Evidence map›Paper›PMID 18216284›Full record

ArticleMolecular biology of the cell2008

APY-1, a novel Caenorhabditis elegans apyrase involved in unfolded protein response signalling and stress responses.

D Uccelletti, A Pascoli, F Farina, A Alberti, P Mancini, C B Hirschberg, C Palleschi

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.2field-weighted citation impact, top 25% 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

21 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
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  5. Virulence · 2019
    Article
  6. Frontiers in microbiology · 2018
    Article
  7. Article
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  10. Review
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  19. Article
  20. Identification of CANT1 mutations in Desbuquois dysplasia.American journal of human genetics · 2009
    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

7 authors at 4 institutions in 3 countries.

D UccellettiDepartment of Developmental and Cell Biology, University of Rome "La Sapienza," 00185 Rome, Italy.
A Pascoli
F Farina
A Alberti
P Mancini
C B Hirschberg
C Palleschi
Sapienza University of Rome · ITBoston University · USCentre de Génétique Moléculaire · FRUniversité Paris-Sud · FR

Funding

GLYCOSYLATION MECHANISMS OF CELL LIPIDS AND PROTEINSR01GM030365 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI HIRSCHBERG, CARLOS BENJAMIN · 1985 to 2009
$3.1M
GLYCOSYLATION MECHANISMSR37GM030365 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI HIRSCHBERG, CARLOS BENJAMIN · 1991 to 2000
$365k
NIGMS NIH HHS GM 30365NIGMS NIH HHS R01 GM030365NIGMS NIH HHS R37 GM030365
6 · The paper itself

Abstract

Protein glycosylation modulates a wide variety of intracellular events and dysfunction of the glycosylation pathway has been reported in a variety of human pathologies. Endo-apyrases have been suggested to have critical roles in protein glycosylation and sugar metabolism. However, deciphering the physiological relevance of Endo-apyrases activity has actually proved difficult, owing to their complexity and the functional redundancy within the family. We report here that a UDP/GDPase, homologous to the human apyrase Scan-1, is present in the membranes of Caenorhabditis elegans, encoded by the ORF F08C6.6 and hereinafter-named APY-1. We showed that ER stress induced by tunicamycin or high temperature resulted in increased transcription of apy-1. This increase was not observed in C. elegans mutants defective in ire-1 or atf-6, demonstrating the requirement of both ER stress sensors for up-regulation of apy-1. Depletion of APY-1 resulted in constitutively activated unfolded protein response. Defects in the pharynx and impaired organization of thin fibers in muscle cells were observed in adult worms depleted of APY-1. Some of the apy-1(RNAi) phenotypes are suggestive of premature aging, because these animals also showed accumulation of lipofuscin and reduced lifespan that was not dependent on the functioning of DAF-2, the receptor of the insulin/IGF-1 signaling pathway.

Indexed as

AnimalsAnimals, Genetically ModifiedApyraseBase SequenceCaenorhabditis elegansCaenorhabditis elegans ProteinsDNA, HelminthEndoplasmic ReticulumGene Expression RegulationGenes, HelminthGlycosylationGreen Fluorescent ProteinsMutationPharynxProtein FoldingPyrophosphatasesApyraseCaenorhabditis elegans ProteinsDNA, HelminthGreen Fluorescent ProteinsPyrophosphatasesRecombinant Fusion Proteinsuridine diphosphatase

Identifiers

PMID18216284
PMCPMC2291423
OpenAlexW2166635722

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.