Evidence map›Paper›PMID 23074248›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance.

Xiaozhe Zhang, Jingjing Wang, Yue Feng, Jingpeng Ge, Wenfei Li, Wending Sun, Irene Iscla, Jie Yu, Paul Blount, Yang Li and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

39 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. The MscS-like channel YnaI has a gating mechanism based on flexible pore helices.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. 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

11 authors at 5 institutions in 2 countries.

Xiaozhe ZhangKey Laboratory for Protein Sciences of Ministry of Education, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Jingjing Wang
Yue Feng
Jingpeng Ge
Wenfei Li
Wending Sun
Irene Iscla
Jie Yu
Paul Blount
Yang Li
Maojun Yang
Center for Life Sciences · CNTsinghua University · CNChinese Academy of Sciences · CNThe University of Texas Southwestern Medical Center · USShanghai Institute of Materia Medica · CN

Funding

MOLECULAR MECHANISMS OF MECHANOSENSITIVE CHANNEL GATINGR01GM061028 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI BLOUNT, PAUL · 2000 to 2017
$4.7M
NIGMS NIH HHS GM61028NIGMS NIH HHS R01 GM061028
6 · The paper itself

Abstract

Mechanosensitive (MS) channels are universal cellular membrane pores. Bacterial MS channels, as typified by MS channel of small conductance (MscS) from Escherichia coli (EcMscS), release osmolytes under hypoosmotic conditions. MS channels are known to be ion selective to different extents, but the underlying mechanism remains poorly understood. Here we identify an anion-selective MscS channel from Thermoanaerobacter tengcongensis (TtMscS). The structure of TtMscS closely resembles that of EcMscS, but it lacks the large cytoplasmic equatorial portals found in EcMscS. In contrast, the cytoplasmic pore formed by the C-terminal β-barrel of TtMscS is larger than that of EcMscS and has a strikingly different pattern of electrostatic surface potential. Swapping the β-barrel region between TtMscS and EcMscS partially switches the ion selectivity. Our study defines the role of the β-barrel in the ion selection of an anion-selective MscS channel and provides a structural basis for understanding the ion selectivity of MscS channels.

Indexed as

AnionsMechanotransduction, CellularAmino Acid SequenceEscherichia coli ProteinsIon ChannelsModels, MolecularMolecular Sequence DataProtein ConformationSequence Homology, Amino AcidStatic ElectricityThermoanaerobacterAnionsEscherichia coli ProteinsIon ChannelsMscS protein, E coli

Identifiers

PMID23074248
PMCPMC3497791
OpenAlexW2127827053

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.