Evidence map›Paper›PMID 16469788›Full record

ArticleThe Journal of physiology2006

Removal of gating in voltage-dependent ClC-2 chloride channel by point mutations affecting the pore and C-terminus CBS-2 domain.

Yamil R Yusef, Leandro Zúñiga, Marcelo Catalán, María Isabel Niemeyer, L Pablo Cid, Francisco V Sepúlveda

Abstract read
In one paragraph

Article in The Journal of physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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

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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

20 citing papers in PubMed.

  1. Identification of a novelFrontiers in genetics · 2026
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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.

Yamil R YusefCentro de Estudios Cientificos (CECS), Av. Arturo Prat 514, Valdivia, Chile.
Leandro Zúñiga
Marcelo Catalán
María Isabel Niemeyer
L Pablo Cid
Francisco V Sepúlveda

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Functional and structural studies demonstrate that Cl(-) channels of the ClC family have a dimeric double-barrelled structure, with each monomer contributing an identical pore. Studies with ClC-0, the prototype ClC channel, show the presence of independent mechanisms gating the individual pores or both pores simultaneously. A single-point mutation in the CBS-2 domain of ClC-0 has been shown to abolish slow gating. We have taken advantage of the high conservation of CBS domains in ClC channels to test for the presence of a slow gate in ClC-2 by reproducing this mutation (H811A). ClC-2-H811A showed faster opening kinetics and opened at more positive potentials than ClC-2. There was no difference in [Cl(-)](i) dependence. Additional neutralization of a putative pore gate glutamate side chain (E207V) abolished all gating. Resolving slow and fast gating relaxations, however, revealed that the H811A mutation affected both fast and slow gating processes in ClC-2. This suggests that slow and fast gating in ClC-2 are coupled, perhaps with slow gating contributing to the operation of the pore E207 as a protopore gate.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionCell LineChloride ChannelsCLC-2 Chloride ChannelsHumansIon Channel GatingKidneyKineticsMembrane PotentialsMolecular Sequence DataMutagenesis, Site-DirectedMutationPorosityProtein Structure, TertiaryStructure-Activity RelationshipChloride ChannelsCLC-2 Chloride Channels

Identifiers

PMID16469788
PMCPMC1779660

What OpenQuestion holds

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Registered trials

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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.