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

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

Biochemical and biophysical research communications - 16 May 2008

Ikeda Shino, Kobayashi Atsushi, Kitamoto Tetsuyuki

Abstract excerpt

Prion protein (PrP) contains two N-linked glycosylation sites. It is unknown which amino acid substitution contributes most efficiently to the abolishment of N-linked glycosylations. To define the influence of amino acid substitution at the N-linked glycosylation sites on the conversion efficiency of mouse PrP, we tested each of all 19 amino acid substitutions at either one of the N-linked glycosylation sites...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Asparagine
Share to Cell Line

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycosylation

Share to Prions

Share to Protein Folding

Share to Threonine

Source

Identifiers

PMID: 18343219
DOI: 10.1016/j.bbrc.2008.03.014

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Thr but Asn of the N-glycosylation sites of PrP is indispensable for its misfolding.PMID 18343219Read ↗

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 ↗

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

Mutagenesis studies in transgenic Xenopus intermediate pituitary cells reveal structural elements necessary for correct prion protein biosynthesis.Semantic proximity Read ↗

The interplay of glycosylation and disulfide formation influences fibrillization in a prion protein fragment.Semantic proximity Read ↗

Removal of the glycosylation of prion protein provokes apoptosis in SF126.Semantic proximity Read ↗

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

Identifying key components of the PrPC-PrPSc replicative interface.Semantic proximity Read ↗

Conservation of a glycine-rich region in the prion protein is required for uptake of prion infectivity.Semantic proximity Read ↗

V180I mutation of the prion protein gene associated with atypical PrPSc glycosylation.Semantic proximity Read ↗

Site-Specific Characterization of the N-Linked Glycans of Murine Prion Protein by High-Performance Liquid Chromatography/Electrospray Mass Spectrometry and Exoglycosidase DigestionsSemantic proximity Read ↗

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