ArticleAngewandte Chemie (Weinheim an der Bergstrasse, Germany)2015
Selective and Potent Proteomimetic Inhibitors of Intracellular Protein-Protein Interactions.
Article in Angewandte Chemie (Weinheim an der Bergstrasse, Germany), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- Selective Disruption of Survivin's Protein-Protein Interactions: A Supramolecular Approach Based on Guanidiniocarbonylpyrrole.Chembiochem : a European journal of chemical biology · 2022Article
- Natural and Synthetic Oligoarylamides: Privileged Structures for Medical Applications.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Review
- Selective Affimers Recognise the BCL-2 Family Proteins BCL-xChembiochem : a European journal of chemical biology · 2021Article
- Stapled Peptides as HIF-1α/p300 Inhibitors: Helicity Enhancement in the Bound State Increases Inhibitory Potency.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Peptide-Directed Binding for the Discovery of Modulators of α-Helix-Mediated Protein-Protein Interactions: Proof-of-Concept Studies with the Apoptosis Regulator Mcl-1.Angewandte Chemie (International ed. in English) · 2017Article
- Cyclic and Macrocyclic Peptides as Chemical Tools To Recognise Protein Surfaces and Probe Protein-Protein Interactions.ChemMedChem · 2016Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Inhibition of protein-protein interactions (PPIs) represents a major challenge in chemical biology and drug discovery. α-Helix mediated PPIs may be amenable to modulation using generic chemotypes, termed "proteomimetics", which can be assembled in a modular manner to reproduce the vectoral presentation of key side chains found on a helical motif from one partner within the PPI. In this work, it is demonstrated that by using a library of N-alkylated aromatic oligoamide helix mimetics, potent helix mimetics which reproduce their biophysical binding selectivity in a cellular context can be identified.
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Registered trials
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