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

Altered conformational dynamics contribute to species-specific effects of cytochrome c mutations on caspase activation.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry - 1 Mar 2024

Chin Thomas C, Wilbanks Sigurd M, Ledgerwood Elizabeth C

Abstract excerpt

Variants in the gene encoding human cytochrome c (CYCS) cause mild autosomal dominant thrombocytopenia. Despite high sequence conservation between mouse and human cytochrome c, this phenotype is not recapitulated in mice for the sole mutant (G41S) that has been investigated. The effect of the G41S mutation on the in vitro activities of cytochrome c is also not conserved between human and mouse. Peroxidase...

Read the complete abstract on PubMed

Topics

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

Share to Caspases
Share to Cytochromes c

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Activation

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Protein Conformation

Share to Species Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 38472487
DOI: 10.1007/s00775-024-02044-2
PMCID: PMC11098916

Genes

CYCS

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

Altered conformational dynamics contribute to species-specific effects of cytochrome c mutations on caspase activation.PMID 38472487Read ↗

Altered structure and dynamics of pathogenic cytochrome c variants correlate with increased apoptotic activitySemantic proximity Read ↗

Interspecies Variation in the Functional Consequences of Mutation of Cytochrome c.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 ↗

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 ↗

A computational study of the fold and stability of cytochrome c with implications for diseaseSemantic proximity Read ↗

Human cytochrome C natural variants: Studying the membrane binding properties of G41S and Y48H by fluorescence energy transfer and molecular dynamics.Semantic proximity Read ↗

Increased dynamics in the 40-57 Ω-loop of the G41S variant of human cytochrome c promote its pro-apoptotic conformation.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 ↗

Backbone resonance assignments of ferric human cytochrome c and the pro-apoptotic G41S mutant in the ferric and ferrous states.Semantic proximity Read ↗

The proportion of Met80-sulfoxide dictates peroxidase activity of human cytochrome c.Semantic proximity Read ↗

Investigation of structural dynamics of Thrombocytopenia Cargeeg mutants of human apoptotic cytochrome c: A molecular dynamics simulation approach.Semantic proximity Read ↗

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