Evidence map›Paper›PMID 24688744›Full record

ReviewComputational and structural biotechnology journal2013

Inverted topologies in membrane proteins: a mini-review.

Amanda M Duran, Jens Meiler

Open access · goldAbstract readReview
In one paragraph

Review in Computational and structural biotechnology journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

25 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Structural and mechanistic basis of the central energy-converting methyltransferase complex of methanogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
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  11. Article
  12. The Archaeal NaFrontiers in chemistry · 2021
    Review
  13. Article
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  15. Article
  16. Article
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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

2 authors at 1 institution in 1 country.

Amanda M DuranCenter for Structural Biology, Department of Chemistry, Vanderbilt University, Nashville, TN 37212, USA.
Jens MeilerCenter for Structural Biology, Department of Chemistry, Vanderbilt University, Nashville, TN 37212, USA.
Vanderbilt University · US

Funding

Membrane Protein Structure Elucidation from sparse NMR data (KAMP)R01GM080403 · NIGMS · VANDERBILT UNIVERSITY · PI MEILER, JENS · 2007 to 2019
$3.0M
Cheminformatics of Allosteric mGluR Modulation promotes Therapeutic DevelopmentR01MH090192 · NIMH · VANDERBILT UNIVERSITY · PI MEILER, JENS · 2010 to 2013
$1.5M
Computational Design of Protein-Ligand Interfaces - a Therapeutic StrategyR01GM099842 · NIGMS · VANDERBILT UNIVERSITY · PI MEILER, JENS · 2012 to 2015
$1.3M
Small Molecule Probes to Investigate Structure and Function of Y ReceptorsR01DK097376 · NIDDK · VANDERBILT UNIVERSITY · PI MEILER, JENS, WEAVER, C DAVID · 2013 to 2015
$1.0M
NIDDK NIH HHS R01 DK097376NIGMS NIH HHS R01 GM080403NIGMS NIH HHS R01 GM099842NIMH NIH HHS R01 MH090192
6 · The paper itself

Abstract

Helical membrane proteins such as transporters, receptors, or channels often exhibit structural symmetry. Symmetry is perfect in homo-oligomers consisting of two or more copies of the same protein chain. Intriguingly, in single chain membrane proteins, often internal pseudo-symmetry is observed, in particular in transporters and channels. In several cases single chain proteins with pseudo-symmetry exist, that share the fold with homo-oligomers suggesting evolutionary pathways that involve gene duplication and fusion. It has been hypothesized that such evolutionary pathways allow for the rapid development of large proteins with novel functionality. At the same time symmetry can be leveraged to recognize highly symmetric substrates such as ions. Here we review helical transporter proteins with an inverted two-fold pseudo-symmetry. In this special scenario the symmetry axis lies in the membrane plane. As a result, the putative ancestral monomeric protein would insert in both directions into the membrane and its open-to-the-inside and open-to-the-outside conformations would be structurally identical and iso-energetic, giving a possible evolutionary pathway to create a transporter protein that needs to flip between the two states.

Indexed as

gene duplicationgene fusioninverted topologyMembrane proteinpseudo-symmetrysymmetry

Identifiers

PMID24688744
PMCPMC3962082
OpenAlexW2088433350

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.