Evidence map›Paper›PMID 1407274›Full record

ReviewNeurochemical research1992

Structure and regulation of the MinK potassium channel.

E M Blumenthal, L K Kaczmarek

Abstract readReview
PubMed Publisher
In one paragraph

Review in Neurochemical research, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

1 citing paper in PubMed, 14 citations in OpenAlex.

  1. Review
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 1 institution in 1 country.

E M BlumenthalInterdepartmental Neuroscience Program, Yale University Medical School, New Haven, CT 06510.
L K Kaczmarek
Yale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MinK is a novel protein which induces an extremely slowly activating potassium channel when expressed in Xenopus oocytes. We discuss the properties and regulation of the current and localization and possible physiological roles of the MinK protein.

Indexed as

Potassium Channels, Voltage-GatedAmino Acid SequenceAnimalsBiophysical PhenomenaBiophysicsGene Expression RegulationMembrane ProteinsMolecular Sequence DataPotassium ChannelsMembrane Proteinspotassium channel protein I(sk)Potassium ChannelsPotassium Channels, Voltage-Gated

Identifiers

PMID1407274
OpenAlexW2044579263

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.