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

Structural features of human DJ-1 in distinct Cys106 oxidative states and their relevance to its loss of function in disease.

Biochimica et biophysica acta. General subjects - 1 Nov 2017

Kiss Róbert, Zhu Max, Jójárt Balázs, Czajlik András, Solti Katalin, Fórizs Balázs, Nagy Éva, Zsila Ferenc, Beke-Somfai Tamás, Tóth Gergely

Abstract excerpt

DJ-1 (PARK7) is a multifunctional protein linked to the onset and progression of a number of diseases, most of which are associated with high oxidative stress. The Cys106 of DJ-1 is unusually reactive and thus sensitive to oxidation, and due to high oxidative stress it was observed to be in various oxidized states in disease condition. The oxidation state of Cys106 of DJ-1 is believed to determine the specific...

Read the complete abstract on PubMed

Topics

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

Share to Biophysical Phenomena
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Oxidation-Reduction

Share to Oxidative Stress

Share to Protein Conformation

Share to Protein Deglycase DJ-1

Source

Identifiers

PMID: 28844983
DOI: 10.1016/j.bbagen.2017.08.017

Genes

PARK7

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

Structural features of human DJ-1 in distinct Cys106 oxidative states and their relevance to its loss of function in disease.PMID 28844983Read ↗

Roles of distinct cysteine residues in S-nitrosylation and dimerization of DJ-1.Semantic proximity Read ↗

Engineered disulfide bonds restore chaperone-like function of DJ-1 mutants linked to familial Parkinson's disease.Semantic proximity Read ↗

Use of cysteine-reactive cross-linkers to probe conformational flexibility of human DJ-1 demonstrates that Glu18 mutations are dimers.Semantic proximity Read ↗

Effect of single amino acid substitution on oxidative modifications of the Parkinson's disease-related protein, DJ-1.Semantic proximity Read ↗

Formation of a stabilized cysteine sulfinic acid is critical for the mitochondrial function of the parkinsonism protein DJ-1.Semantic proximity Read ↗

Structural Impact of Three Parkinsonism-Associated Missense Mutations on Human DJ-1,Semantic proximity Read ↗

On the oligomeric state of DJ-1 protein and its mutants associated with Parkinson Disease. A combined computational and in vitro study.Semantic proximity Read ↗

Structural Biology of the DJ-1 Superfamily.Semantic proximity Read ↗

Mechanism of BAG1 repair on Parkinson's disease-linked DJ1 mutation.Semantic proximity Read ↗

Distinct Mechanisms of Pathogenic DJ-1 Mutations in Mitochondrial Quality ControlSemantic proximity Read ↗

A novel splicing variant of DJ-1 in Parkinson's disease induces mitochondrial dysfunctionSemantic proximity Read ↗

The 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease.Semantic proximity Read ↗

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