Evidence map›Paper›PMID 22444835›Full record

ArticleTrends in biochemical sciences2012

Undecided membrane proteins insert in random topologies. Up, down and sideways: it does not really matter.

Shimon Schuldiner

Abstract read
In one paragraph

Article in Trends in biochemical sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
  2. Bacterial Resistance to Antimicrobial Agents.Antibiotics (Basel, Switzerland) · 2021
    Review
  3. Review
  4. Article
  5. Stable membrane orientations of small dual-topology membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Transforming a drug/H+ antiporter into a polyamine importer by a single mutation.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  14. Role of protons in sugar binding to LacY.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  15. 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.

Shimon SchuldinerDepartment of Biological Chemistry, Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, 91904 Jerusalem, Israel. shimon.schuldiner@huji.ac.il

Funding

MOLECULAR MECHANISM OF ACTIVE NEUROTRANSMITTER TRANSPORTR01NS016708 · NINDS · HEBREW UNIVERSITY OF JERUSALEM · PI KANNER, BARUCH I, SCHULDINER, SHIMON · 1985 to 2014
$3.0M
Mechanisms of Active Neurotransmitter TransportR56NS016708 · NINDS · HEBREW UNIVERSITY OF JERUSALEM · PI KANNER, BARUCH I, SCHULDINER, SHIMON · 2009 to 2009
$306k
NINDS NIH HHS NS16708NINDS NIH HHS R01 NS016708NINDS NIH HHS R56 NS016708
6 · The paper itself

Abstract

It is usually assumed that to ensure proper function, membrane proteins must be inserted in a unique topology. However, a number of dimeric small multidrug transporters can function in the membrane in various topologies. Thus, the dimers can be a random mixture of NiCi (N and C termini facing the cell cytoplasm) and NoCo (N and C termini facing the outside) orientation. In addition, the dimer functions whether the two protomers are parallel (N and C termini of both protomers on the same side of the membrane) or antiparallel (N and C termini of each protomer on opposite sides of the membrane). This unique phenomenon provides strong support for a simple mechanism of transport where the directionality is determined solely by the driving force.

Indexed as

AntiportersCell MembraneEscherichia coliEscherichia coli ProteinsMembrane ProteinsPromoter Regions, GeneticProtein BiosynthesisProtein ConformationProtein MultimerizationProtein TransportStructure-Activity RelationshipAntiportersEmrE protein, E coliEscherichia coli ProteinsMembrane Proteins

Identifiers

PMID22444835
PMCPMC3372635

What OpenQuestion holds

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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.