Literature DB >> 1353727

Spontaneous conversion of PrPC to PrPSc.

E Sulkowski1.   

Abstract

Octa-repeats of prion proteins (PrP) contain histidine and tryptophan residues which are known to function as ligands for transition metals. It is proposed that the spontaneous conversion of the PrPC (cellular) isoform into PrPSc (scrapie) isoform may be triggered by the coordination of these metals.

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Year:  1992        PMID： 1353727     DOI： 10.1016/0014-5793(92)80750-b

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  3 in total

1.  Copper binding to the prion protein: structural implications of four identical cooperative binding sites.

Authors:  J H Viles; F E Cohen; S B Prusiner; D B Goodin; P E Wright; H J Dyson
Journal:  Proc Natl Acad Sci U S A       Date:  1999-03-02       Impact factor: 11.205

2.  Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy.

Authors:  E Aronoff-Spencer; C S Burns; N I Avdievich; G J Gerfen; J Peisach; W E Antholine; H L Ball; F E Cohen; S B Prusiner; G L Millhauser
Journal:  Biochemistry       Date:  2000-11-14       Impact factor: 3.162

Review 3.  Inhibition of scrapie-associated PrP accumulation. Probing the role of glycosaminoglycans in amyloidogenesis.

Authors:  S A Priola; B Caughey
Journal:  Mol Neurobiol       Date:  1994 Apr-Jun       Impact factor: 5.590
  3 in total

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