Evidence map›Paper›PMID 1602495›Full record

ReviewJournal of molecular evolution1992

Evolution of EF-hand calcium-modulated proteins. II. Domains of several subfamilies have diverse evolutionary histories.

S Nakayama, N D Moncrief, R H Kretsinger, New Collective Author

Abstract readComparative StudyReview
PubMed Publisher
In one paragraph

Review in Journal of molecular evolution, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
–field-weighted citation impact
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

47 citing papers in PubMed.

  1. Article
  2. What Is Parvalbumin for?Biomolecules · 2022
    Review
  3. Article
  4. Diel transcriptional oscillations of light-sensitive regulatory elements in open-ocean eukaryotic plankton communities.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. The evolutionary landscape of the Rab family in chordates.Cellular and molecular life sciences : CMLS · 2019
    Article
  6. Structural and functional diversity of EF-hand proteins: Evolutionary perspectives.Protein science : a publication of the Protein Society · 2017
    Review
  7. Article
  8. Tertiary alphabet for the observable protein structural universe.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  9. Conserved properties of individual Ca2+-binding sites in calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. From damage response to action potentials: early evolution of neural and contractile modules in stem eukaryotes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. GCAP1 mutations associated with autosomal dominant cone dystrophy.Advances in experimental medicine and biology · 2010
    Review
  17. Inherent flexibility determines the transition mechanisms of the EF-hands of calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  18. Article
  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

4 authors.

S NakayamaDepartment of Biology, University of Virginia, Charlottesville 22901.
N D Moncrief
R H Kretsinger
New Collective Author

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the first report in this series we described the relationships and evolution of 152 individual proteins of the EF-hand subfamilies. Here we add 66 additional proteins and define eight (CDC, TPNV, CLNB, LPS, DGK, 1F8, VIS, TCBP) new subfamilies and seven (CAL, SQUD, CDPK, EFH5, TPP, LAV, CRGP) new unique proteins, which we assume represent new subfamilies. The main focus of this study is the classification of individual EF-hand domains. Five subfamilies--calmodulin, troponin C, essential light chain, regulatory light chain, CDC31/caltractin--and three uniques--call, squidulin, and calcium-dependent protein kinase--are congruent in that all evolved from a common four-domain precursor. In contrast calpain and sarcoplasmic calcium-binding protein (SARC) each evolved from its own one-domain precursor. The remaining 19 subfamilies and uniques appear to have evolved by translocation and splicing of genes encoding the EF-hand domains that were precursors to the congruent eight and to calpain and to SARC. The rates of evolution of the EF-hand domains are slower following formation of the subfamilies and establishment of their functions. Subfamilies are not readily classified by patterns of calcium coordination, interdomain linker stability, and glycine and proline distribution. There are many homoplasies indicating that similar variants of the EF-hand evolved by independent pathways.

Indexed as

Biological EvolutionMultigene FamilyAmino Acid SequenceAnimal Population GroupsAnimalsCalcium-Binding ProteinsGenesHelminth ProteinsHumansMolecular Sequence DataPhylogenyPlant ProteinsProtein ConformationProtozoan ProteinsSequence Homology, Nucleic AcidSpecies SpecificityCalcium-Binding ProteinsHelminth ProteinsPlant ProteinsProtozoan ProteinsNASA Discipline ExobiologyNon-NASA Center

Identifiers

PMID1602495

What OpenQuestion holds

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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.