Evidence map›Paper›PMID 20130186›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2010

The N-glycanase png-1 acts to limit axon branching during organ formation in Caenorhabditis elegans.

Nasrin Habibi-Babadi, Anna Su, Carlos E de Carvalho, Antonio Colavita

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
0.6field-weighted citation impact, top 40% 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

28 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
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  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. JF1/B6F1 Ngly1Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2021
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Loss of RAD-23 Protects Against Models of Motor Neuron Disease by Enhancing Mutant Protein Clearance.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  19. Generation and degradation of free asparagine-linked glycans.Cellular and molecular life sciences : CMLS · 2015
    Review
  20. Endo-β-N-acetylglucosaminidase forms N-GlcNAc protein aggregates during ER-associated degradation in Ngly1-defective cells.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

4 authors at 2 institutions in 1 country.

Nasrin Habibi-BabadiOttawa Health Research Institute, Neuroscience Program, University of Ottawa, Ontario K1H 8M5, Canada.
Anna Su
Carlos E de Carvalho
Antonio Colavita
Heart and Stroke Foundation · CAUniversity of Ottawa · CA

Funding

Canadian Institutes of Health Research MOP-69049
6 · The paper itself

Abstract

Peptide:N-glycanases (PNGases) are cytoplasmic de-N-glycosylation enzymes that have been shown in cultured cells to facilitate the degradation of misfolded glycoproteins during endoplasmic reticulum-associated degradation and in the processing of major histocompatibility complex class I antigens for proper cell-surface presentation. The gene encoding PNGase activity was initially described in budding yeast (Png1p) and shown to be highly conserved from yeast to humans, but physiological roles in higher organisms have not been elucidated. Here we describe peripheral nervous system defects associated with the first loss-of-function mutations in an animal PNGase. Mutations in png-1, the Caenorhabditis elegans PNGase ortholog, result in an increase in axon branching during morphogenesis of the vulval egg-laying organ and egg-laying behavior changes. Neuronal defects include an increase in the branched morphology of the VC4 and VC5 egg-laying neurons as well as inappropriate branches from axons that run adjacent to the vulva but would normally remain unbranched. We show that png-1 is widely expressed and can act from both neurons and epithelial cells to restrict axon branching. A deletion allele of the DNA repair gene rad-23, orthologs of which are known to physically interact with PNGases in yeast and mammals, displays similar axon branching defects and genetic interactions with png-1. In summary, our analysis reveals a novel developmental role for a PNGase and Rad-23 in the regulation of neuronal branching during organ innervation.

Indexed as

AnimalsAnimals, Genetically ModifiedAxonsCaenorhabditis elegansCaenorhabditis elegans ProteinsFemaleMutationOrganogenesisOvulationPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseVulvaCaenorhabditis elegans ProteinsPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidaseRad-23 protein, C elegans

Identifiers

PMID20130186
PMCPMC6634002
OpenAlexW2088822805

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.