Evidence map›Paper›PMID 8510180›Full record

ArticleJournal of molecular evolution1993

Evolution of EF-hand calcium-modulated proteins. IV. Exon shuffling did not determine the domain compositions of EF-hand proteins.

R H Kretsinger, S Nakayama

Abstract read
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In one paragraph

Article in Journal of molecular evolution, 1993. 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
2.0field-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

10 citing papers in PubMed, 43 citations in OpenAlex.

  1. Conserved properties of individual Ca2+-binding sites in calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. The amino acid sequence of the light chain of Acanthamoeba myosin IC.Journal of muscle research and cell motility · 1997
    Article
  7. Direct modulation of calmodulin targets by the neuronal calcium sensor NCS-1.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  8. Article
  9. Review
  10. 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

2 authors at 1 institution in 1 country.

R H KretsingerDepartment of Biology, University of Virginia, Charlottesville 22901.
S Nakayama
University of Virginia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the previous three reports in this series we demonstrated that the EF-hand family of proteins evolved by a complex pattern of gene duplication, transposition, and splicing. The dendrograms based on exon sequences are nearly identical to those based on protein sequences for troponin C, the essential light chain myosin, the regulatory light chain, and calpain. This validates both the computational methods and the dendrograms for these subfamilies. The proposal of congruence for calmodulin, troponin C, essential light chain, and regulatory light chain was confirmed. There are, however, significant differences in the calmodulin dendrograms computed from DNA and from protein sequences. In this study we find that introns are distributed throughout the EF-hand domain and the interdomain regions. Further, dendrograms based on intron type and distribution bear little resemblance to those based on protein or on DNA sequences. We conclude that introns are inserted, and probably deleted, with relatively high frequency. Further, in the EF-hand family exons do not correspond to structural domains and exon shuffling played little if any role in the evolution of this widely distributed homolog family. Calmodulin has had a turbulent evolution. Its dendrograms based on protein sequence, exon sequence, 3'-tail sequence, intron sequences, and intron positions all show significant differences.

Indexed as

Biological EvolutionAnimalsCalciumCalcium-Binding ProteinsCalmodulinExonsHumansIntronsProtein ConformationSequence Homology, Nucleic AcidCalciumCalcium-Binding ProteinsCalmodulinNASA Discipline ExobiologyNon-NASA Center

Identifiers

PMID8510180
OpenAlexW2036625622

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.