Evidence map›Paper›PMID 12626684›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2003

Two families of mechanosensitive channel proteins.

Christopher D Pivetti, Ming-Ren Yen, Samantha Miller, Wolfgang Busch, Yi-Hsiung Tseng, Ian R Booth, Milton H Saier

Abstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
4.9field-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

111 citing papers in PubMed, 244 citations in OpenAlex.

  1. The MscS channel frombioRxiv : the preprint server for biology · 2026
    Article
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  8. Sonogenetics in the Treatment of Chronic Diseases: A New Method for Cell Regulation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Review
  9. Effects ofMicroorganisms · 2024
    Article
  10. Biofilm · 2024
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Genetic Basis ofLife (Basel, Switzerland) · 2023
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

51 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

7 authors at 4 institutions in 4 countries.

Christopher D PivettiDivision of Biology, University of California San Diego, La Jolla, California 92093-0116, USA.
Ming-Ren Yen
Samantha Miller
Wolfgang Busch
Yi-Hsiung Tseng
Ian R Booth
Milton H Saier
University of California, San Diego · USInstitute of Medical Sciences · INNational Chung Hsing University · TWUniversity of Aberdeen · GB

Funding

Mechanism of Carbohydrate Transport in BacteriaR01GM064368 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI SAIER, MILTON H. · 2001 to 2004
$1.4M
ATP DEPENDENT PROTEIN KINASES IN GRAM POSITIVE BACTERIAR01GM055434 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI SAIER, MILTON H. · 1997 to 2004
$1.1M
NIGMS NIH HHS GM55434NIGMS NIH HHS GM64368NIGMS NIH HHS R01 GM055434NIGMS NIH HHS R01 GM064368Wellcome Trust
6 · The paper itself

Abstract

Mechanosensitive (MS) channels that provide protection against hypoosmotic shock are found in the membranes of organisms from the three domains of life: bacteria, archaea, and eucarya. Two families of ubiquitous MS channels are recognized, and these have been designated the MscL and MscS families. A high-resolution X-ray crystallographic structure is available for a member of the MscL family, and extensive molecular genetic, biophysical, and biochemical studies conducted in many laboratories have allowed postulation of a gating mechanism allowing the interconversion of a tightly closed state and an open state that controls transmembrane ion and metabolite fluxes. In contrast to the MscL channel proteins, which are of uniform topology, the much larger MscS family includes protein members with topologies that are predicted to vary from 3 to 11 alpha-helical transmembrane segments (TMSs) per polypeptide chain. Sequence analyses reveal that the three C-terminal TMSs of MscS channel proteins are conserved among family members and that the third of these three TMSs exhibits a 20-residue motif that is shared by the channel-forming TMS (TMS 1) of the MscL proteins. We propose that this C-terminal TMS in MscS family homologues serves as the channel-forming helix in a homooligomeric structure. The presence of a conserved residue pattern for the putative channel-forming TMSs in the MscL and MscS family proteins suggests a common structural organization, gating mechanism, and evolutionary origin.

Indexed as

Mechanotransduction, CellularPhylogenyAmino Acid SequenceConserved SequenceEscherichia coli ProteinsIon ChannelsModels, MolecularMolecular Sequence DataMultigene FamilyEscherichia coli ProteinsIon ChannelsMscL protein, E coliMscS protein, E coli

Identifiers

PMID12626684
PMCPMC150521
OpenAlexW1974141650

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.