Evidence map›Paper›PMID 7980436›Full record

ArticleThe Biochemical journal1994

Identification and characterization of ATPase activity associated with maize (Zea mays) annexins.

A D McClung, A D Carroll, N H Battey

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 35% 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

14 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  3. Review
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  7. Article
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  11. Article
  12. Article
  13. Article
  14. Annexins of plant cells.Plant physiology · 1995
    Review
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.

A D McClungSchool of Plant Sciences, University of Reading, Berks, U.K.
A D Carroll
N H Battey
University of Reading · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An ATPase activity is associated with maize (Zea mays) annexins. It has a pH optimum of 6.0, shows Michaelis-Menten kinetics and is not stimulated by Ca2+, Mg2+, EDTA or KCl; it is not inhibited by vanadate, molybdate, nitrate or azide, but N-ethylmaleimide inhibits by approximately 30% at 1-2 mM. These properties indicate that the activity is unlike other ATPases, although it has many features in common with the myosin ATPase. Gel filtration shows that the ATPase activity is mainly associated with a 68 kDa protein that is extracted with the p33/p35 annexins and cross-reacts with antibodies to these proteins.

Indexed as

Adenosine TriphosphatasesAnnexinsHydrogen-Ion ConcentrationKineticsSubstrate SpecificityZea maysAdenosine TriphosphatasesAnnexins

Identifiers

PMID7980436
PMCPMC1137604
OpenAlexW140922522

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.