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

Highly neurotoxic monomeric α-helical prion protein

7 Feb 2012

Abstract excerpt

Prion diseases are infectious and belong to the group of protein misfolding neurodegenerative diseases. In these diseases, neuronal dysfunction and death are caused by the neuronal toxicity of a particular misfolded form of their cognate protein. The ability to specifically target the toxic protein conformer or the neuronal death pathway would provide powerful therapeutic approaches to these diseases. The...

Read the complete abstract on PubMed

Topics

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

Share to Alzheimer's disease research and treatments
Share to Neurological diseases and metabolism
Share to Prion Diseases and Protein Misfolding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 22323583
DOI: 10.1073/pnas.1118090109

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Highly neurotoxic monomeric α-helical prion proteinPMID 22323583Read ↗

Prion diseases: what is the neurotoxic molecule?Semantic proximity Read ↗

In Vivo Generation of Neurotoxic Prion Protein: Role for Hsp70 in Accumulation of Misfolded IsoformsSemantic proximity Read ↗

Prion neurotoxicity: insights from prion protein mutants.Semantic proximity Read ↗

Prions: generation and spread versus neurotoxicity.Semantic proximity Read ↗

Neuroprotective and neurotoxic signaling by the prion protein.Semantic proximity Read ↗

The Prion Basis of Progressive Neurodegenerative DisordersSemantic proximity Read ↗

Prion diseases: a riddle wrapped in a mystery inside an enigma.Semantic proximity Read ↗

The prion protein unstructured N‐terminal region is a broad‐spectrum molecular sensor with diverse and contrasting potential functionsSemantic proximity Read ↗

Reduced Abundance and Subverted Functions of Proteins in Prion-Like Diseases: Gained Functions Fascinate but Lost Functions Affect AetiologySemantic proximity Read ↗

Prions.Semantic proximity Read ↗

Prion Diseases: A Unique Transmissible Agent or a Model for Neurodegenerative Diseases?Semantic proximity Read ↗

Pathogenic mutations within the hydrophobic domain of the prion protein lead to the formation of protease-sensitive prion species with increased lethality.Semantic proximity Read ↗

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