Evidence map›Paper›PMID 17846164›Full record

ArticleThe Journal of general physiology2007

The mechanism of fast-gate opening in ClC-0.

Anita M Engh, José D Faraldo-Gómez, Merritt Maduke

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Chloride Ion Transport by theFrontiers in chemistry · 2018
    Article
  4. Article
  5. Article
  6. ClC-1 and ClC-2 form hetero-dimeric channels with novel protopore functions.Pflugers Archiv : European journal of physiology · 2014
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Paul F. Cranefield Award to Merritt C. Maduke.The Journal of general physiology · 2010
    Article
  12. Proton block of the CLC-5 Cl-/H+ exchanger.The Journal of general physiology · 2010
    Article
  13. Article
  14. Article
  15. Intracellular proton regulation of ClC-0.The Journal of general physiology · 2008
    Article
  16. 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.

Anita M EnghDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.
José D Faraldo-Gómez
Merritt Maduke
Stanford University · USUniversity of Chicago · US

Funding

Mechanisms of CIC Chloride Transport ProteinsR01GM070773 · NIGMS · STANFORD UNIVERSITY · PI MADUKE, MERRITT C · 2005 to 2009
$1.5M
NIGMS NIH HHS R01 GM070773
6 · The paper itself

Abstract

ClC-0 is a chloride channel whose gating is sensitive to both voltage and chloride. Based on analysis of gating kinetics using single-channel recordings, a five-state model was proposed to describe the dependence of ClC-0 fast-gate opening on voltage and external chloride (Chen, T.-Y., and C. Miller. 1996. J. Gen. Physiol. 108:237-250). We aimed to use this five-state model as a starting point for understanding the structural changes that occur during gating. Using macroscopic patch recordings, we were able to reproduce the effects of voltage and chloride that were reported by Chen and Miller and to fit our opening rate constant data to the five-state model. Upon further analysis of both our data and those of Chen and Miller, we learned that in contrast to their conclusions, (a) the features in the data are not adequate to rule out a simpler four-state model, and (b) the chloride-binding step is voltage dependent. In order to be able to evaluate the effects of mutants on gating (described in the companion paper, see Engh et al. on p. 351 of this issue), we developed a method for determining the error on gating model parameters, and evaluated the sources of this error. To begin to mesh the kinetic model(s) with the known CLC structures, a model of ClC-0 was generated computationally based on the X-ray crystal structure of the prokaryotic homolog ClC-ec1. Analysis of pore electrostatics in this homology model suggests that at least two of the conclusions derived from the gating kinetics analysis are consistent with the known CLC structures: (1) chloride binding is necessary for channel opening, and (2) chloride binding to any of the three known chloride-binding sites must be voltage dependent.

Indexed as

Chloride ChannelsIon Channel GatingModels, BiologicalAmino Acid SubstitutionAnimalsBinding SitesChloridesFactor Analysis, StatisticalKineticsMembrane PotentialsPatch-Clamp TechniquesRegression AnalysisStatic ElectricityStructure-Activity RelationshipTorpedoChloride ChannelsChloridesCLC-0 chloride channel protein, Torpedo californica

Identifiers

PMID17846164
PMCPMC2151655
OpenAlexW2167748126

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.