Evidence map›Paper›PMID 25234613›Full record

ReviewSeminars in cell & developmental biology2015

Extracellular regulation of type IIa receptor protein tyrosine phosphatases: mechanistic insights from structural analyses.

Charlotte H Coles, E Yvonne Jones, A Radu Aricescu

Abstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Cell Adhesion Molecule Signaling at the Synapse: Beyond the Scaffold.Cold Spring Harbor perspectives in biology · 2024
    Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. The Role of SliTrk5 in Central Nervous System.BioMed research international · 2022
    Review
  9. Altered ClProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Review
  11. LAR Receptor Tyrosine Phosphatase Family in Healthy and Diseased Brain.Frontiers in cell and developmental biology · 2021
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  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

3 authors.

Charlotte H ColesLaboratory for Axon Growth and Regeneration, German Center for Neurodegenerative Diseases (DZNE), Ludwig-Erhard-Allee 2, 53175 Bonn, Germany. Electronic address: charlotte.coles@dzne.de.
E Yvonne JonesDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK. Electronic address: yvonne@strubi.ox.ac.uk.
A Radu AricescuDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK. Electronic address: radu@strubi.ox.ac.uk.

Funding

Cancer Research UK 10976Cancer Research UK 17721Cancer Research UK A10976Medical Research Council G0700232Medical Research Council G0900084Medical Research Council G9900061Medical Research Council L009609Medical Research Council MR/L009609/1Wellcome Trust 090532Wellcome Trust 090532/Z/09/Z
6 · The paper itself

Abstract

The receptor protein tyrosine phosphatases (RPTPs) exhibit a wide repertoire of cellular signalling functions. In particular, type IIa RPTP family members have recently been highlighted as hubs for extracellular interactions in neurons, regulating neuronal extension and guidance, as well as synaptic organisation. In this review, we will discuss the recent progress of structural biology investigations into the architecture of type IIa RPTP ectodomains and their interactions with extracellular ligands. Structural insights, in combination with biophysical and cellular studies, allow us to begin to piece together molecular mechanisms for the transduction and integration of type IIa RPTP signals and to propose hypotheses for future experimental validation.

Indexed as

AnimalsHumansModels, MolecularNeuronsProtein Structure, TertiaryReceptor-Like Protein Tyrosine Phosphatases, Class 2SynapsesReceptor-Like Protein Tyrosine Phosphatases, Class 2Cell surface receptorCell surface signallingCrystal structureNeuronal extensionNeuronal synapseReceptor protein tyrosine phosphatase

Identifiers

PMID25234613
PMCPMC4765084

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.