Prion protein structural features indicate possible relations to signal peptidases
Open Access
- 24 April 1998
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 426 (3) , 291-296
- https://doi.org/10.1016/s0014-5793(98)00372-x
Abstract
Transmissible spongiform encephalopathies (TSEs) in mammalian species are believed to be caused by an oligomeric isoform, PrPSc, of the cellular prion protein, PrPC. One of the key questions in TSE r...Keywords
This publication has 43 references indexed in Scilit:
- Type II DNA topoisomerasesCurrent Opinion in Structural Biology, 1998
- Autonomous and Reversible Folding of a Soluble Amino-terminally Truncated Segment of the Mouse Prion ProteinJournal of Molecular Biology, 1996
- Structure of the UmuD′ protein and its regulation in response to DNA damageNature, 1996
- MOLMOL: A program for display and analysis of macromolecular structuresJournal of Molecular Graphics, 1996
- Copper Binding to the N-Terminal Tandem Repeat Region of Mammalian and Avian Prion Protein: Structural Studies Using Synthetic PeptidesBiochemical and Biophysical Research Communications, 1995
- Rescue of neurophysiological phenotype seen in PrP null mice by transgene encoding human prion proteinNature Genetics, 1995
- Identification of the Potential Active Site of the Signal Peptidase SipS of Bacillus subtilisPublished by Elsevier ,1995
- Prion Protein Gene Variation Among PrimatesJournal of Molecular Biology, 1995
- Novel Proteinaceous Infectious Particles Cause ScrapieScience, 1982
- Does the Agent of Scrapie Replicate without Nucleic Acid ?Nature, 1967