Evidence map›Paper›PMID 20109220›Full record

ArticleBMC developmental biology2010

Characterization of the astacin family of metalloproteases in C. elegans.

Ja-On Park, Jie Pan, Frank Möhrlen, Marcus-Oliver Schupp, Robert Johnsen, David L Baillie, Richard Zapf, Donald G Moerman, Harald Hutter

Open access · bronzeAbstract read
In one paragraph

Article in BMC developmental biology, 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
0.9field-weighted citation impact, top 29% 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, 66 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Invade or die: behaviours and biochemical mechanisms that drive skin penetration inPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. A Zinc MetalloproteaseFrontiers in cell and developmental biology · 2021
    Article
  15. Journal of developmental biology · 2020
    Review
  16. Article
  17. Article
  18. Article
  19. Transcriptome Analysis of the NematodeFrontiers in physiology · 2020
    Article
  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

9 authors at 2 institutions in 3 countries.

Ja-On ParkDepartment of Biological Sciences, Simon Fraser University, Burnaby, BC, Canada.
Jie Pan
Frank Möhrlen
Marcus-Oliver Schupp
Robert Johnsen
David L Baillie
Richard Zapf
Donald G Moerman
Harald Hutter
Simon Fraser University · CAHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAstacins are a large family of zinc metalloproteases found in bacteria and animals. They have diverse roles ranging from digestion of food to processing of extracellular matrix components. The C. elegans genome contains an unusually large number of astacins, of which the majority have not been functionally characterized yet.

resultsWe analyzed the expression pattern of previously uncharacterized members of the astacin family to try and obtain clues to potential functions. Prominent sites of expression for many members of this family are the hypodermis, the alimentary system and several specialized cells including sensory sheath and sockets cells, which are located at openings in the body wall. We isolated mutants affecting representative members of the various subfamilies. Mutants in nas-5, nas-21 and nas-39 (the BMP-1/Tolloid homologue) are viable and have no apparent phenotypic defects. Mutants in nas-6 and nas-6; nas-7 double mutants are slow growing and have defects in the grinder of the pharynx, a cuticular structure important for food processing.

conclusionsExpression data and phenotypic characterization of selected family members suggest a diversity of functions for members of the astacin family in nematodes. In part this might be due to extracellular structures unique to nematodes.

Indexed as

AnimalsCaenorhabditis elegansMetalloendopeptidasesMetalloproteasesPhylogenyastacinMetalloendopeptidasesMetalloproteases

Identifiers

PMID20109220
PMCPMC2824743
OpenAlexW2146274451

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.