Evidence map›Paper›PMID 7643916›Full record

ArticleNaunyn-Schmiedeberg's archives of pharmacology1995

Suramin analogs, divalent cations and ATP gamma S as inhibitors of ecto-ATPase.

M W Beukers, C J Kerkhof, M A van Rhee, U Ardanuy, C Gurgel, H Widjaja, P Nickel, A P IJzerman, W Soudijn

Abstract read
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In one paragraph

Article in Naunyn-Schmiedeberg's archives of pharmacology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

10 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Purine and pyrimidine (P2) receptors as drug targets.Journal of medicinal chemistry · 2002
    Review
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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

9 authors at 2 institutions in 2 countries.

M W BeukersLeiden/Amsterdam Center for Drug Research, Division of Medicinal Chemistry.
C J Kerkhof
M A van Rhee
U Ardanuy
C Gurgel
H Widjaja
P Nickel
A P IJzerman
W Soudijn
Centre for Human Drug Research · NLUniversity of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ecto-nucleotidases are plasma membrane-bound enzymes that sequentially dephosphorylate extracellular nucleotides such as ATP. This breakdown of ATP and other nucleotides obscures the characterization and classification of P2 (nucleotide) receptors. We therefore studied suramin and several of its analogs, divalent cations and ATP gamma S for their ability to inhibit ecto-ATPase in human blood cells. Suramin itself and Ni2+ were the more potent, non-competitive inhibitors with micromolar affinity. ATP gamma S also displayed micromolar affinity and inhibited ecto-ATPase competitively. The data obtained with the divalent cations demonstrate that coordination of the phosphate chain but not the N7 of the adenine ring is required for the breakdown of ATP by ecto-ATPase. Divalent cations that coordinate both the phosphate chain and N7 inhibit ecto-ATPase in a non-competitive manner.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAffinity LabelsBlood CellsCations, DivalentCopperHumansMathematicsMercuryMetalsReceptors, Purinergic P2Structure-Activity RelationshipSuraminadenosine 5'-O-(3-thiotriphosphate)Adenosine TriphosphatasesAdenosine TriphosphateAffinity LabelsCations, DivalentCopperectoATPaseMercuryMetalsReceptors, Purinergic P2Suramin

Identifiers

PMID7643916
OpenAlexW1988847736

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.