Evidence map›Paper›PMID 15350194›Full record

ArticleThe Biochemical journal2005

Tissue specificity and regulation of the N-terminal diversity of reticulon 3.

Franck Di Scala, Luc Dupuis, Christian Gaiddon, Marc De Tapia, Natasa Jokic, Jose-Luis Gonzalez de Aguilar, Jean-Sébastien Raul, Bertrand Ludes, Jean-Philippe Loeffler

RetractedOpen access · bronzeAbstract readRetracted Publication
In one paragraph

Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Impact of RTN3 deficiency on expression of BACE1 and amyloid deposition.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  12. RTN/Nogo in forming Alzheimer's neuritic plaques.Neuroscience and biobehavioral reviews · 2010
    Article
  13. Expression of reticulon 3 in Alzheimer's disease brain.Neuropathology and applied neurobiology · 2009
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Franck Di ScalaLaboratoire de Signalisations Moléculaires et Neurodégénérescence, EA 3433, Université Louis Pasteur, Faculté de Médecine, 11 rue Humann, 67085 Strasbourg Cedex, France.
Luc Dupuis
Christian Gaiddon
Marc De Tapia
Natasa Jokic
Jose-Luis Gonzalez de Aguilar
Jean-Sébastien Raul
Bertrand Ludes
Jean-Philippe Loeffler
Mécanismes Centraux et Périphériques de la Neurodégénérescence · FRInstitut de Médecine et d'Epidémiologie Africaines · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Over the last few years, the widely distributed family of reticulons (RTNs) is receiving renewed interest because of the implication of RTN4/Nogo in neurite regeneration. Four genes were identified in mammals and are referred to as RTN1, 2, 3 and the neurite outgrowth inhibitor RTN4/Nogo. In the present paper, we describe the existence of five new isoforms of RTN3 that differ in their N-termini, and analysed their tissue distribution and expression in neurons. We redefined the structure of human and murine rtn3 genes, and identified two supplementary exons that may generate up to seven putative isoforms arising by alternative splicing or differential promoter usage. We confirmed the presence of five of these isoforms at the mRNA and protein levels, and showed their preferential expression in the central nervous system. We analysed rtn3 expression in the cerebellum further, and observed increased levels of several of the RTN3 isoforms during cerebellum development and during in vitro maturation of cerebellar granule cells. This pattern of expression paralleled that shown by RTN4/Nogo isoforms. Specifically, RTN3A1 expression was down-regulated upon cell death of cerebellar granule neurons triggered by potassium deprivation. Altogether, our results demonstrate that the rtn3 gene generates multiple isoforms varying in their N-termini, and that their expression is tightly regulated in neurons. These findings suggest that RTN3 isoforms may contribute, by as yet unknown mechanisms, to neuronal survival and plasticity.

Indexed as

Gene Expression ProfilingGene Expression RegulationAlternative SplicingAnimalsApoptosisBase SequenceCarrier ProteinsCell DifferentiationCells, CulturedCerebellumCloning, MolecularComputational BiologyExonsHumansIntronsMembrane ProteinsCarrier ProteinsMembrane ProteinsMyelin ProteinsNerve Tissue ProteinsNogo ProteinsProtein IsoformsRNA, MessengerRNA Splice SitesRTN3 protein, humanRtn3 protein, mouseRTN4 protein, humanRtn4 protein, mouse

Identifiers

PMID15350194
PMCPMC1134680
OpenAlexW2067105566

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.