Evidence map›Paper›PMID 12533192›Full record

ArticleThe Biochemical journal2003

Functional characterization of the non-catalytic ectodomains of the nucleotide pyrophosphatase/phosphodiesterase NPP1.

Rik Gijsbers, Hugo Ceulemans, Mathieu Bollen

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 51 citations in OpenAlex.

  1. Review
  2. Review
  3. Enzymology of extracellular NAD metabolism.Cellular and molecular life sciences : CMLS · 2021
    Review
  4. Crystal structures of human ENPP1 in apo and bound forms.Acta crystallographica. Section D, Structural biology · 2020
    Article
  5. Article
  6. The hepatic ectonucleotide pyrophosphatase/phosphodiesterase 1 gene mRNA abundance is reduced by insulin and induced by dexamethasone.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2018
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Crystal structure of Enpp1, an extracellular glycoprotein involved in bone mineralization and insulin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  12. Review
  13. Article
  14. Autotaxin.Cellular and molecular life sciences : CMLS · 2009
    Review
  15. Article
  16. Article
  17. Lysophospholipid interactions with protein targets.Biochimica et biophysica acta · 2008
    Review
  18. Review
  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 at 1 institution in 1 country.

Rik GijsbersAfdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit Leuven, Campus Gasthuisberg, Herestraat 49, B-3000 Leuven, Belgium.
Hugo Ceulemans
Mathieu Bollen
KU Leuven · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitous nucleotide pyrophosphatases/phosphodiesterases NPP1-3 consist of a short intracellular N-terminal domain, a single transmembrane domain and a large extracellular part, comprising two somatomedin-B-like domains, a catalytic domain and a poorly defined C-terminal domain. We show here that the C-terminal domain of NPP1-3 is structurally related to a family of DNA/RNA non-specific endonucleases. However, none of the residues that are essential for catalysis by the endonucleases are conserved in NPP1-NPP3, suggesting that the nuclease-like domain of NPP1-3 does not represent a second catalytic domain. Truncation analysis revealed that the nuclease-like domain of NPP1 is required for protein stability, for the targeting of NPP1 to the plasma membrane and for the expression of catalytic activity. We also demonstrate that 16 conserved cysteines in the somatomedin-B-like domains of NPP1, in concert with two flanking cysteines, mediate the dimerization of NPP1. The K173Q polymorphism of NPP1, which maps to the second somatomedin-B-like domain and has been associated with the aetiology of insulin resistance, did not affect the dimerization or catalytic activity of NPP1, and did not endow NPP1 with an affinity for the insulin receptor. Our data suggest that the non-catalytic ectodomains contribute to the subunit structure, stability and function of NPP1-3.

Indexed as

3T3 CellsAmino Acid SequenceAnimalsBinding SitesCatalysisChlorocebus aethiopsCOS CellsDimerizationEndonucleasesHeLa CellsHumansInsulinKineticsMiceModels, MolecularMolecular Sequence DataEndonucleasesInsulinnucleotide pyrophosphatase - phosphodiesterase IPhosphoric Diester HydrolasesPyrophosphatasesRecombinant Proteins

Identifiers

PMID12533192
PMCPMC1223305
OpenAlexW2125198748

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.