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Article

Subcellular trafficking abnormalities of a prion protein with a disrupted disulfide loop.

FEBS letters - 22 Oct 1999

Yanai A, Meiner Z, Gahali I, Gabizon R, Taraboulos A

Abstract excerpt

The single disulfide loop (Cys178-Cys213) of the prion protein (PrP) may stabilize the conformation of this protein by bridging the C-terminal alpha-helices. The substitution mutant Cys178Ala fails to form the prion isoform PrPSc when expressed in scrapie-infected neuroblastoma ScN2a cells (Muramoto et al., Proc. Natl. Acad. Sci. USA 93, 15457-15462). To investigate the reasons for this failure, we introduced the...

Topics

Animals
CHO Cells
Cricetinae
Disulfides
Endopeptidase K
Fluorescent Antibody Technique
Hexosaminidases
Mice
Mutation
Neuroblastoma
PrPC Proteins
PrPSc Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation

Sarcosine

Scrapie

Solubility

Tumor Cells, Cultured

Source

Identifiers

PMID: 10571052
DOI: 10.1016/s0014-5793(99)01316-2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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