Evidence map›Paper›PMID 24648514›Full record

ArticleThe Journal of biological chemistry2014

Decreased O-linked GlcNAcylation protects from cytotoxicity mediated by huntingtin exon1 protein fragment.

Amit Kumar, Pankaj Kumar Singh, Rashmi Parihar, Vibha Dwivedi, Subhash C Lakhotia, Subramaniam Ganesh

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

37 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. ProteinMetabolites · 2022
    Review
  12. In vitro selection of blackberry (Plant biotechnology (Tokyo, Japan) · 2022
    Article
  13. Article
  14. Pathophysiological interplay betweenProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. O-GlcNAcylation in health and neurodegenerative diseases.Experimental & molecular medicine · 2021
    Review
  16. Article
  17. Article
  18. Review
  19. Review
  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

6 authors at 2 institutions in 1 country.

Amit KumarFrom the Department of Biological Sciences and Bioengineering, Indian Institute of Technology, Kanpur 208016 and.
Pankaj Kumar Singh
Rashmi Parihar
Vibha Dwivedi
Subhash C Lakhotia
Subramaniam Ganesh
Indian Institute of Technology Kanpur · INBanaras Hindu University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

O-GlcNAcylation is an important post-translational modification of proteins and is known to regulate a number of pathways involved in cellular homeostasis. This involves dynamic and reversible modification of serine/threonine residues of different cellular proteins catalyzed by O-linked N-acetylglucosaminyltransferase and O-linked N-acetylglucosaminidase in an antagonistic manner. We report here that decreasing O-GlcNAcylation enhances the viability of neuronal cells expressing polyglutamine-expanded huntingtin exon 1 protein fragment (mHtt). We further show that O-GlcNAcylation regulates the basal autophagic process and that suppression of O-GlcNAcylation significantly increases autophagic flux by enhancing the fusion of autophagosome with lysosome. This regulation considerably reduces toxic mHtt aggregates in eye imaginal discs and partially restores rhabdomere morphology and vision in a fly model for Huntington disease. This study is significant in unraveling O-GlcNAcylation-dependent regulation of an autophagic process in mediating mHtt toxicity. Therefore, targeting the autophagic process through the suppression of O-GlcNAcylation may prove to be an important therapeutic approach in Huntington disease.

Indexed as

AutophagyAcylationAnimalsCytotoxinsDisease Models, AnimalDrosophila melanogasterDrosophila ProteinsHuntingtin ProteinHuntington DiseaseImaginal DiscsMiceMicrotubule-Associated ProteinsNeuronsCytotoxinsDrosophila ProteinsHtt protein, DrosophilaHuntingtin ProteinMicrotubule-Associated ProteinsAutophagyNeurodegenerative DiseasesO-GlcNAcylationPost-translational ModificationProtein Aggregation

Identifiers

PMID24648514
PMCPMC4036360
OpenAlexW2055727332

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.