ArticleACS chemical biology2020
Covalent Targeting of Ras G12C by Rationally Designed Peptidomimetics.
Article in ACS chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 34 citations in OpenAlex.
- Fragment-Based Screening of Heterocyclic Electrophiles Identified Acrylamide Bioisoteres for Covalent KRasArchiv der Pharmazie · 2026Article
- Enhancing De Novo Designed Peptides and Proteins via Irreversible Covalent Isoquinolinium Capture.ACS chemical biology · 2026Article
- Ligand-Directed Site-Selective Cysteine Bioconjugation of the KELCH Domain of KEAP1 with Hypervalent Iodine Reagents.Journal of the American Chemical Society · 2025Article
- Reengineering of a Proteomimetic Pan-Ras Inhibitor into a Ras Degrader.Angewandte Chemie (International ed. in English) · 2025Article
- An mRNA Display Approach for Covalent Targeting of aJournal of the American Chemical Society · 2025Article
- Discovering covalent cyclic peptide inhibitors of peptidyl arginine deiminase 4 (PADI4) using mRNA-display with a genetically encoded electrophilic warhead.Communications chemistry · 2024Article
- An mRNA Display Approach for Covalent Targeting of abioRxiv : the preprint server for biology · 2024Article
- Biospecific Chemistry for Covalent Linking of Biomacromolecules.Chemical reviews · 2024Review
- Affinity-Driven Aryl Diazonium Labeling of Peptide Receptors on Living Cells.Journal of the American Chemical Society · 2024Article
- Identification of Covalent Cyclic Peptide Inhibitors in mRNA Display.Journal of the American Chemical Society · 2023Article
- Peptide-based covalent inhibitors of protein-protein interactions.Journal of peptide science : an official publication of the European Peptide Society · 2023Review
- Covalent Proteomimetic Inhibitor of the Bacterial FtsQB Divisome Complex.Journal of the American Chemical Society · 2022Article
- Controlling oncogenic KRAS signaling pathways with a Palladium-responsive peptide.Communications chemistry · 2022Article
- Covalent labeling of a chromatin reader domain using proximity-reactive cyclic peptides.Chemical science · 2022Article
- Targeting intracellular protein-protein interactions with macrocyclic peptides.Trends in pharmacological sciences · 2022Review
- A primer on harnessing non-enzymatic post-translational modifications for drug design.RSC medicinal chemistry · 2021Article
- Covalent and Noncovalent Targeting of the Tcf4/β-Catenin Strand Interface with β-Hairpin Mimics.ACS chemical biology · 2021Article
- Covalent flexible peptide docking in Rosetta.Chemical science · 2021Article
- A Sos proteomimetic as a pan-Ras inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Divergent Mechanisms Activating RAS and Small GTPases Through Post-translational Modification.Frontiers in molecular biosciences · 2021Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Protein-protein interactions (PPIs) play a critical role in fundamental biological processes. Competitive inhibition of these interfaces requires compounds that can access discontinuous binding epitopes along a large, shallow binding surface area. Conformationally defined protein surface mimics present a viable route to target these interactions. However, the development of minimal protein mimics that engage intracellular targets with high affinity remains a major challenge because mimicry of a portion of the binding interface is often associated with the loss of critical binding interactions. Covalent targeting provides an attractive approach to overcome the loss of noncovalent contacts but have the inherent risk of dominating noncovalent contacts and increasing the likelihood of nonselective binding. Here, we report the iterative design of a proteolytically stable α
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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.