Evidence map›Paper›PMID 12071838›Full record

ArticleThe Biochemical journal2002

A kinetic model of the co-operative binding of calcium and ADP to scallop (Argopecten irradians) heavy meromyosin.

Miklós Nyitrai, Andrew G Szent-Györgyi, Michael A Geeves

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2002. 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
1.9field-weighted citation impact, top 13% 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, 30 citations in OpenAlex.

  1. Article
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  4. Article
  5. Broad disorder and the allosteric mechanism of myosin II regulation by phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  6. Article
  7. Article
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  9. Review
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  12. Adenosine diphosphate and strain sensitivity in myosin motors.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004
    Review
  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.

Miklós NyitraiDepartment of Biosciences, University of Kent at Canterbury, Canterbury, Kent, CT2 7NJ, UK.
Andrew G Szent-Györgyi
Michael A Geeves
University of Pecs · HU

Funding

REGULATORY DOMAIN/S1 CRYSTAL STRUCTURE--SCALLOP MYOSINR01AR041808 · NIAMS · BRANDEIS UNIVERSITY · PI COHEN, CAROLYN · 1995 to 1999
–
NIAMS NIH HHS AR41808
6 · The paper itself

Abstract

Analysis of the kinetics of ATP and ADP binding to scallop (Argopecten irradians) heavy meromyosin (HMM) showed that the only calcium-dependent process is the rate of ADP release. At physiological ionic strength calcium accelerated ADP release about 20-fold. Notably in the absence of calcium only one ADP bound HMM, with an affinity of 0.5-1 microM. The second nucleotide site remained unoccupied at up to 50 microM ADP yet could bind ATP rapidly. The calcium dependence of ADP-release rates showed that calcium binds co-operatively to scallop HMM with an affinity of 0.78 microM and a Hill coefficient of 1.9. Detailed interpretation of the data suggests that HMM exists in equilibrium between the on and off states and that calcium and ADP modulate the equilibrium between the two states. The on state is favoured in the presence of calcium and in the absence of both calcium and nucleotide. The off state is favoured by ADP (or ADP * P(i)) in the absence of calcium. A detailed co-operative model of the interaction of ADP and calcium with HMM is presented.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateAnimalsCa(2+) Mg(2+)-ATPaseCalciumIn Vitro TechniquesKineticsModels, BiologicalMolluscaMyosin Subfragmentsortho-AminobenzoatesProtein BindingProtein ConformationSpectrometry, FluorescenceTryptophan3'-O-(N-methylanthraniloyl) ATPAdenosine DiphosphateAdenosine TriphosphateCa(2+) Mg(2+)-ATPaseCalciumMyosin Subfragmentsortho-AminobenzoatesTryptophan

Identifiers

PMID12071838
PMCPMC1222655
OpenAlexW1994376265

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.