Evidence map›Paper›PMID 24489789›Full record

ArticlePloS one2014

Protein synthesis dependence of growth cone collapse induced by different Nogo-A-domains.

Richard Manns, Andre Schmandke, Antonio Schmandke, Prem Jareonsettasin, Geoffrey Cook, Martin E Schwab, Christine Holt, Roger Keynes

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.8field-weighted citation impact, top 34% 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

2 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
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

8 authors at 2 institutions in 2 countries.

Richard MannsDepartment of Physiology, Development and Neuroscience, University of Cambridge, Cambridge, United Kingdom.
Andre SchmandkeBrain Research Institute, University of Zurich and Department of Health Sciences and Technology, Swiss Federal Institute of Technology, Zurich, Switzerland.
Antonio SchmandkeBrain Research Institute, University of Zurich and Department of Health Sciences and Technology, Swiss Federal Institute of Technology, Zurich, Switzerland.
Prem JareonsettasinDepartment of Physiology, Development and Neuroscience, University of Cambridge, Cambridge, United Kingdom.
Geoffrey CookDepartment of Physiology, Development and Neuroscience, University of Cambridge, Cambridge, United Kingdom.
Martin E SchwabBrain Research Institute, University of Zurich and Department of Health Sciences and Technology, Swiss Federal Institute of Technology, Zurich, Switzerland.
Christine HoltDepartment of Physiology, Development and Neuroscience, University of Cambridge, Cambridge, United Kingdom.
Roger KeynesDepartment of Physiology, Development and Neuroscience, University of Cambridge, Cambridge, United Kingdom.
University of Cambridge · GBUniversity of Zurich · CH

Funding

Wellcome TrustWellcome Trust 08534/Z/08/Z
6 · The paper itself

Abstract

backgroundThe protein Nogo-A regulates axon growth in the developing and mature nervous system, and this is carried out by two distinct domains in the protein, Nogo-A-Δ20 and Nogo-66. The differences in the signalling pathways engaged in axon growth cones by these domains are not well characterized, and have been investigated in this study. METHODOLOGY/PRINCIPAL

findingsWe analyzed growth cone collapse induced by the Nogo-A domains Nogo-A-Δ20 and Nogo-66 using explanted chick dorsal root ganglion neurons growing on laminin/poly-lysine substratum. Collapse induced by purified Nogo-A-Δ20 peptide is dependent on protein synthesis whereas that induced by Nogo-66 peptide is not. Nogo-A-Δ20-induced collapse is accompanied by a protein synthesis-dependent rise in RhoA expression in the growth cone, but is unaffected by proteasomal catalytic site inhibition. Conversely Nogo-66-induced collapse is inhibited ∼ 50% by proteasomal catalytic site inhibition. CONCLUSION/SIGNIFICANCE: Growth cone collapse induced by the Nogo-A domains Nogo-A-Δ20 and Nogo-66 is mediated by signalling pathways with distinguishable characteristics concerning their dependence on protein synthesis and proteasomal function.

Indexed as

AnimalsAnisomycinChick EmbryoGanglia, SpinalGene Expression Regulation, DevelopmentalGrowth ConesLamininLeupeptinsMyelin ProteinsNogo ProteinsPolylysineProteasome Endopeptidase ComplexProteasome InhibitorsProtein BiosynthesisProtein Structure, TertiaryProtein Synthesis Inhibitorsacetylleucyl-leucyl-norleucinalAnisomycinLamininLeupeptinsMyelin ProteinsNogo ProteinsPolylysineProteasome Endopeptidase ComplexProteasome InhibitorsProtein Synthesis InhibitorsRecombinant ProteinsrhoA GTP-Binding Protein

Identifiers

PMID24489789
PMCPMC3906062
OpenAlexW2025762488

What OpenQuestion holds

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LicenceCC BY
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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.