ArticleNature chemistry2014
Dithiol amino acids can structurally shape and enhance the ligand-binding properties of polypeptides.
Article in Nature chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 85 citations in OpenAlex.
- Benchmarking AI-driven protocols for cyclic peptide conformer prediction and ranking.RSC medicinal chemistry · 2026Article
- Directing the oxidative folding of disulfide-rich peptides for enhanced engineering and applications.Chemical science · 2025Review
- A facile strategy for the construction of a phage display cyclic peptide library for the selection of functional macrocycles.Chemical science · 2024Article
- Article
- Structure-guided design of CPPC-paired disulfide-rich peptide libraries for ligand and drug discovery.Chemical science · 2022Article
- Peptidic Sulfhydryl for Interfacing Nanocrystals and Subsequent Sensing of SARS-CoV-2 Protease.Chemistry of materials : a publication of the American Chemical Society · 2022Article
- An evolution-inspired strategy to design disulfide-rich peptides tolerant to extensive sequence manipulation.Chemical science · 2021Article
- Biosynthetic Strategies for Macrocyclic Peptides.Molecules (Basel, Switzerland) · 2021Review
- Identification of highly selective covalent inhibitors by phage display.Nature biotechnology · 2021Article
- Assessing Methodologies to Synthesize α-Sulfenylated Carbonyl Compounds by Green Chemistry Metrics.ChemSusChem · 2021Review
- Stereoselective and Divergent Construction of β-Thiolated/Selenolated Amino Acids via Photoredox-Catalyzed Asymmetric Giese Reaction.Journal of the American Chemical Society · 2020Article
- Oligophenyls with Multiple Disulfide Bridges as Higher Homologues of Dibenzo[c,e][1,2]dithiin: Synthesis and Application in Lithium-Ion Batteries.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Therapeutics targeting the fibrinolytic system.Experimental & molecular medicine · 2020Review
- Editorial: Chemical Design and Biomedical Applications of Disulfide-rich Peptides: Challenges and Opportunities.Frontiers in chemistry · 2020Article
- Article
- Iodine-promoted stereoselective amidosulfenylation of electron-deficient alkynes.RSC advances · 2018Article
- Peptide and protein nanoparticle conjugates: versatile platforms for biomedical applications.Chemical Society reviews · 2018Review
- Bicyclic Peptides as Next-Generation Therapeutics.Chemistry (Weinheim an der Bergstrasse, Germany) · 2017Review
- Role of CysACS omega · 2017Article
- Sulfur-Switch Ugi Reaction for Macrocyclic Disulfide-Bridged Peptidomimetics.Organic letters · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The disulfide bonds that form between two cysteine residues are important in defining and rigidifying the structures of proteins and peptides. In polypeptides containing multiple cysteine residues, disulfide isomerization can lead to multiple products with different biological activities. Here, we describe the development of a dithiol amino acid (Dtaa) that can form two disulfide bridges at a single amino acid site. Application of Dtaas to a serine protease inhibitor and a nicotinic acetylcholine receptor inhibitor that contain disulfide constraints enhanced their inhibitory activities 40- and 7.6-fold, respectively. X-ray crystallographic and NMR structure analysis show that the peptide ligands containing Dtaas have retained their native tertiary structures. We furthermore show that replacement of two cysteines by Dtaas can avoid the formation of disulfide bond isomers. With these properties, Dtaas are likely to have broad application in the rational design or directed evolution of peptides and proteins with high activity and stability.
Indexed as
Identifiers
What OpenQuestion holds
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.