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

Neutralizing Mutations Significantly Inhibit Amyloid Formation by Human Prion Protein and Decrease Its Cytotoxicity.

Journal of molecular biology - 14 Feb 2020

Huang Jun-Jie, Li Xiang-Ning, Liu Wan-Li, Yuan Han-Ye, Gao Yuan, Wang Kan, Tang Bo, Pang Dai-Wen, Chen Jie, Liang Yi

Abstract excerpt

Prion diseases, such as Creutzfeldt-Jakob disease and bovine spongiform encephalopathy, are fatal neurodegenerative diseases that affect many mammals including humans and are caused by the misfolding of prion protein (PrP). A naturally occurring protective polymorphism G127V in human PrP has recently been found to significantly attenuate prion diseases, but the mechanism has remained elusive. We herein report...

Read the complete abstract on PubMed

Topics

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

Share to Amyloid
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen-Ion Concentration

Share to Mutation

Share to Prion Proteins

Share to Prions

Share to Protein Aggregates

Share to Spectroscopy, Fourier Transform Infrared

Source

Identifiers

PMID: 31821812
DOI: 10.1016/j.jmb.2019.11.020

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

Neutralizing Mutations Significantly Inhibit Amyloid Formation by Human Prion Protein and Decrease Its Cytotoxicity.PMID 31821812Read ↗

Protective V127 prion variant prevents prion disease by interrupting the formation of dimer and fibril from molecular dynamics simulations.Semantic proximity Read ↗

Atomic insights into the effects of pathological mutants through the disruption of hydrophobic core in the prion protein.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 ↗

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

Prion proteins with pathogenic and protective mutations show similar structure and dynamics.Semantic proximity Read ↗

Distinct effects of mutations on biophysical properties of human prion protein monomers and oligomers.Semantic proximity Read ↗

The G127V variant of the prion protein interferes with dimer formation in vitro but not in cellulo.Semantic proximity Read ↗

Biophysical characterization of oligomerization and fibrillization of the G131V pathogenic mutant of human prion protein.Semantic proximity Read ↗

A self-complementary recombinant adeno-associated virus vector coding for an anchorless prion protein carrying the G127V mutation extends survival in a rodent prion disease model.Semantic proximity Read ↗

The charge structure of helix 1 in the prion protein regulates conversion to pathogenic PrPSc.Semantic proximity Read ↗

Leveraging the dominant-negative effect of the kuru-protective G127V prion protein variant as a novel therapeutic strategySemantic proximity Read ↗

The N-terminal, polybasic region is critical for prion protein neuroprotective activity.Semantic proximity Read ↗

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