Evidence map›Paper›PMID 8798343›Full record

ArticleJournal of molecular evolution1996

Molecular evolution of the 14-3-3 protein family.

W Wang, D C Shakes

Abstract read
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In one paragraph

Article in Journal of molecular evolution, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

72 citing papers in PubMed, 217 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Redundant and Distinct Roles of Two 14-3-3 Proteins inJournal of fungi (Basel, Switzerland) · 2024
    Article
  10. Review
  11. Compact Programmable Control of Protein Secretion in Mammalian Cells.bioRxiv : the preprint server for biology · 2023
    Article
  12. Article
  13. Emerging Evidence onMicroorganisms · 2022
    Review
  14. Article
  15. Review
  16. Article
  17. Molecular Analysis ofInternational journal of molecular sciences · 2021
    Article
  18. 14-3-3σ and Its Modulators in Cancer.Pharmaceuticals (Basel, Switzerland) · 2020
    Review
  19. Review
  20. Article

12 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

W WangDepartment of Biology, University of Houston, Houston, TX 77204-5513, USA.
D C Shakes
University of Houston · USWilliam & Mary · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of the highly conserved and ubiquitous 14-3-3 protein family modulate a wide variety of cellular processes. To determine the evolutionary relationships among specific 14-3-3 proteins in different plant, animal, and fungal species and to initiate a predictive analysis of isoform-specific differences in light of the latest functional and structural studies of 14-3-3, multiple alignments were constructed from forty-six 14-3-3 sequences retrieved from the GenBank and SwissProt databases and a newly identified second 14-3-3 gene from Caenorhabditis elegans. The alignment revealed five highly conserved sequence blocks. Blocks 2-5 correlate well with the alpha helices 3, 5, 7, and 9 which form the proposed internal binding domain in the three-dimensional structure model of the functioning dimer. Amino acid differences within the functional and structural domains of plant and animal 14-3-3 proteins were identified which may account for functional diversity amongst isoforms. Protein phylogenic trees were constructed using both the maximum parsimony and neighbor joining methods of the PHYLIP(3.5c) package; 14-3-3 proteins from Entamoeba histolytica, an amitochondrial protozoa, were employed as an outgroup in our analysis. Epsilon isoforms from the animal lineage form a distinct grouping in both trees, which suggests an early divergence from the other animal isoforms. Epsilons were found to be more similar to yeast and plant isoforms than other animal isoforms at numerous amino acid positions, and thus epsilon may have retained functional characteristics of the ancestral protein. The known invertebrate proteins group with the nonepsilon mammalian isoforms. Most of the current 14-3-3 isoform diversity probably arose through independent duplication events after the divergence of the major eukaryotic kingdoms. Divergence of the seven mammalian isoforms beta, zeta, gamma, eta, epsilon, tau, and sigma (stratifin/HME1) occurred before the divergence of mammalian and perhaps before the divergence of vertebrate species. A possible ancestral 14-3-3 sequence is proposed.

Indexed as

Caenorhabditis elegans ProteinsEvolution, MolecularTyrosine 3-Monooxygenase14-3-3 ProteinsAmino Acid SequenceAnimalsCaenorhabditis elegansConsensus SequenceConserved SequenceDatabases, FactualGenes, HelminthMolecular Sequence DataPhylogenyProtein ConformationProteinsSequence Alignment14-3-3 ProteinsCaenorhabditis elegans Proteinspar-5 protein, C elegansProteinsTyrosine 3-Monooxygenase

Identifiers

PMID8798343
OpenAlexW2002370642

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.