Evidence map›Paper›PMID 18957377›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2009

Review. The mammalian proton-coupled peptide cotransporter PepT1: sitting on the transporter-channel fence?

David Meredith

Open access · hybridAbstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Di- and tripeptide transport in vertebrates: the contribution of teleost fish models.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2017
    Review
  5. Molecular identification and functional characteristics of peptide transporters in the bonnethead shark (Sphyrna tiburo).Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2016
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Peptide transporter DtpA has two alternate conformations, one of which is promoted by inhibitor binding.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  11. Review
  12. Article
  13. Assimilation of water and dietary ions by the gastrointestinal tract during digestion in seawater-acclimated rainbow trout.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2011
    Article
  14. Article
  15. Article
  16. Article
  17. Introduction. The blurred boundary between channels and transporters.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 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

1 author at 1 institution in 1 country.

David MeredithSchool of Life Sciences, Oxford Brookes University, Gipsy Lane, Headington, Oxford, UK. dmeredith@brookes.ac.uk
Oxford Brookes University · GB

Funding

Cancer Research UKWellcome Trust
6 · The paper itself

Abstract

The proton-coupled di- and tripeptide transporter PepT1 (SLC15a1) is the major route by which dietary nitrogen is taken up from the small intestine, as well as being the route of entry for important therapeutic (pro)drugs such as the beta-lactam antibiotics, angiotensin-converting enzyme inhibitors and antiviral and anti-cancer agents. PepT1 is a member of the major facilitator superfamily of 12 transmembrane domain transporter proteins. Expression studies in Xenopus laevis on rabbit PepT1 that had undergone site-directed mutagenesis of a conserved arginine residue (arginine282 in transmembrane domain 7) to a glutamate revealed that this residue played a role in the coupling of proton and peptide transport and prevented the movement of non-coupled ions during the transporter cycle. Mutations of arginine282 to other non-positive residues did not uncouple proton-peptide cotransport, but did allow additional ion movements when substrate was added. By contrast, mutations to positive residues appeared to function the same as wild-type. These findings are discussed in relation to the functional role that arginine282 may play in the way PepT1 operates, together with structural information from the homology model of PepT1 based on the Escherichia coli lactose permease crystal structure.

Indexed as

Amino Acid SequenceAnimalsMammalsPeptide Transporter 1Protein ConformationSymportersPeptide Transporter 1Symporters

Identifiers

PMID18957377
PMCPMC2674094
OpenAlexW2126151264

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.