Evidence map›Paper›PMID 22576124›Full record

ReviewFEBS letters2012

Plasticity of PDZ domains in ligand recognition and signaling.

Ylva Ivarsson

Open access · hybridAbstract readReview
In one paragraph

Review in FEBS letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

74 citing papers in PubMed, 136 citations in OpenAlex.

  1. Proteome-wide prediction of interactions between structured domains and peptide motifs reveals functionally coherent subnetworks.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Biomolecular NMR assignments · 2025
    Article
  3. Structural Evidence for DUF512 as a RadicalACS bio & med chem Au · 2024
    Article
  4. Article
  5. Functional protein dynamics in a crystal.Nature communications · 2024
    Article
  6. Functional Protein Dynamics in a Crystal.bioRxiv : the preprint server for biology · 2024
    Article
  7. DexDesign: an OSPREY-based algorithm for designing de novo D-peptide inhibitors.Protein engineering, design & selection : PEDS · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Cryptic binding properties of a transient folding intermediate in a PDZ tandem repeat.Protein science : a publication of the Protein Society · 2022
    Article
  14. Article
  15. Human Serine Racemase Weakly Binds the Third PDZ Domain of PSD-95.International journal of molecular sciences · 2022
    Article
  16. Review
  17. Review
  18. Allosterism in the PDZ Family.International journal of molecular sciences · 2022
    Review
  19. Review
  20. Review

14 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

1 author at 1 institution in 1 country.

Ylva IvarssonTerrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario, Canada. ylva.ivarsson@kimlab.org
University of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The PDZ domain is a protein-protein interacting module that plays an important role in the organization of signaling complexes. The recognition of short intrinsically disordered C-terminal peptide motifs is the archetypical PDZ function, but the functional repertoire of this versatile module also includes recognition of internal peptide sequences, dimerization and phospholipid binding. The PDZ function can be tuned by various means such as allosteric effects, changes of physiological buffer conditions and phosphorylation of PDZ domains and/or ligands, which poses PDZ domains as dynamic regulators of cell signaling. This review is focused on the plasticity of the PDZ interactions.

Indexed as

LigandsPDZ DomainsProtein BindingAllosteric SiteAlternative SplicingAmino Acid MotifsAnimalsBuffersDimerizationHumansLipidsModels, MolecularPeptidesPhospholipidsPhosphorylationProtein ConformationBuffersLigandsLipidsPeptidesPhospholipids

Identifiers

PMID22576124
PMCPMC7094393
OpenAlexW2052323707

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.