Substitutions at residue 211 in the prion protein drive a switch between CJD and GSS syndrome, a new mechanism governing inherited neurodegenerative disorders.

doi:10.1093/hmg/dds377

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

Community

Back to search

Article

Substitutions at residue 211 in the prion protein drive a switch between CJD and GSS syndrome, a new mechanism governing inherited neurodegenerative disorders.

Human molecular genetics - 15 Dec 2012

Peoc'h Katell, Levavasseur Etienne, Delmont Emilien, De Simone Alfonso, Laffont-Proust Isabelle, Privat Nicolas, Chebaro Yassmine, Chapuis Céline, Bedoucha Pierre, Brandel Jean-Philippe, Laquerriere Annie, Kemeny Jean-Louis, Hauw Jean-Jacques, Borg Michel, Rezaei Human, Derreumaux Philippe, Laplanche Jean-Louis, Haïk Stéphane

Abstract excerpt

Human prion diseases are a heterogeneous group of fatal neurodegenerative disorders, characterized by the deposition of the partially protease-resistant prion protein (PrP(res)), astrocytosis, neuronal loss and spongiform change in the brain. Among inherited forms that represent 15% of patients, different phenotypes have been described depending on the variations detected at different positions within the prion...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Creutzfeldt-Jakob Syndrome

Share to Gerstmann-Straussler-Scheinker Disease

Share to Molecular Dynamics Simulation

Share to Phosphorylation

Share to Plaque, Amyloid

Share to Prions

Share to Protein Conformation

Source

Open in PubMed

Identifiers

PMID: 22965875
DOI: 10.1093/hmg/dds377

Genes

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

Substitutions at residue 211 in the prion protein drive a switch between CJD and GSS syndrome, a new mechanism governing inherited neurodegenerative disorders.PMID 22965875Read ↗

The Prion Basis of Progressive Neurodegenerative DisordersSemantic proximity Read ↗

The prion diseases.Semantic proximity Read ↗

Detailed computational analysis revealed mutation V210I on PrP induced conformational conversion on β2-α2 loop and α2-α3.Semantic proximity Read ↗

Prions mediated neurodegenerative disorders.Semantic proximity Read ↗

Biology and Genetics of Prions Causing NeurodegenerationSemantic proximity Read ↗

Familial prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EMSemantic proximity Read ↗

Identification of three novel mutations (E196K, V203I, E211Q) in the prion protein gene (PRNP) in inherited prion diseases with Creutzfeldt-Jakob disease phenotype.Semantic proximity Read ↗

Molecular pathogenesis of sporadic prion diseases in man.Semantic proximity Read ↗

Mutation-Dependent Refolding of Prion Protein Unveils Amyloidogenic-Related Structural Ramifications: Insights from Molecular Dynamics Simulations.Semantic proximity Read ↗

Prion protein amyloidosis.Semantic proximity Read ↗

Search for a genetic cause of variably protease-sensitive prionopathySemantic proximity Read ↗

Different misfolding mechanisms converge on common conformational changes: human prion protein pathogenic mutants Y218N and E196K.Semantic proximity Read ↗

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