Evidence map›Paper›PMID 8037685›Full record

ArticleThe Biochemical journal1994

Characterization of 14-3-3 proteins in adrenal chromaffin cells and demonstration of isoform-specific phospholipid binding.

D Roth, A Morgan, H Martin, D Jones, G J Martens, A Aitken, R D Burgoyne

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 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.0field-weighted citation impact, top 7% 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

20 citing papers in PubMed, 60 citations in OpenAlex.

  1. From 1957 to Nowadays: A Brief History of Epigenetics.International journal of molecular sciences · 2020
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  4. Components of the CtBP1/BARS-dependent fission machinery.Histochemistry and cell biology · 2013
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  8. Implications for proteasome nuclear localization revealed by the structure of the nuclear proteasome tether protein Cut8.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  9. Article
  10. Article
  11. Article
  12. Article
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  14. Article
  15. Article
  16. Molecular evolution of the 14-3-3 protein family.Journal of molecular evolution · 1996
    Article
  17. Article
  18. Article
  19. Article
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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

7 authors at 1 institution in 1 country.

D RothPhysiological Laboratory, University of Liverpool, U.K.
A Morgan
H Martin
D Jones
G J Martens
A Aitken
R D Burgoyne
Radboud University Nijmegen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Isoform-specific antisera were used to examine which 14-3-3 isoforms were present in bovine adrenal chromaffin cells. The eta, tau and sigma isoforms were not detectable, and the epsilon isoform was present at only low levels. 14-3-3 isoforms were readily detected with antisera against the beta, gamma and zeta isoforms. The latter isoforms were found to leak from digitonin-permeabilized chromaffin cells, as expected for cytosolic proteins, but a proportion of each isoform was retained. In subcellular fractionation studies isoforms recognized by the beta and zeta antisera were found in the cytosol and Triton-insoluble cytoskeletal fractions, while the gamma isoform was found in cytosol and also in microsomal and chromaffin granule membrane fractions. The gamma 14-3-3 protein associated with granule membranes was partially removed by a high-salt/carbonate wash, and the membranes could bind further gamma from cytosol or from a purified brain 14-3-3 protein mixture. The binding of gamma 14-3-3 was not Ca(2+)-dependent, nor was it affected by phorbol ester, GTP analogues or cyclic AMP. Using pure phospholipid vesicles it was found that gamma and also epsilon 14-3-3 proteins bound directly to phospholipids. Little binding of brain beta, eta or zeta to phospholipid vesicles was detected. Brain 14-3-3 proteins were also able to aggregate phospholipid vesicles. Recombinant 14-3-3 isoforms (tau and the Xenopus protein) were able to stimulate Ca(2+)-dependent exocytosis in digitonin-permeabilized chromaffin cells. The Xenopus proteins lacks part of the extreme N-terminus, indicating that this domain is not essential for function in exocytosis.

Indexed as

Tyrosine 3-Monooxygenase14-3-3 ProteinsAdrenal MedullaAmino Acid SequenceAnimalsCalciumCattleChromaffin GranulesExocytosisMolecular Sequence DataNerve Tissue ProteinsPhospholipidsProtein BindingRecombinant ProteinsSheepSubcellular Fractions14-3-3 ProteinsCalciumNerve Tissue ProteinsPhospholipidsRecombinant ProteinsTyrosine 3-Monooxygenase

Identifiers

PMID8037685
PMCPMC1137176
OpenAlexW2338512986

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.