Evidence map›Paper›PMID 9626666›Full record

ReviewMolecular neurobiology1998

14-3-3 proteins in neuronal development and function.

E M Skoulakis, R L Davis

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular neurobiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. 14-3-3/Tau Interaction and Tau Amyloidogenesis.Journal of molecular neuroscience : MN · 2019
    Review
  17. 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

2 authors.

E M SkoulakisDepartment of Cell Biology, Baylor College of Medicine, Houston, TX 77030, USA.
R L Davis

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 14-3-3 proteins are small, cytosolic, evolutionarily conserved proteins expressed abundantly in the nervous system. Although they were discovered more than 30 yr ago, their function in the nervous system has remained enigmatic. Several recent studies have helped to clarify their biological function. Crystallographic investigations have revealed that 14-3-3 proteins exist as dimers and that they contain a specific region for binding to other proteins. The interacting proteins, in turn, contain a 14-3-3 binding motif; proteins that interact with 14-3-3 dimers include PKC and Raf, protein kinases with critical roles in neuronal signaling. These proteins are capable of activating Raf in vitro, and this role has been verified by in vivo studies in Drosophila. Most interestingly, mutations in the Drosophila 14-3-3 genes disrupt neuronal differentiation, synaptic plasticity, and behavioral plasticity, establishing a role for these proteins in the development and function of the nervous system.

Indexed as

Nervous System Physiological PhenomenaProtein BiosynthesisTyrosine 3-Monooxygenase14-3-3 ProteinsAnimalsDimerizationDrosophilaEnzyme InhibitorsHumansMammalsModels, NeurologicalNeuronsProtein Kinase CProtein KinasesProteinsProto-Oncogene Proteins c-raf14-3-3 ProteinsEnzyme InhibitorsProtein Kinase CProtein KinasesProteinsProto-Oncogene Proteins c-rafTyrosine 3-Monooxygenase

Identifiers

PMID9626666

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.