Evidence map›Paper›PMID 9403867›Full record

ReviewMolecular biology reports1997

Receptor-like protein tyrosine phosphatases: alike and yet so different.

R Schaapveld, B Wieringa, W Hendriks

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular biology reports, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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 at 1 institution in 1 country.

R SchaapveldDepartment of Cell Biology & Histology, Institute of Cellular Signalling, University of Nijmegen, The Netherlands.
B Wieringa
W Hendriks
Radboud University Nijmegen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reversible phosphorylation on tyrosine residues is an extremely rapid and powerful posttranslational modification that is used in signalling pathways for the regulation of cell growth and differentiation. Over the past several years an impressive number of receptor-like protein tyrosine phosphatase (RPTPase) family members have been identified by molecular cloning, and undoubtedly many more will follow. This review provides an overview of the molecular data that are available for the currently identified RPTPases and discusses their possible biological implications.

Indexed as

AnimalsAxonsBinding SitesCell Adhesion MoleculesDiabetes Mellitus, Type 1DrosophilaHumansLeukocyte Common AntigensProtein Tyrosine Phosphatase, Non-Receptor Type 1Protein Tyrosine PhosphatasesCell Adhesion MoleculesLeukocyte Common AntigensProtein Tyrosine Phosphatase, Non-Receptor Type 1Protein Tyrosine Phosphatases

Identifiers

PMID9403867
OpenAlexW1692715431

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.