Evidence map›Paper›PMID 15215526›Full record

ArticleProtein science : a publication of the Protein Society2004

Structural conservation in the major facilitator superfamily as revealed by comparative modeling.

Eyal Vardy, Isaiah T Arkin, Kay E Gottschalk, H Ronald Kaback, Shimon Schuldiner

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
  2. Article
  3. Plant glucose transporter structure and function.Pflugers Archiv : European journal of physiology · 2020
    Review
  4. Engineering of Pentose Transport inFrontiers in bioengineering and biotechnology · 2019
    Review
  5. The ins and outs of vesicular monoamine transporters.The Journal of general physiology · 2018
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Identification of molecular hinge points mediating alternating access in the vesicular monoamine transporter VMAT2.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

5 authors at 3 institutions in 2 countries.

Eyal VardyAlexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem, 91904 Israel.
Isaiah T Arkin
Kay E Gottschalk
H Ronald Kaback
Shimon Schuldiner
Hebrew University of Jerusalem · ILUniversity of California, Los Angeles · USWeizmann Institute of Science · 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

The structures of membrane transporters are still mostly unsolved. Only recently, the first two high-resolution structures of transporters of the major facilitator superfamily (MFS) were published. Despite the low sequence similarity of the two proteins involved, lactose permease and glycerol-3-phosphate transporter, the reported structures are highly similar. This leads to the hypothesis that all members of the MFS share a similar structure, regardless of their low sequence identity. To test this hypothesis, we generated models of two other members of the MFS, the Tn10-encoded metal-tetracycline/H(+) antiporter (TetAB) and the rat vesicular monoamine transporter (rVMAT2). The models are based on the two MFS structures and on experimental data. The models for both proteins are in good agreement with the data available and support the notion of a shared fold for all MFS proteins.

Indexed as

Computer SimulationStructural Homology, ProteinAnimalsAntiportersBacterial ProteinsMembrane GlycoproteinsMembrane Transport ProteinsRatsVesicular Biogenic Amine Transport ProteinsVesicular Monoamine Transport ProteinsAntiportersBacterial ProteinsMembrane GlycoproteinsMembrane Transport ProteinstetA protein, BacteriaVesicular Biogenic Amine Transport ProteinsVesicular Monoamine Transport Proteins

Identifiers

PMID15215526
PMCPMC2279927
OpenAlexW2098837867

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.