Evidence map›Paper›PMID 23868316›Full record

ArticleNature chemical biology2013

Channels: Sticking to nooks and crannies.

Heike Wulff, Vladimir Yarov-Yarovoy

Abstract readNewsComment
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2013. 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
0.3field-weighted citation impact, top 38% 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, 3 citations in OpenAlex.

  1. Discovery of KMedicinal research reviews · 2021
    Review
  2. Article
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Heike Wulff
Vladimir Yarov-Yarovoy
University of California, Davis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Drug design for voltage-gated ion channels has long been hampered by the absence of crystal structures and the challenge of achieving subtype selectivity. A combination of mutagenesis, electrophysiology and molecular modeling has led to the identification of a new side pocket binding site for the small molecule Psora-4 between the pore and the voltage-sensor domain of Kv1.5, offering opportunities to design allosteric ion channel modulators.

Indexed as

Kv1.5 Potassium ChannelKv1.5 Potassium Channel

Identifiers

PMID23868316
OpenAlexW2020580765

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.