Evidence map›Paper›PMID 26488689›Full record

ReviewChannels (Austin, Tex.)2016

Structures of multidrug and toxic compound extrusion transporters and their mechanistic implications.

Min Lu

Open access · goldAbstract readReview
In one paragraph

Review in Channels (Austin, Tex.), 2016. 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
3.2field-weighted citation impact, top 6% 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, 72 citations in OpenAlex.

  1. Article
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  12. The structure of theProceedings of the National Academy of Sciences of the United States of America · 2021
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  13. Review
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  19. Sequence and structural determinants of ligand-dependent alternating access of a MATE transporter.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

1 author at 1 institution in 1 country.

Min Lua Department of Biochemistry & Molecular Biology , Rosalind Franklin University of Medicine & Science , Chicago , IL , USA.
Rosalind Franklin University of Medicine and Science · US

Funding

Structural mechanisms of multidrug extrusion by the MATE antiportersR01GM094195 · NIGMS · ROSALIND FRANKLIN UNIV OF MEDICINE & SCI · PI LU, MIN · 2010 to 2018
$2.7M
NIGMS NIH HHS R01 GM094195NIGMS NIH HHS R01-GM094195
6 · The paper itself

Abstract

Multidrug resistance poses grand challenges to the effective treatment of infectious diseases and cancers. Integral membrane proteins from the multidrug and toxic compound extrusion (MATE) family contribute to multidrug resistance by exporting a wide variety of therapeutic drugs across cell membranes. MATE proteins are conserved from bacteria to humans and can be categorized into the NorM, DinF and eukaryotic subfamilies. MATE transporters hold great appeal as potential therapeutic targets for curbing multidrug resistance, yet their transport mechanism remains elusive. During the past 5 years, X-ray structures of 4 NorM and DinF transporters have been reported and guided biochemical studies to reveal how MATE transporters extrude different drugs. Such advances, although substantial, have yet to be discussed collectively. Herein I review these structures and the unprecedented mechanistic insights that have been garnered from those structure-inspired studies, as well as lay out the outstanding questions that present exciting opportunities for future work.

Indexed as

Genes, MDRAmino Acid SequenceAnti-Infective AgentsAntineoplastic AgentsAntiportersBacterial ProteinsCommunicable DiseasesConserved SequenceDrug Resistance, MultipleEscherichia coli ProteinsGene ExpressionHumansNeoplasmsOrganic Cation Transport ProteinsProtein DomainsProtein Structure, SecondaryAnti-Infective AgentsAntineoplastic AgentsAntiportersBacterial ProteinsDinF protein, E coliEscherichia coli ProteinsNorM protein, bacteriaOrganic Cation Transport Proteinscation bindingmembrane transportermultidrug efflux inhibitormultidrug resistancesubstrate recognition

Identifiers

PMID26488689
PMCPMC4960993
OpenAlexW2276180411

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.