Evidence map›Paper›PMID 16167151›Full record

ReviewPflugers Archiv : European journal of physiology2006

Role of intramolecular and intermolecular interactions in ClC channel and transporter function.

Sonja U Dhani, Christine E Bear

Abstract readReview
PubMed Publisher
In one paragraph

Review in Pflugers Archiv : European journal of physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 41% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. The mechanism of fast-gate opening in ClC-0.The Journal of general physiology · 2007
    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

2 authors at 2 institutions in 2 countries.

Sonja U DhaniProgramme in Structural Biology and Biochemistry, Research Institute, Hospital for Sick Children, 555 University Avenue, Toronto, Ontario, Canada.
Christine E Bear
SickKids Foundation · CAUniversity College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ClC family of chloride channels and transporters includes several members in which mutations have been associated with human disease. Clearly, an understanding of the structure-function relationships of these proteins will be critical in defining the molecular mechanisms underlying disease pathogenesis. The X-ray crystal structure of prokaryotic ClC proteins provides an exquisite template with which to model molecular aspects of eukaryotic ClC protein function. The dimeric structure of these proteins highlights the pivotal importance of intermolecular interactions in the modulation of channel/transporter activity, while mutagenesis studies implicate a crucial role for intrinsic interdomain interactions in regulated function. In this review, we will initially focus on the channel forming members of this family and discuss interactions within homodimeric channel complexes important for gating. Finally, with regard to both channel and transporter family members, we will discuss the multiple heteromeric interactions which occur with cytosolic proteins, and the putative functional impact of these interactions.

Indexed as

Chloride ChannelsGene Expression RegulationHumansModels, MolecularMutationProtein ConformationChloride Channels

Identifiers

PMID16167151
OpenAlexW2007584006

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.