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

Trans-species amplification of PrPCWD and correlation with rigid loop 170N

10 Mar 2009

Abstract excerpt

No abstract is available from the source.

Read the complete abstract on PubMed

Topics

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

Share to Food Allergy and Anaphylaxis Research
Share to Neurological diseases and metabolism
Share to Prion Diseases and Protein Misfolding

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 19269662
DOI: 10.1016/j.virol.2009.02.025

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Trans-species amplification of PrPCWD and correlation with rigid loop 170NPMID 19269662Read ↗

Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.Semantic proximity Read ↗

Prion diseases: from transmission experiments to structural biology--still searching for the cause.Semantic proximity Read ↗

Toward the molecular basis of inherited prion diseases: NMR structure of the human prion protein with V210I mutation.Semantic proximity Read ↗

TSE agent strains and PrP: reconciling structure and functionSemantic proximity Read ↗

A structural overview of the vertebrate prion proteins.Semantic proximity Read ↗

N-terminal helix-cap in α-helix 2 modulates β-state misfolding in rabbit and hamster prion proteins.Semantic proximity Read ↗

The Pathogenic Mutation T182A Converts the Prion Protein into a Molten Globule-like Conformation Whose Misfolding to Oligomers but Not to Fibrils Is Drastically Accelerated.Semantic proximity Read ↗

Expanding the prion model for the yeast [PSI+] element.Semantic proximity Read ↗

Chimeric Peptide Species Contribute to Divergent Dipeptide Repeat Pathology in c9ALS/FTD and SCA36Semantic proximity Read ↗

Directed Evolution of an Anti-prion Protein scFv Fragment to an Affinity of 1 pM and its Structural InterpretationSemantic proximity Read ↗

The three-dimensional structure of prion protein: implications for prion disease.Semantic proximity Read ↗

The unfolding of the prion protein sheds light on the mechanisms of prion susceptibility and species barrier.Semantic proximity Read ↗

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