Evidence map›Paper›PMID 12841577›Full record

ReviewMolecular biology reports2003

PDZ domains-glue and guide.

Marco van Ham, Wiljan Hendriks

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular biology reports, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
–field-weighted citation impact
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

59 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Association betweenInternational journal of molecular sciences · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Allosterism in the PDZ Family.International journal of molecular sciences · 2022
    Review
  9. In Silico Structural and Functional Characterization of HtrA Proteins ofTropical medicine and infectious disease · 2020
    Article
  10. Seeking allosteric networks in PDZ domains.Protein engineering, design & selection : PEDS · 2018
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article
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

2 authors.

Marco van HamDepartment of Cell Biology, Institute of Cellular Signalling, Nijmegen Center for Molecular Life Sciences, University of Nijmegen, Geert Grooteplein 28, 6525 GA Nijmegen, The Netherlands.
Wiljan Hendriks

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PDZ domains are small globular building blocks that are amongst the most abundant protein interaction domains in organisms. Over the past several years an avalanche of data has implicated these modules in the clustering, targeting and routing of associating proteins. An overview is given of the types of interactions displayed by PDZ domains and how this relates to the current knowledge on their spatial structure. Furthermore, the different levels on which PDZ--ligand binding can be regulated and the consequences of PDZ domain-mediated clustering for activity, routing and targeting of interacting proteins will be addressed. Finally, some cell and animal models that illustrate the impact of PDZ domain-containing proteins on (multi-) cellular processes will be discussed.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsBinding SitesCarrier ProteinsCell Cycle ProteinsCytoskeletal ProteinsHumansMiceModels, BiologicalProtein BindingProtein Structure, TertiaryProtein TransportSignal TransductionAdaptor Proteins, Signal TransducingCarrier ProteinsCell Cycle ProteinsCytoskeletal ProteinsUSH1C protein, humanUsh1c protein, mouse

Identifiers

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.