Evidence map›Paper›PMID 12023896›Full record

ArticleThe Biochemical journal2002

Purification of the Escherichia coli ammonium transporter AmtB reveals a trimeric stoichiometry.

Dan Blakey, Andrew Leech, Gavin H Thomas, Graham Coutts, Kim Findlay, Mike Merrick

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

34 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Function and Regulation of Ammonium Transporters in Plants.International journal of molecular sciences · 2020
    Review
  7. The lipid environment determines the activity of the Escherichia coli ammonium transporter AmtB.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Periplasmic vestibule plays an important role for solute recruitment, selectivity, and gating in the Rh/Amt/MEP superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  17. Article
  18. Article
  19. Detergent binding explains anomalous SDS-PAGE migration of membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2009
    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

6 authors at 1 institution in 1 country.

Dan BlakeyDepartment of Molecular Microbiology, John Innes Centre, Norwich NR4 7UH, UK.
Andrew Leech
Gavin H Thomas
Graham Coutts
Kim Findlay
Mike Merrick
University of East Anglia · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Amt family of high-affinity ammonium transporters is a family of integral membrane proteins that are found in archaea, bacteria, fungi, plants and animals. Furthermore, the family has recently been extended to humans with the recognition that both the erythroid and non-erythroid Rhesus proteins are also ammonium transporters. The Escherichia coli AmtB protein offers a good model system for the Amt family and in order to address questions relating to both its structure and function we have overproduced a histidine-tagged form of the protein (AmtB6H) and purified it to homogeneity. We examined the quaternary structure of AmtB6H (which is active in vivo) by SDS/PAGE, gel-filtration chromatography, dynamic light scattering and sedimentation ultracentrifugation. The protein was resistant to dissociation by SDS and behaved as a stable oligomer on SDS/PAGE. By equilibrium desorption chromatography we determined the mass ratio of dodecyl beta-D-maltoside to AmtB in the detergent-solubilized complex to be 1.03+/-0.03, and this allowed us to calculate, from analytical-ultracentrifugation data, that AmtB purifies as a trimer.

Indexed as

Escherichia coli ProteinsBase SequenceBiopolymersBlotting, WesternCation Transport ProteinsDNA PrimersElectrophoresis, Polyacrylamide GelEscherichia coliMicroscopy, ElectronParticle SizeUltracentrifugationAmtB protein, E coliBiopolymersCation Transport ProteinsDNA PrimersEscherichia coli Proteins

Identifiers

PMID12023896
PMCPMC1222598
OpenAlexW2159594922

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.