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

Oxidative stress is tightly regulated by cytochrome c phosphorylation and respirasome factors in mitochondria.

Proceedings of the National Academy of Sciences of the United States of America - 31 Jul 2018

Guerra-Castellano Alejandra, Díaz-Quintana Antonio, Pérez-Mejías Gonzalo, Elena-Real Carlos A, González-Arzola Katiuska, García-Mauriño Sofía M, De la Rosa Miguel A, Díaz-Moreno Irene

Abstract excerpt

Respiratory cytochrome c has been found to be phosphorylated at tyrosine 97 in the postischemic brain upon neuroprotective insulin treatment, but how such posttranslational modification affects mitochondrial metabolism is unclear. Here, we report the structural features and functional behavior of a phosphomimetic cytochrome c mutant, which was generated by site-specific incorporation at position 97 of...

Read the complete abstract on PubMed

Topics

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

Share to Caspase 3
Share to Cytochromes c

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Electron Transport Complex IV

Share to Intracellular Signaling Peptides and Proteins

Share to Mitochondrial Proteins

Share to Neoplasm Proteins

Share to Oxidative Stress

Share to Rabbits

Source

Open in PubMed Open full text

Identifiers

PMID: 30018060
DOI: 10.1073/pnas.1806833115
PMCID: PMC6077723

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Oxidative stress is tightly regulated by cytochrome c phosphorylation and respirasome factors in mitochondria.PMID 30018060Read ↗

Structural basis of mitochondrial dysfunction in response to cytochrome c phosphorylation at tyrosine 48.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 ↗

Phosphomimetic substitution of cytochrome C tyrosine 48 decreases respiration and binding to cardiolipin and abolishes ability to trigger downstream caspase activation.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 ↗

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

The cytochrome b p.278Y>C mutation causative of a multisystem disorder enhances superoxide production and alters supramolecular interactions of respiratory chain complexes.Semantic proximity Read ↗

Mild phenotypes and proper supercomplex assembly in human cells carrying the homoplasmic m.15557G > A mutation in cytochrome b gene.Semantic proximity Read ↗

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

[Molecular effects of mitochondrial mutations in cytochrome b of complex III and their impact on the levels of free radical production].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 ↗

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 ↗

Conformational flexibility decreased due to Y67F and F82H mutations in cytochrome c: molecular dynamics simulation studies.Semantic proximity Read ↗

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