Evidence map›Paper›PMID 24747941›Full record

ArticleNature structural & molecular biology2014

Conformational changes required for H(+)/Cl(-) exchange mediated by a CLC transporter.

Daniel Basilio, Kristin Noack, Alessandra Picollo, Alessio Accardi

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

46 citing papers in PubMed, 78 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Structural basis of pH-dependent activation in a CLC transporter.Nature structural & molecular biology · 2024
    Article
  5. Fluoride Transport and Inhibition Across CLC Transporters.Handbook of experimental pharmacology · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Q-cubed mutant cues clues to CLC antiport mechanism.The Journal of general physiology · 2021
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Divergent CleLife · 2020
    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

4 authors at 1 institution in 1 country.

Daniel BasilioDepartment of Anesthesiology, Weill Cornell Medical College, New York, New York, USA.
Kristin NoackDepartment of Anesthesiology, Weill Cornell Medical College, New York, New York, USA.
Alessandra PicolloDepartment of Anesthesiology, Weill Cornell Medical College, New York, New York, USA.
Alessio Accardi1] Department of Anesthesiology, Weill Cornell Medical College, New York, New York, USA. [2] Department of Physiology and Biophysics, Weill Cornell Medical College, New York, New York, USA. [3] Department of Biochemistry, Weill Cornell Medical College, New York, New York, USA.
Cornell University · US

Funding

Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
Structure and function of chloride channels and transportersR01GM085232 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI ACCARDI, ALESSIO · 2009 to 2013
$1.7M
NIGMS NIH HHS GM085232NIGMS NIH HHS P41 GM111244NIGMS NIH HHS R01 GM085232
6 · The paper itself

Abstract

CLC-type exchangers mediate transmembrane Cl(-) transport. Mutations altering their gating properties cause numerous genetic disorders. However, their transport mechanism remains poorly understood. In conventional models, two gates alternatively expose substrates to the intra- or extracellular solutions. A glutamate was identified as the only gate in the CLCs, suggesting that CLCs function by a nonconventional mechanism. Here we show that transport in CLC-ec1, a prokaryotic homolog, is inhibited by cross-links constraining movement of helix O far from the transport pathway. Cross-linked CLC-ec1 adopts a wild-type-like structure, indicating stabilization of a native conformation. Movements of helix O are transduced to the ion pathway via a direct contact between its C terminus and a tyrosine that is a constitutive element of the second gate of CLC transporters. Therefore, the CLC exchangers have two gates that are coupled through conformational rearrangements outside the ion pathway.

Indexed as

Biological TransportChloride ChannelsCrystallography, X-RayEscherichia coli K12Escherichia coli ProteinsModels, MolecularMutationProtein Structure, TertiaryChloride ChannelsEscherichia coli Proteins

Identifiers

PMID24747941
PMCPMC4040230
OpenAlexW1982831381

What OpenQuestion holds

Textmetadata
LicenceTDM
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.