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Prion protein isoform interactions

Horiuchi, M., Baron, G. S., Xiong, L. W., and Caughey, B. (2001). Inhibition of interactions and interconversions of prion protein isoforms by peptide fragments from the C-terminal folded domain./. Biol. Chem. 276, 15489-15497. [Pg.208]

Caughey B (2001) Interactions between prion protein isoforms the kiss of death Trends Biochem Sci 26 235-242... [Pg.166]

Prions—protein particles that lack nucleic acid— cause fatal transmissible spongiform encephalopathies such as Creutzfeldt-Jakob disease, scrapie, and bovine spongiform encephalopathy. Prion diseases involve an altered secondary-tertiary strucmre of a namrally occurring protein, PrPc. When PrPc interacts with its pathologic isoform PrPSc, its conformation is transformed from a predominantly a-helical strucmre to the P-sheet strucmre characteristic of PrPSc. [Pg.39]

According to the protein-only hypothesis, proposed by Prusiner (Fig. 5), the interaction of the cellular prion protein with the pathological isoform seems to be the crucial step in the conversion of PrP = to PrP . The existence of the hypothetical PrP =/PrP heterodimer may require the presence of a homodimer consisting of two PrP = molecules. This homodimer is thought to be in equilibrium with the PrP monomers. It is unclear to date wether the spontaneous conversion reaction involves PrP monomers or the PrP homodimers. [Pg.248]


See other pages where Prion protein isoform interactions is mentioned: [Pg.139]    [Pg.141]    [Pg.143]    [Pg.145]    [Pg.147]    [Pg.149]    [Pg.151]    [Pg.153]    [Pg.155]    [Pg.157]    [Pg.159]    [Pg.163]    [Pg.165]    [Pg.167]    [Pg.169]    [Pg.419]    [Pg.26]    [Pg.292]    [Pg.395]    [Pg.701]    [Pg.127]    [Pg.240]   
See also in sourсe #XX -- [ Pg.248 , Pg.249 , Pg.250 ]




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Isoforms

Prion protein

Prion proteins interaction

Prions

Protein isoform

Proteins isoforms

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