Evidence map›Paper›PMID 18537473›Full record

ReviewAnnual review of microbiology2008

Ins and outs of major facilitator superfamily antiporters.

Christopher J Law, Peter C Maloney, Da-Neng Wang

Abstract readReview
In one paragraph

Review in Annual review of microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 246 papers.

0numbers the graph read from it
0cells of the map it votes in
246citing papers in PubMed
–field-weighted citation impact
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

246 citing papers in PubMed.

  1. Article
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  15. Article
  16. Review
  17. Key sugar transporters drive development and pathogenicity inFrontiers in cellular and infection microbiology · 2025
    Article
  18. Article
  19. Variation at the major facilitator superfamilyFrontiers in plant science · 2025
    Article
  20. Mycology · 2025
    Article

186 more citing papers are in PubMed but not listed here.

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.

Christopher J LawThe Helen L. and Martin S. Kimmel Center for Biology and Medicine at the Skirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, NY 10016, USA. law@saturn.med.nyu.edu
Peter C Maloney
Da-Neng Wang

Funding

ION GRADIENTS AND ENERGY COUPLING IN BACTERIAR01GM024195 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI MALONEY, PETER C · 1985 to 2012
$4.5M
STRUCTURAL STUDIES OF SUGAR TRANSPORTERSR01DK053973 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WANG, DANENG · 1998 to 2014
$3.6M
Structural and Mechanistic Characterization of Neurotransmitter Reuptake InhibitiR01MH083840 · NIMH · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WANG, DANENG · 2008 to 2012
$2.2M
Ion Gradients and Energy Coupling in BacteriaR56GM024195 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI MALONEY, PETER C · 2007 to 2007
$515k
NIDDK NIH HHS DK-053973NIDDK NIH HHS R01 DK053973NIGMS NIH HHS GM-24195NIGMS NIH HHS R01 GM024195NIGMS NIH HHS R56 GM024195
6 · The paper itself

Abstract

The major facilitator superfamily (MFS) represents the largest group of secondary active membrane transporters, and its members transport a diverse range of substrates. Recent work shows that MFS antiporters, and perhaps all members of the MFS, share the same three-dimensional structure, consisting of two domains that surround a substrate translocation pore. The advent of crystal structures of three MFS antiporters sheds light on their fundamental mechanism; they operate via a single binding site, alternating-access mechanism that involves a rocker-switch type movement of the two halves of the protein. In the sn-glycerol-3-phosphate transporter (GlpT) from Escherichia coli, the substrate-binding site is formed by several charged residues and a histidine that can be protonated. Salt-bridge formation and breakage are involved in the conformational changes of the protein during transport. In this review, we attempt to give an account of a set of mechanistic principles that characterize all MFS antiporters.

Indexed as

AntiportersBacterial ProteinsBinding SitesEscherichia coli ProteinsKineticsMembrane Transport ProteinsModels, MolecularProtein ConformationAntiportersBacterial ProteinsEmrD protein, E coliEscherichia coli ProteinsGlpT protein, E coliMembrane Transport ProteinsOxlT protein, bacteria

Identifiers

PMID18537473
PMCPMC2612782

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.