Evidence map›Paper›PMID 32313833›Full record

ReviewAdvanced therapeutics2019

PDZ Domains as Drug Targets.

Nikolaj R Christensen, Jelena Čalyševa, Eduardo F A Fernandes, Susanne Lüchow, Louise S Clemmensen, Linda M Haugaard-Kedström, Kristian Strømgaard

Open access · bronzeAbstract readReview
In one paragraph

Review in Advanced therapeutics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
7.0field-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

61 citing papers in PubMed, 110 citations in OpenAlex.

  1. Review
  2. Article
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  5. Review
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  7. Article
  8. Review
  9. Article
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  12. Review
  13. Article
  14. Structural Evidence for DUF512 as a RadicalACS bio & med chem Au · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. DexDesign: an OSPREY-based algorithm for designing de novo D-peptide inhibitors.Protein engineering, design & selection : PEDS · 2024
    Article

1 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

7 authors at 3 institutions in 3 countries.

Nikolaj R ChristensenCenter for Biopharmaceuticals Department of Drug Design and Pharmacology University of Copenhagen Universitetsparken 2 2100 Copenhagen Denmark.
Jelena ČalyševaEuropean Molecular Biology Laboratory (EMBL) Structural and Computational Biology Unit Meyerhofstraße 1 69117 Heidelberg Germany.
Eduardo F A FernandesCenter for Biopharmaceuticals Department of Drug Design and Pharmacology University of Copenhagen Universitetsparken 2 2100 Copenhagen Denmark.
Susanne LüchowDepartment of Chemistry - BMC Uppsala University Box 576 SE 75123 Uppsala Sweden.
Louise S ClemmensenCenter for Biopharmaceuticals Department of Drug Design and Pharmacology University of Copenhagen Universitetsparken 2 2100 Copenhagen Denmark.
Linda M Haugaard-KedströmCenter for Biopharmaceuticals Department of Drug Design and Pharmacology University of Copenhagen Universitetsparken 2 2100 Copenhagen Denmark.
Kristian StrømgaardCenter for Biopharmaceuticals Department of Drug Design and Pharmacology University of Copenhagen Universitetsparken 2 2100 Copenhagen Denmark.ORCID https://orcid.org/0000-0003-2206-4737
University of Copenhagen · DKEuropean Molecular Biology Organization · DEUppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-protein interactions within protein networks shape the human interactome, which often is promoted by specialized protein interaction modules, such as the postsynaptic density-95 (PSD-95), discs-large, zona occludens 1 (ZO-1) (PDZ) domains. PDZ domains play a role in several cellular functions, from cell-cell communication and polarization, to regulation of protein transport and protein metabolism. PDZ domain proteins are also crucial in the formation and stability of protein complexes, establishing an important bridge between extracellular stimuli detected by transmembrane receptors and intracellular responses. PDZ domains have been suggested as promising drug targets in several diseases, ranging from neurological and oncological disorders to viral infections. In this review, the authors describe structural and genetic aspects of PDZ-containing proteins and discuss the current status of the development of small-molecule and peptide modulators of PDZ domains. An overview of potential new therapeutic interventions in PDZ-mediated protein networks is also provided.

Indexed as

drug targetsinhibitorPDZprotein–protein interactions

Identifiers

PMID32313833
PMCPMC7161847
OpenAlexW2941674263

What OpenQuestion holds

Textmetadata
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.