ArticleJournal of the American Chemical Society2018
Minimal Heterochiral de Novo Designed 4Fe-4S Binding Peptide Capable of Robust Electron Transfer.
Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
33 citing papers in PubMed.
- The Ascent of Miniproteins.Biochemistry · 2026Review
- An Automated Electrochemistry Platform for Accelerating the Characterization of Enzymatic Electrochemistry.ACS electrochemistry · 2026Article
- Probing anion recognition in a cobalt(II) de novo designed metalloprotein.Journal of inorganic biochemistry · 2026Article
- The Borderlands of Foldability: Lessons from Simplified Proteins.Trends in chemistry · 2026Article
- Article
- Article
- Science of the gaps.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- RNA binding and coacervation promote preservation of peptide form and function across the heterochiral-homochiral divide.Protein science : a publication of the Protein Society · 2025Article
- On the emergence of metabolism: the evolution of proteins that powered life.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- Recent advances in de novo designed metallopeptides as tailored enzyme mimics.Current opinion in chemical biology · 2025Review
- Shedding Light on the Electron Delocalization Pathway at the [FeInorganic chemistry · 2025Article
- Redefining the Limits of Functional Continuity in the Early Evolution of P-Loop NTPases.Molecular biology and evolution · 2025Article
- Bottom-up construction of chiral metal-peptide assemblies from metal cluster motifs.Nature communications · 2024Article
- Protocellular Heme and Iron-Sulfur Clusters.Accounts of chemical research · 2024Review
- An Artificial [FeJournal of the American Chemical Society · 2023Article
- Atomically Accurate Design of Metalloproteins with Predefined Coordination Geometries.Journal of the American Chemical Society · 2023Article
- Protection of Catalytic Cofactors by Polypeptides as a Driver for the Emergence of Primordial Enzymes.Molecular biology and evolution · 2023Article
- Design of a minimal di-nickel hydrogenase peptide.Science advances · 2023Article
- Metals in Prebiotic Catalysis: A Possible Evolutionary Pathway for the Emergence of Metalloproteins.ACS omega · 2023Review
- Exploration of Structured Symmetric Cyclic Peptides as Ligands for Metal-Organic Frameworks.Chemistry of materials : a publication of the American Chemical Society · 2022Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Ambidoxin is a designed, minimal dodecapeptide consisting of alternating L and D amino acids that binds a 4Fe-4S cluster through ligand-metal interactions and an extensive network of second-shell hydrogen bonds. The peptide can withstand hundreds of oxidation-reduction cycles at room temperature. Ambidoxin suggests how simple, prebiotic peptides may have achieved robust redox catalysis on the early Earth.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.