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Article

Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein.

Journal of molecular biology - 25 Jun 1999

Wopfner F, Weidenhöfer G, Schneider R, von Brunn A, Gilch S, Schwarz T F, Werner T, Schätzl H M

Abstract excerpt

Prion diseases are fatal neurodegenerative disorders in man and animal associated with conformational conversion of a cellular prion protein (PrPc) into the pathologic isoform (PrPSc). The function of PrPcand the tertiary structure of PrPScare unclear. Various data indicate which parts of PrP might control the species barrier in prion diseases and the binding of putative factors to PrP. To elucidate these...

Topics

Amino Acid Sequence
Animals
Base Sequence
Birds
Cats
Conserved Sequence
DNA, Complementary
Dogs
Genetic Variation
Humans
Mammals
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Prions

Rodentia

Sequence Homology, Amino Acid

Source

Identifiers

PMID: 10373359
DOI: 10.1006/jmbi.1999.2831

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein.PMID 10373359Read ↗

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