The F54L mutation of Thioredoxin shows protein instability and increased fluctuations of the catalytic center.

doi:10.1016/j.bbagen.2025.130860

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

Back to search

Article

The F54L mutation of Thioredoxin shows protein instability and increased fluctuations of the catalytic center.

Biochimica et biophysica acta. General subjects - 1 Dec 2025

Baba Takumi, Ueno Go, Ohe Chika, Saji Shuku, Yamamoto Sachiko, Yamamoto Masaki, Nakagawa Hiroshi, Okazaki Nobuo, Ouchida Mamoru, Ohmori Iori Kawasaki, Takeshita Kohei

Abstract excerpt

Thioredoxin is a ubiquitous redox protein that acts as an electron donor via its conserved dithiol motif (C32GPC35), catalyzing dithiol-disulfide exchange to regulate the redox state of target proteins. It supports antioxidant defense via peroxiredoxins, facilitates DNA synthesis by donating electrons to ribonucleotide reductase, and regulates redox-sensitive signaling pathways, including those controlling...

Topics

Thioredoxins
Animals
Catalytic Domain
Rats
Molecular Dynamics Simulation
Mutation
Protein Stability
Oxidation-Reduction
Crystallography, X-Ray

Source

Open in PubMed

Identifiers

PMID: 40953808
DOI: 10.1016/j.bbagen.2025.130860

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics