. Jansen et al., Structural intermediates in the putative pathway from the cellular prion protein to the pathogenic form, BIOL CHEM, 382(4), 2001, pp. 683-691
Engineering the prion protein using chemical synthesis
Authors: Ball, HL King, DS Cohen, FE Prusiner, SB Baldwin, MA
Citation: Hl. Ball et al., Engineering the prion protein using chemical synthesis, J PEPT RES, 58(5), 2001, pp. 357-374
Decreased MK-801 binding in discrete hippocampal regions of prion-infectedmice
Authors: Diez, M DeArmond, SJ Groth, D Prusiner, SB Hokfelt, T
Citation: M. Diez et al., Decreased MK-801 binding in discrete hippocampal regions of prion-infectedmice, NEUROBIOL D, 8(4), 2001, pp. 692-699
Conformational propagation with prion-like characteristics in a simple model of protein folding
Authors: Harrison, PM Chan, HS Prusiner, SB Cohen, FE
Citation: Pm. Harrison et al., Conformational propagation with prion-like characteristics in a simple model of protein folding, PROTEIN SCI, 10(4), 2001, pp. 819-835
Strain-specified relative conformational stability of the scrapie prion protein
Authors: Peretz, D Scott, MR Groth, D Williamson, RA Burton, DR Cohen, FE Prusiner, SB
Citation: D. Peretz et al., Strain-specified relative conformational stability of the scrapie prion protein, PROTEIN SCI, 10(4), 2001, pp. 854-863
Cryptic epitopes in N-terminally truncated prion protein are exposed in the full-length molecule: Dependence of conformation on pH
Authors: Matsunaga, Y Peretz, D Williamson, A Burton, D Mehlhorn, I Groth, D Cohen, FE Prusiner, SB Baldwin, MA
Citation: Y. Matsunaga et al., Cryptic epitopes in N-terminally truncated prion protein are exposed in the full-length molecule: Dependence of conformation on pH, PROTEINS, 44(2), 2001, pp. 110-118
A protease-resistant 61-residue prion peptide causes neurodegeneration in transgenic mice
Authors: Supattapone, S Bouzamondo, E Ball, HL Wille, H Nguyen, HOB Cohen, FE DeArmond, SJ Prusiner, SB Scott, M
Citation: S. Supattapone et al., A protease-resistant 61-residue prion peptide causes neurodegeneration in transgenic mice, MOL CELL B, 21(7), 2001, pp. 2608-2616
Induction of distinct [URE3] yeast prion strains
Authors: Schlumpberger, M Prusiner, SB Herskowitz, I
Citation: M. Schlumpberger et al., Induction of distinct [URE3] yeast prion strains, MOL CELL B, 21(20), 2001, pp. 7035-7046
Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form
Authors: Leclerc, E Peretz, D Ball, H Sakurai, H Legname, G Serban, A Prusiner, SB Burton, DR Williamson, RA
Citation: E. Leclerc et al., Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form, EMBO J, 20(7), 2001, pp. 1547-1554
Shattuck lecture - Neurodegenerative diseases and prions.
Authors: Prusiner, SB
Citation: Sb. Prusiner, Shattuck lecture - Neurodegenerative diseases and prions., N ENG J MED, 344(20), 2001, pp. 1516-1526
Antibodies inhibit prion propagation and clear cell cultures of prion infectivity
Authors: Peretz, D Williamson, RA Kaneko, K Vergara, J Leclerc, E Schmitt-Ulms, G Mehlhorn, IR Legname, G Wormald, MR Rudd, PM Dwek, RA Burton, DR Prusiner, SB
Citation: D. Peretz et al., Antibodies inhibit prion propagation and clear cell cultures of prion infectivity, NATURE, 412(6848), 2001, pp. 739-743
Two different neurodegenerative diseases caused by proteins with similar structures
Authors: Mo, HP Moore, RC Cohen, FE Westaway, D Prusiner, SB Wright, PE Dyson, HJ
Citation: Hp. Mo et al., Two different neurodegenerative diseases caused by proteins with similar structures, P NAS US, 98(5), 2001, pp. 2352-2357
Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration
Authors: Laws, DD Bitter, HML Liu, K Ball, HL Kaneko, K Wille, H Cohen, FE Prusiner, SB Pines, A Wemmer, DE
Citation: Dd. Laws et al., Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration, P NAS US, 98(20), 2001, pp. 11686-11690
Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease
Authors: Korth, C May, BCH Cohen, FE Prusiner, SB
Citation: C. Korth et al., Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease, P NAS US, 98(17), 2001, pp. 9836-9841
Copper-catalyzed oxidation of the recombinant SHa(29-231) prion protein
Authors: Requena, JR Groth, D Legname, G Stadtman, ER Prusiner, SB Levine, RL
Citation: Jr. Requena et al., Copper-catalyzed oxidation of the recombinant SHa(29-231) prion protein, P NAS US, 98(13), 2001, pp. 7170-7175
Branched polyamines cure prion-infected neuroblastoma cells
Authors: Supattapone, S Wille, H Uyechi, L Safar, J Tremblay, P Szoka, FC Cohen, FE Prusiner, SB Scott, MR
Citation: S. Supattapone et al., Branched polyamines cure prion-infected neuroblastoma cells, J VIROLOGY, 75(7), 2001, pp. 3453-3461
Identification of two prion protein regions that modify scrapie incubationtime
Authors: Supattapone, S Muramoto, T Legname, G Mehlhorn, I Cohen, FE DeArmond, SJ Prusiner, SB Scott, MR
Citation: S. Supattapone et al., Identification of two prion protein regions that modify scrapie incubationtime, J VIROLOGY, 75(3), 2001, pp. 1408-1413
Folding of prion protein to its native alpha-helical conformation is underkinetic control
Authors: Baskakov, IV Legname, G Prusiner, SB Cohen, FE
Citation: Iv. Baskakov et al., Folding of prion protein to its native alpha-helical conformation is underkinetic control, J BIOL CHEM, 276(23), 2001, pp. 19687-19690
Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics
Authors: Viles, JH Donne, D Kroon, G Prusiner, SB Cohen, FE Dyson, HJ Wright, PE
Citation: Jh. Viles et al., Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics, BIOCHEM, 40(9), 2001, pp. 2743-2753
Prion glycoprotein: Structure, dynamics, and roles for the sugars
Authors: Rudd, PM Wormald, MR Wing, DR Prusiner, SB Dwek, RA
Citation: Pm. Rudd et al., Prion glycoprotein: Structure, dynamics, and roles for the sugars, BIOCHEM, 40(13), 2001, pp. 3759-3766
Huntington disease phenocopy is a familial prion disease
Authors: Moore, RC Xiang, FQ Monaghan, J Han, D Zhang, ZP Edstrom, L Anvret, M Prusiner, SB
Citation: Rc. Moore et al., Huntington disease phenocopy is a familial prion disease, AM J HU GEN, 69(6), 2001, pp. 1385-1388
Scrapie infectivity is independent of amyloid staining properties of the N-terminally truncated prion protein
Authors: Wille, H Prusiner, SB Cohen, FE
Citation: H. Wille et al., Scrapie infectivity is independent of amyloid staining properties of the N-terminally truncated prion protein, J STRUCT B, 130(2-3), 2000, pp. 323-338
The prion domain of yeast Ure2p induces autocatalytic formation of amyloidfibers by a recombinant fusion protein
Authors: Schlumpberger, M Wille, H Baldwin, MA Butler, DA Herskowitz, I Prusiner, SB
Citation: M. Schlumpberger et al., The prion domain of yeast Ure2p induces autocatalytic formation of amyloidfibers by a recombinant fusion protein, PROTEIN SCI, 9(3), 2000, pp. 440-451
Copper binding to octarepeat peptides of the prion protein monitored by mass spectrometry
Authors: Whittal, RM Ball, HL Cohen, FE Burlingame, AL Prusiner, SB Baldwin, MA
Citation: Rm. Whittal et al., Copper binding to octarepeat peptides of the prion protein monitored by mass spectrometry, PROTEIN SCI, 9(2), 2000, pp. 332-343
Quantitative trait loci affecting prion incubation time in mice
Authors: Stephenson, DA Chiotti, K Ebeling, C Groth, D DeArmond, SJ Prusiner, SB Carlson, GA
Citation: Da. Stephenson et al., Quantitative trait loci affecting prion incubation time in mice, GENOMICS, 69(1), 2000, pp. 47-53
Risultati: 1-25 | 26-50 | 51-62