Evidence map›Paper›PMID 19745816›Full record

ArticleThe EMBO journal2009

Substrate-driven conformational changes in ClC-ec1 observed by fluorine NMR.

Shelley M Elvington, Corey W Liu, Merritt C Maduke

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

34 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
  2. Article
  3. International journal of molecular sciences · 2024
    Article
  4. Structural basis of pH-dependent activation in a CLC transporter.Nature structural & molecular biology · 2024
    Article
  5. Article
  6. Article
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  13. Article
  14. Multiscale Kinetic Modeling Reveals an Ensemble of ClJournal of the American Chemical Society · 2018
    Article
  15. Chloride Ion Transport by theFrontiers in chemistry · 2018
    Article
  16. Article
  17. The Origin of Coupled Chloride and Proton Transport in a ClJournal of the American Chemical Society · 2016
    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

3 authors at 2 institutions in 1 country.

Shelley M ElvingtonDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305-5345, USA.
Corey W Liu
Merritt C Maduke
Stanford University · USResonance Research (United States) · US

Funding

Mechanisms of CIC Chloride Transport ProteinsR01GM070773 · NIGMS · STANFORD UNIVERSITY · PI MADUKE, MERRITT C · 2005 to 2009
$1.5M
Probing conformational changes in CLC chloride transport proteins using 19F NMRF32GM080840 · NIGMS · STANFORD UNIVERSITY · PI ELVINGTON, SHELLEY M · 2008 to 2009
$101k
NIGMS NIH HHS F32 GM080840NIGMS NIH HHS R01 GM070773
6 · The paper itself

Abstract

The CLC 'Cl(-) channel' family consists of both Cl(-)/H(+) antiporters and Cl(-) channels. Although CLC channels can undergo large, conformational changes involving cooperativity between the two protein subunits, it has been hypothesized that conformational changes in the antiporters may be limited to small movements localized near the Cl(-) permeation pathway. However, to date few studies have directly addressed this issue, and therefore little is known about the molecular movements that underlie CLC-mediated antiport. The crystal structure of the Escherichia coli antiporter ClC-ec1 provides an invaluable molecular framework, but this static picture alone cannot depict the protein movements that must occur during ion transport. In this study we use fluorine nuclear magnetic resonance (NMR) to monitor substrate-induced conformational changes in ClC-ec1. Using mutational analysis, we show that substrate-dependent (19)F spectral changes reflect functionally relevant protein movement occurring at the ClC-ec1 dimer interface. Our results show that conformational change in CLC antiporters is not restricted to the Cl(-) permeation pathway and show the usefulness of (19)F NMR for studying conformational changes in membrane proteins of known structure.

Indexed as

Models, MolecularAntiportersChloride ChannelsEscherichia coli ProteinsMagnetic Resonance SpectroscopyProtein Structure, SecondaryAntiportersChloride ChannelsClC protein, E coliEscherichia coli Proteinshydrogen-chloride symporter

Identifiers

PMID19745816
PMCPMC2771095
OpenAlexW2133281929

What OpenQuestion holds

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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.