Evidence map›Paper›PMID 22100111›Full record

ReviewCurrent opinion in structural biology2012

Analyzing conformational changes in the transport cycle of EmrE.

Katherine Henzler-Wildman

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Microsecond Motion of the Bacterial Transporter EmrE in Lipid Bilayers.Journal of the American Chemical Society · 2023
    Article
  2. Review
  3. Protonation-dependent conformational dynamics of the multidrug transporter EmrE.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  4. Article
  5. 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.

Katherine Henzler-WildmanDepartment of Biochemistry and Molecular Biophysics Washington University School of Medicine, St. Louis, MO 63110, United States. khenzler@biochem.wustl.edu

Funding

TRANSPORT MECHANISM OF THE MULTIDRUG RESISTANCE EFFLUX PROTEIN, EMRER01GM095839 · NIGMS · WASHINGTON UNIVERSITY · PI HENZLER-WILDMAN, KATHERINE ANNE · 2011 to 2020
$3.1M
NIGMS NIH HHS R01 GM095839
6 · The paper itself

Abstract

The small multidrug resistance transporters represent a unique model system for studying the mechanism of secondary active transport and membrane protein evolution. However, this seemingly simple protein has been highly controversial. Recent studies have provided experimental evidence that EmrE exists as an asymmetric dimer that exchanges between identical inward-facing and outward-facing states. Re-examination of the published literature in light of these findings fills in many details of the microscopic steps in the transport cycle. Future work will need to examine how the symmetry observed in vitro affects EmrE function in the asymmetric environment of its native Escherichia coli membrane.

Indexed as

AntiportersBiological TransportEscherichia coliEscherichia coli ProteinsKineticsProtein ConformationAntiportersEmrE protein, E coliEscherichia coli Proteins

Identifiers

PMID22100111
PMCPMC3288627

What OpenQuestion holds

Textmetadata
LicenceTDM
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.