Evidence map›Paper›PMID 25224873›Full record

ReviewThe Journal of membrane biology2015

The Structure and Function of OxlT, the Oxalate Transporter of Oxalobacter formigenes.

Osigbemhe Iyalomhe, Chandra M Khantwal, Di Cody Kang

Abstract readReview
PubMed Publisher
In one paragraph

Review in The Journal of membrane biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.2field-weighted citation impact, top 46% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. 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

3 authors at 2 institutions in 1 country.

Osigbemhe IyalomheGeriatrics Division, Department of Medicine, Howard University Hospital, 2041 Georgia Ave NW, Washington, DC, 20060, USA, osiyal@jhmi.edu.
Chandra M Khantwal
Di Cody Kang
Howard University Hospital · USStanford University · US

Funding

ION GRADIENTS AND ENERGY COUPLING IN BACTERIAR01GM024195 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI MALONEY, PETER C · 1985 to 2012
$4.5M
NIGMS NIH HHS R01 GM024195
6 · The paper itself

Abstract

OxlT, the oxalate transporter of Oxalobacter formigenes, is a member of the Major Facilitator Superfamily of transporters (MFS), one of the largest groups of membrane proteins with substantial relevance to solute transport physiology, pharmacology, and possible drug development. MFS proteins transport a wide range of substrates such as organic and inorganic anions, sugars, drugs, and neurotransmitters. This review succinctly summarizes experimental work on a model MFS protein, OxlT, beginning with its identification as an electrogenic oxalate/formate exchanger, its three-dimensional structure, and discussion of biochemical and biophysical data that have shed further light on its structure and function. We also discuss the structure and function of OxlT in relation to notable MFS carriers such as LacY and GlpT.

Indexed as

Bacterial ProteinsMembrane Transport ProteinsModels, BiologicalModels, MolecularOxalobacter formigenesBiological Transport, ActiveOxalic AcidBacterial ProteinsMembrane Transport ProteinsOxalic AcidOxlT protein, bacteria

Identifiers

PMID25224873
OpenAlexW2167855056

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.