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

Redox induces diverse effects on recombinant human wild-type PrP and mutated PrP with inserted or deleted octarepeats.

International journal of molecular medicine - 1 Apr 2018

Shi Qi, Chen Cao, Zhang Bao-Yun, Zhou Wei, Xiao Kang, Dong Xiao-Ping

Abstract excerpt

Normal prion protein (PrP) contains two cysteines at amino acids 179 and 214, which may form intra‑ and interpeptide disulfide bonds. To determine the possible effects of this disulfide bridge on the biochemical features of PrP, prokaryotic recombinant human wild‑type PrP (PG5), and mutated PrPs with seven extra octarepeats (PG12) or with all five octarepeats removed (PG0), were subjected to redox in vitro....

Read the complete abstract on PubMed

Topics

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

Share to Endopeptidase K
Share to Mutagenesis, Insertional

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oxidation-Reduction

Share to Prion Proteins

Share to Protein Structure, Secondary

Share to Recombinant Proteins

Share to Repetitive Sequences, Amino Acid

Share to Sequence Deletion

Source

Identifiers

PMID: 29393338
DOI: 10.3892/ijmm.2018.3441

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

Redox induces diverse effects on recombinant human wild-type PrP and mutated PrP with inserted or deleted octarepeats.PMID 29393338Read ↗

PrP mutants with different numbers of octarepeat sequences are more susceptible to the oxidative stress.Semantic proximity Read ↗

Reactive oxygen species-mediated beta-cleavage of the prion protein in the cellular response to oxidative stress.Semantic proximity Read ↗

The Octarepeat Region of the Prion Protein Is Conformationally Altered in PrPScSemantic proximity Read ↗

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

The non-octarepeat copper binding site of the prion protein is a key regulator of prion conversion.Semantic proximity Read ↗

The expanded octarepeat domain selectively binds prions and disrupts homomeric prion protein interactions.Semantic proximity Read ↗

Neurometals in the Pathogenesis of Prion DiseasesSemantic proximity Read ↗

Prion protein with a mutant N-terminal octarepeat region undergoes cobalamin-dependent assembly into high-molecular weight complexes.Semantic proximity Read ↗

Prion proteins with insertion mutations have altered N-terminal conformation and increased ligand binding activity and are more susceptible to oxidative attack.Semantic proximity Read ↗

Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism.Semantic proximity Read ↗

A 3-disulfide mutant of mouse prion protein expression, oxidative folding, reductive unfolding, conformational stability, aggregation and isomerization.Semantic proximity Read ↗

Methionine oxidation accelerates the aggregation and enhances the neurotoxicity of the D178N variant of the human prion protein.Semantic proximity Read ↗

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