Evidence map›Paper›PMID 22555564›Full record

ReviewPurinergic signalling2012

Cellular function and molecular structure of ecto-nucleotidases.

Herbert Zimmermann, Matthias Zebisch, Norbert Sträter

Open access · bronzeAbstract readReview
In one paragraph

Review in Purinergic signalling, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 507 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
507citing papers in PubMed, 1 pooled it
44.4field-weighted citation impact, top 1% 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

507 citing papers in PubMed, 1 synthesis or guideline pooled it, 968 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Effects and Mechanism of 2'-AMP on Renal Vascular Resistance: Role of P2X1 Receptors.Journal of the American Society of Nephrology : JASN · 2026
    Article
  14. Article
  15. Article
  16. Article
  17. Adenosine APurinergic signalling · 2026
    Article
  18. Proteasomal-dependent endothelial P2YPurinergic signalling · 2026
    Article
  19. Article
  20. Article

447 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

3 authors at 3 institutions in 3 countries.

Herbert ZimmermannInstitute of Cell Biology and Neuroscience, Molecular and Cellular Neurobiology, Biologicum, Goethe-University Frankfurt, Max-von-Laue-Str. 13, 60438, Frankfurt am Main, Germany. h.zimmermann@bio.uni-frankurt.de
Matthias Zebisch
Norbert Sträter
Centre for Human Genetics · GBGoethe University Frankfurt · DELeipzig University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ecto-nucleotidases play a pivotal role in purinergic signal transmission. They hydrolyze extracellular nucleotides and thus can control their availability at purinergic P2 receptors. They generate extracellular nucleosides for cellular reuptake and salvage via nucleoside transporters of the plasma membrane. The extracellular adenosine formed acts as an agonist of purinergic P1 receptors. They also can produce and hydrolyze extracellular inorganic pyrophosphate that is of major relevance in the control of bone mineralization. This review discusses and compares four major groups of ecto-nucleotidases: the ecto-nucleoside triphosphate diphosphohydrolases, ecto-5'-nucleotidase, ecto-nucleotide pyrophosphatase/phosphodiesterases, and alkaline phosphatases. Only recently and based on crystal structures, detailed information regarding the spatial structures and catalytic mechanisms has become available for members of these four ecto-nucleotidase families. This permits detailed predictions of their catalytic mechanisms and a comparison between the individual enzyme groups. The review focuses on the principal biochemical, cell biological, catalytic, and structural properties of the enzymes and provides brief reference to tissue distribution, and physiological and pathophysiological functions.

Indexed as

5'-NucleotidaseAlkaline PhosphataseAnimalsCatalysisCatalytic DomainGlycosylationHumansIsoenzymesModels, MolecularNucleoside-Diphosphate KinaseNucleotidasesNucleotidesPhosphoric Diester HydrolasesPhylogenyProtein ConformationProteins5'-NucleotidaseAlkaline PhosphataseIsoenzymesNucleoside-Diphosphate KinaseNucleotidasesNucleotidesPhosphoric Diester HydrolasesProteinsPyrophosphatasesReceptors, Purinergic

Identifiers

PMID22555564
PMCPMC3360096
OpenAlexW1995321301

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.