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

The oxidative nuclease activity of human cytochrome c with mutations in Ω-loop C/D.

Biochimica et biophysica acta. Proteins and proteomics - 1 May 2023

Feng Yu, Dong Yao, Du Ke-Jie, Liu Xi-Chun, Gao Shu-Qin, Lin Ying-Wu

Abstract excerpt

Natural and artificial nucleases have extensive applications in biotechnology and biomedicine. The exploration of protein with potential DNA cleavage activity also inspires the design of artificial nuclease and helps to understand the physiological process of DNA damage. In this study, we engineered four human cytochrome c (Cyt c) mutants (N52S, N52A, I81N, and I81D Cyt c), which showed enhanced DNA cleavage...

Read the complete abstract on PubMed

Topics

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

Share to Cytochromes c
Share to Mutation
Share to Oxidation-Reduction

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oxidative Stress

Share to Superoxides

Source

Identifiers

PMID: 36642204
DOI: 10.1016/j.bbapap.2023.140897

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

The oxidative nuclease activity of human cytochrome c with mutations in Ω-loop C/D.PMID 36642204Read ↗

Influence of cysteine-directed mutations at the Ω-loops on peroxidase activity of human cytochrome c.Semantic proximity Read ↗

Molecular insights on the conformational dynamics of a P76C mutant of human cytochrome c and the enhancement on its peroxidase activity.Semantic proximity Read ↗

Cytochrome C mutants for superoxide biosensors.Semantic proximity Read ↗

Mutant Cytochrome C as a Potential Detector of Superoxide Generation: Effect of Mutations on the Function and Properties.Semantic proximity Read ↗

The Increase in the Peroxidase Activity of the Cytochrome C with Substitutions in the Universal Binding Site Is Associated with Changes in the Ability to Interact with External Ligands.Semantic proximity Read ↗

Mutation T71R enhanced the structural stability and functional activity of wild type superoxide dismutase cloned from soil metagenome.Semantic proximity Read ↗

Production of Human Cu,Zn SOD with Higher Activity and Lower Toxicity in E. coli via Mutation of Free Cysteine Residues.Semantic proximity Read ↗

The proapoptotic G41S mutation to human cytochrome c alters the heme electronic structure and increases the electron self-exchange rate.Semantic proximity Read ↗

Effects of naturally occurring S47F/A mutations on the structure and function of human cytochrome c.Semantic proximity Read ↗

Leu169Trp substitution in MnSOD from Staphylococcus equorum created an active new form of similar resistance to UVC irradiation.Semantic proximity Read ↗

Tyrosine phosphorylation turns alkaline transition into a biologically relevant process and makes human cytochrome c behave as an anti-apoptotic switch.Semantic proximity Read ↗

Structural and functional characterization of phosphomimetic mutants of cytochrome c at threonine 28 and serine 47.Semantic proximity Read ↗

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