Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Altered glycosylated PrP proteins can have different neuronal trafficking in brain but do not acquire scrapie-like properties.

The Journal of biological chemistry - 30 Dec 2005

Cancellotti Enrico, Wiseman Frances, Tuzi Nadia L, Baybutt Herbert, Monaghan Paul, Aitchison Lorraine, Simpson Jennifer, Manson Jean C

Abstract excerpt

N-Linked glycans have been shown to have an important role in the cell biology of a variety of cell surface glycoproteins, including PrP protein. It has been suggested that glycosylation of PrP can influence the susceptibility to transmissible spongiform encephalopathy and determine the characteristics of the many different strains observed in this particular type of disease. To understand the role of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Asparagine
Share to Carbohydrates

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Detergents

Share to Endopeptidase K

Share to Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase

Share to Polysaccharides

Share to Scrapie

Share to Type C Phospholipases

Source

Identifiers

PMID: 16219759
DOI: 10.1074/jbc.M509557200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Altered glycosylated PrP proteins can have different neuronal trafficking in brain but do not acquire scrapie-like properties.PMID 16219759Read ↗

Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform encephalopathy and scrapie infections.Semantic proximity Read ↗

Loss of glycosylation associated with the T183A mutation in human prion disease.Semantic proximity Read ↗

GFP-tagged prion protein is correctly localized and functionally active in the brains of transgenic mice.Semantic proximity Read ↗

The Glycosylation Status of PrP <sup>C</sup> Is a Key Factor in Determining Transmissible Spongiform Encephalopathy Transmission between SpeciesSemantic proximity Read ↗

Neurodegenerative illness in transgenic mice expressing a transmembrane form of the prion protein.Semantic proximity Read ↗

Thr but Asn of the N-glycosylation sites of PrP is indispensable for its misfolding.Semantic proximity Read ↗

Cellular prion proteins in human platelets show a phenotype different to those in brain tissues.Semantic proximity Read ↗

Selective processing and metabolism of disease-causing mutant prion proteins.Semantic proximity Read ↗

The role of host PrP in Transmissible Spongiform Encephalopathies.Semantic proximity Read ↗

Intracellular accumulation of a 46 kDa species of mouse prion protein as a result of loss of glycosylation in cultured mammalian cells.Semantic proximity Read ↗

A transmembrane form of the prion protein is localized in the Golgi apparatus of neurons.Semantic proximity Read ↗

Heterogeneity of normal prion protein in two‐dimensional immunoblot: presence of various glycosylated and truncated formsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.