Evidence map›Paper›PMID 8890153›Full record

ArticleThe EMBO journal1996

Membrane topology and multimeric structure of a mechanosensitive channel protein of Escherichia coli.

P Blount, S I Sukharev, P C Moe, M J Schroeder, H R Guy, C Kung

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

83 citing papers in PubMed, 177 citations in OpenAlex.

  1. Article
  2. Article
  3. Mechanosensitive channel MscL gating transitions coupling with constriction point shift.Protein science : a publication of the Protein Society · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Calcium Regulation of Bacterial Virulence.Advances in experimental medicine and biology · 2020
    Review
  11. Novel compounds that specifically bind and modulate MscL: insights into channel gating mechanisms.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  12. Article
  13. Article
  14. Dynamics of Escherichia coli's passive response to a sudden decrease in external osmolarity.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Article
  16. Article
  17. The application of theBiotechnology reports (Amsterdam, Netherlands) · 2015
    Article
  18. A new antibiotic with potent activity targets MscL.The Journal of antibiotics · 2015
    Article
  19. Article
  20. Review

23 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

P BlountLaboratory of Molecular Biology, University of Wisconsin-Madison 53706, USA.
S I Sukharev
P C Moe
M J Schroeder
H R Guy
C Kung
University of Wisconsin–Madison · US

Funding

Study of mechanosensation using microbial TRP channelsR01GM047856 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI KUNG, CHING · 1994 to 2008
$2.2M
NIGMS NIH HHS GM47856
6 · The paper itself

Abstract

We have studied the membrane topology and multimeric structure of a mechanosensitive channel, MscL, which we previously isolated and cloned from Escherichia coli. We have localized this 15-kDa protein to the inner membrane and, by PhoA fusion, have shown that it contains two transmembrane domains with both the amino and carboxyl termini on the cytoplasmic side. Mutation of the glutamate at position 56 to histidine led to changes in channel kinetics which were dependent upon the pH on the periplasmic, but not cytoplasmic side of the membrane, providing additional evidence for the periplasmic positioning of this part of the molecule. Tandems of two MscL subunits expressed as a single polypeptide formed functional channels, suggesting an even number of transmembrane domains per subunit (amino and carboxyl termini on the same side of the membrane), and an even number of subunits per functional complex. Finally, cross-linking studies suggest that the functional MscL complex is a homohexamer. In summary, these data are all consistent with a protein domain assignment and topological model which we propose and discuss.

Indexed as

Escherichia coli ProteinsAlkaline PhosphataseAmino Acid SequenceCytoplasmDeoxyribonuclease BamHIEscherichia coliHistidineIntracellular MembranesIon ChannelsKineticsLiposomesMolecular Sequence DataMutagenesis, Site-DirectedProtein ConformationStructure-Activity RelationshipAlkaline PhosphataseDeoxyribonuclease BamHIEscherichia coli ProteinsHistidineIon ChannelsLiposomesMscL protein, E coliNon-programmatic

Identifiers

PMID8890153
PMCPMC452216
OpenAlexW1963764470

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.