Evidence map›Paper›PMID 16329762›Full record

ArticleBMC genomics2005

The angiotensin-converting enzyme (ACE) gene family of Anopheles gambiae.

Susan Burnham, Judith A Smith, Alison J Lee, R Elwyn Isaac, Alan D Shirras

Open access · goldAbstract read
In one paragraph

Article in BMC genomics, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

15 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. International journal of molecular sciences · 2024
    Article
  4. Proteomic analyses of venom from a Spider Hawk,The journal of venomous animals and toxins including tropical diseases · 2023
    Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. ACE for all - a molecular perspective.Journal of cell communication and signaling · 2014
    Article
  12. Article
  13. Article
  14. Article
  15. 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

5 authors at 2 institutions in 1 country.

Susan BurnhamFaculty of Biological Sciences, Miall Building, University of Leeds, Clarendon Way, Leeds LS2 9JT, UK. bgysbu@leeds.ac.uk
Judith A Smith
Alison J Lee
R Elwyn Isaac
Alan D Shirras
University of Leeds · GBLancaster University · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

backgroundMembers of the M2 family of peptidases, related to mammalian angiotensin converting enzyme (ACE), play important roles in regulating a number of physiological processes. As more invertebrate genomes are sequenced, there is increasing evidence of a variety of M2 peptidase genes, even within a single species. The function of these ACE-like proteins is largely unknown. Sequencing of the A. gambiae genome has revealed a number of ACE-like genes but probable errors in the Ensembl annotation have left the number of ACE-like genes, and their structure, unclear.

resultsTBLASTN and sequence analysis of cDNAs revealed that the A. gambiae genome contains nine genes (AnoACE genes) which code for proteins with similarity to mammalian ACE. Eight of these genes code for putative single domain enzymes similar to other insect ACEs described so far. AnoACE9, however, has several features in common with mammalian somatic ACE such as a two domain structure and a hydrophobic C terminus. Four of the AnoACE genes (2, 3, 7 and 9) were shown to be expressed at a variety of developmental stages. Expression of AnoACE3, AnoACE7 and AnoACE9 is induced by a blood meal, with AnoACE7 showing the largest (approximately 10-fold) induction.

conclusionGenes coding for two-domain ACEs have arisen several times during the course of evolution suggesting a common selective advantage to having an ACE with two active-sites in tandem in a single protein. AnoACE7 belongs to a sub-group of insect ACEs which are likely to be membrane-bound and which have an unusual, conserved gene structure.

Indexed as

Amino Acid SequenceAnimalsAnophelesBinding SitesCloning, MolecularConserved SequenceDNA, ComplementaryEvolution, MolecularExonsExpressed Sequence TagsFemaleGenomeMaleModels, GeneticMolecular Sequence DataMultigene FamilyDNA, ComplementaryPeptidyl-Dipeptidase A

Identifiers

PMID16329762
PMCPMC1325048
OpenAlexW2153823153

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.