Evidence map›Paper›PMID 29026209›Full record

ReviewNature reviews. Drug discovery2017

WD40 repeat domain proteins: a novel target class?

Matthieu Schapira, Mike Tyers, Maricel Torrent, Cheryl H Arrowsmith

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Drug discovery, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 190 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
190citing papers in PubMed, 1 pooled it
8.0field-weighted citation impact, top 2% 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

190 citing papers in PubMed, 1 synthesis or guideline pooled it, 334 citations in OpenAlex.

  1. Pooled it
  2. Science advances · 2026
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  20. DeepDegradome: A structure-aware deep learning framework for PROTAC and ligand generation against protein targets.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article

130 more citing papers are in PubMed but not listed here.

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

4 authors at 3 institutions in 2 countries.

Matthieu SchapiraStructural Genomics Consortium, University of Toronto, Toronto, 101 College St, MaRS South Tower, Suite 700, Ontario M5G 1L7, Canada.
Mike TyersInstitute for Research in Immunology and Cancer, Université de Montréal, Pavillon Marcelle-Coutu, 2950 Chemin de Polytechnique, Montréal, Québec H3T 1J4, Canada.
Maricel TorrentDiscovery Research, AbbVie, Inc., 1 North Waukegan Road, North Chicago, Illinois 60064, USA.
Cheryl H ArrowsmithStructural Genomics Consortium, University of Toronto, Toronto, 101 College St, MaRS South Tower, Suite 700, Ontario M5G 1L7, Canada.
University of Toronto · CAAbbVie (United States) · USInstitute for Research in Immunology and Cancer · CA

Funding

BioGRID: An open resource for biological interactions and network analysisR01OD010929 · OD · SINAI HEALTH SYSTEM · PI KARA DOLINSKI, Mike Tyers · 2012 to 2026
$13.9M
NIH HHS R01 OD010929Wellcome Trust
6 · The paper itself

Abstract

Antagonism of protein-protein interactions (PPIs) with small molecules is becoming more feasible as a therapeutic approach. Successful PPI inhibitors tend to target proteins containing deep peptide-binding grooves or pockets rather than the more common large, flat protein interaction surfaces. Here, we review one of the most abundant PPI domains in the human proteome, the WD40 repeat (WDR) domain, which has a central peptide-binding pocket and is a member of the β-propeller domain-containing protein family. Recently, two WDR domain-containing proteins, WDR5 and EED, as well as other β-propeller domains have been successfully targeted by potent, specific, cell-active, drug-like chemical probes. Could WDR domains be a novel target class for drug discovery? Although the research is at an early stage and therefore not clinically validated, cautious optimism is justified, as WDR domain-containing proteins are involved in multiple disease-associated pathways. The druggability and structural diversity of WDR domain binding pockets suggest that understanding how to target this prevalent domain class will open up areas of disease biology that have so far resisted drug discovery efforts.

Indexed as

AnimalsHumansMolecular Targeted TherapyWD40 Repeats

Identifiers

PMID29026209
PMCPMC5975957
OpenAlexW2761872853

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.