Evidence map›Paper›PMID 33022847›Full record

ArticleAngewandte Chemie (International ed. in English)2021

Structure Based Design of Bicyclic Peptide Inhibitors of RbAp48.

Peter 't Hart, Pascal Hommen, Anaïs Noisier, Adrian Krzyzanowski, Darijan Schüler, Arthur T Porfetye, Mohammad Akbarzadeh, Ingrid R Vetter, Hélène Adihou, Herbert Waldmann

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 20% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 29 citations in OpenAlex.

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  14. Structure Based Design of Bicyclic Peptide Inhibitors of RbAp48.Angewandte Chemie (International ed. in English) · 2021
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 3 countries.

Peter 't HartDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227, Dortmund, Germany.
Pascal HommenDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227, Dortmund, Germany.
Anaïs NoisierMedicinal Chemistry, Research and Early Development Cardiovascular, Renal and Metabolism, BioPharmaceutical R&D, AstraZeneca, Gothenburg, Sweden.
Adrian KrzyzanowskiDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227, Dortmund, Germany.
Darijan SchülerDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227, Dortmund, Germany.
Arthur T PorfetyeDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227, Dortmund, Germany.
Mohammad AkbarzadehDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227, Dortmund, Germany.
Ingrid R VetterDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227, Dortmund, Germany.
Hélène AdihouMedicinal Chemistry, Research and Early Development Cardiovascular, Renal and Metabolism, BioPharmaceutical R&D, AstraZeneca, Gothenburg, Sweden.
Herbert WaldmannDepartment of Chemical Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227, Dortmund, Germany.ORCID 0000-0002-9606-7247
Max Planck Institute of Molecular Physiology · DEMax Planck Society · DEAstraZeneca (Finland) · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The scaffolding protein RbAp48 is part of several epigenetic regulation complexes and is overexpressed in a variety of cancers. In order to develop tool compounds for the study of RbAp48 function, we have developed peptide inhibitors targeting the protein-protein interaction interface between RbAp48 and the scaffold protein MTA1. Based on a MTA1-derived linear peptide with low micromolar affinity and informed by crystallographic analysis, a bicyclic peptide was developed that inhibits the RbAp48/MTA1 interaction with a very low nanomolar K

Indexed as

Drug DesignAmino Acid SequenceCircular DichroismCrystallography, X-RayHumansHydrophobic and Hydrophilic InteractionsMutationPeptides, CyclicProtein ConformationRetinoblastoma-Binding Protein 4ThermodynamicsPeptides, CyclicRBBP4 protein, humanRetinoblastoma-Binding Protein 4cyclizationinhibitorspeptidesprotein-protein interactionsstructure-based design

Identifiers

PMID33022847
PMCPMC7894522
OpenAlexW3092001562

What OpenQuestion holds

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Registered trials

None linked

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.