ArticleACS chemical biology2014
Anatomy of β-strands at protein-protein interfaces.
Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 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
57 citing papers in PubMed, 115 citations in OpenAlex.
- Four subtypes of disease-causing missense mutations underlie pathogenic protein interactions in neurodegenerative VPS13A disease.The Journal of clinical investigation · 2026Article
- Improved protein binder design using β-pairing targeted RFdiffusion.Nature communications · 2026Article
- Using generative AI to transform peptide hits into small molecule leads.Beilstein journal of organic chemistry · 2026Article
- Intrastrand Peptide Staples That Promote β-Sheet Folding, Self-Assembly, and Amyloid Seeding.Journal of the American Chemical Society · 2025Article
- From Concepts to Inhibitors: A Blueprint for Targeting Protein-Protein Interactions.Chemical reviews · 2025Review
- Reengineering of a Proteomimetic Pan-Ras Inhibitor into a Ras Degrader.Angewandte Chemie (International ed. in English) · 2025Article
- Selection of Nucleotide-Encoded Mass Libraries of Macrocyclic Peptides for Inaccessible Drug Targets.Chemical reviews · 2024Review
- Design of amyloidogenic peptide traps.Nature chemical biology · 2024Article
- Understanding β-strand mediated protein-protein interactions: tuning binding behaviour of intrinsically disordered sequences by backbone modification.Chemical science · 2024Article
- Beyond N-Alkylation: Synthesis, Structure, and Function of N-Amino Peptides.Accounts of chemical research · 2024Article
- Targeting Allosteric Site of PCSK9 Enzyme for the Identification of Small Molecule Inhibitors: An In Silico Drug Repurposing Study.Biomedicines · 2024Article
- Macrocyclic β-Sheets Stabilized by Hydrogen Bond Surrogates.Angewandte Chemie (International ed. in English) · 2023Article
- Diagonal Interactions between Glutamate and Arginine Analogs with Varying Side-Chain Lengths in a β-Hairpin.Molecules (Basel, Switzerland) · 2023Article
- A nascent peptide code for translational control of mRNA stability in human cells.Nature communications · 2022Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- The Effects of Charged Amino Acid Side-Chain Length on Diagonal Cross-Strand Interactions between Carboxylate- and Ammonium-Containing Residues in a β-Hairpin.Molecules (Basel, Switzerland) · 2022Article
- Design and Synthesis of Crosslinked Helix Dimers as Protein Tertiary Structure Mimics.Current protocols · 2022Article
- Bispidine as a β-strand nucleator: from a β-arch to self-assembled cages and vesicles.Chemical science · 2021Article
- N-Amination Converts Amyloidogenic Tau Peptides into Soluble Antagonists of Cellular Seeding.ACS chemical neuroscience · 2021Article
- Peptoid-based reprogrammable template for cell-permeable inhibitors of protein-protein interactions.Chemical science · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The development of inhibitors for protein-protein interactions frequently involves the mimicry of secondary structure motifs. While helical protein-protein interactions have been heavily targeted, a similar level of success for the inhibition of β-strand and β-sheet rich interfaces has been elusive. We describe an assessment of the full range of β-strand interfaces whose high-resolution structures are available in the Protein Data Bank. This analysis identifies complexes where a β-stand or β-sheet contributes significantly to binding. The results highlight the molecular recognition complexity in strand-mediated interactions relative to helical interfaces and offer guidelines for the construction of β-strand and β-sheet mimics as ligands for protein receptors. The online data set will potentially serve as an entry-point to new classes of protein-protein interaction inhibitors.
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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.