ReviewEuropean journal of medicinal chemistry2015
Structure-based inhibition of protein-protein interactions.
Review in European journal of medicinal chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed.
- 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
- AlphaFold Ensemble Competition Screens Enable Peptide Binder Design with Single-Residue Sensitivity.ACS chemical biology · 2024Article
- Integrative Modeling of Protein-Polypeptide Complexes by Bayesian Model Selection using AlphaFold and NMR Chemical Shift Perturbation Data.bioRxiv : the preprint server for biology · 2024Article
- Stabilized cyclic peptides as modulators of protein-protein interactions: promising strategies and biological evaluation.RSC medicinal chemistry · 2023Review
- SVSBI: sequence-based virtual screening of biomolecular interactions.Communications biology · 2023Article
- Strategies for Conditional Regulation of Proteins.JACS Au · 2023Review
- Harnessing protein folding neural networks for peptide-protein docking.Nature communications · 2022Article
- Identification of Secondary Binding Sites on Protein Surfaces for Rational Elaboration of Synthetic Protein Mimics.ACS chemical biology · 2021Article
- Bent Into Shape: Folded Peptides to Mimic Protein Structure and Modulate Protein Function.Peptide science (Hoboken, N.J.) · 2020Article
- Molecular recognition of ubiquitin and Lys63-linked diubiquitin by STAM2 UIM-SH3 dual domain: the effect of its linker length and flexibility.Scientific reports · 2019Article
- Design criteria for minimalist mimics of protein-protein interface segments.Organic & biomolecular chemistry · 2019Article
- Small-molecule CaProceedings of the National Academy of Sciences of the United States of America · 2018Article
- An adaptive geometric search algorithm for macromolecular scaffold selection.Protein engineering, design & selection : PEDS · 2018Article
- Cell penetrating peptides to dissect host-pathogen protein-protein interactions in Theileria-transformed leukocytes.Bioorganic & medicinal chemistry · 2018Review
- Drugging tRNA aminoacylation.RNA biology · 2018Review
- Protein-protein binding selectivity and network topology constrain global and local properties of interface binding networks.Scientific reports · 2017Article
- Article
- Small Molecules Engage Hot Spots through Cooperative Binding To Inhibit a Tight Protein-Protein Interaction.Biochemistry · 2017Article
- Elucidating the druggable interface of protein-protein interactions using fragment docking and coevolutionary analysis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Protein-protein interactions (PPIs) are emerging as attractive targets for drug design because of their central role in directing normal and aberrant cellular functions. These interactions were once considered "undruggable" because their large and dynamic interfaces make small molecule inhibitor design challenging. However, landmark advances in computational analysis, fragment screening and molecular design have enabled development of a host of promising strategies to address the fundamental molecular recognition challenge. An attractive approach for targeting PPIs involves mimicry of protein domains that are critical for complex formation. This approach recognizes that protein subdomains or protein secondary structures are often present at interfaces and serve as organized scaffolds for the presentation of side chain groups that engage the partner protein(s). Design of protein domain mimetics is in principle rather straightforward but is enabled by a host of computational strategies that provide predictions of important residues that should be mimicked. Herein we describe a workflow proceeding from interaction network analysis, to modeling a complex structure, to identifying a high-affinity sub-structure, to developing interaction inhibitors. We apply the design procedure to peptidomimetic inhibitors of Ras-mediated signaling.
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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.