Evidence map›Paper›PMID 30926318›Full record

ReviewChemico-biological interactions2019

Biochemical and physiological properties of K

Sean M Raph, Aruni Bhatnagar, Matthew A Nystoriak

Open access · greenAbstract readReview
In one paragraph

Review in Chemico-biological interactions, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed, 1 pooled it
0.5field-weighted citation impact, top 33% 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

9 citing papers in PubMed, 1 synthesis or guideline pooled it, 13 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. HInternational journal of molecular sciences · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Insights into3 Biotech · 2023
    Article
  9. 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 1 institution in 1 country.

Sean M RaphDepartment of Pharmacology and Toxicology, University of Louisville, Louisville, KY, 40202, USA.
Aruni BhatnagarDepartment of Medicine, Diabetes and Obesity Center, University of Louisville, Louisville, KY, 40202, USA.
Matthew A NystoriakDepartment of Medicine, Diabetes and Obesity Center, University of Louisville, Louisville, KY, 40202, USA. Electronic address: matthew.nystoriak@louisville.edu.
University of Louisville · US

Funding

Regulation of Coronary Blood FlowR01HL142710 · NHLBI · UNIVERSITY OF LOUISVILLE · PI NYSTORIAK, MATTHEW A · 2018 to 2022
$3.1M
NHLBI NIH HHS R01 HL142710
6 · The paper itself

Abstract

Voltage-gated potassium (Kv) channels play an essential role in the regulation of membrane excitability and thereby control physiological processes such as cardiac excitability, neural communication, muscle contraction, and hormone secretion. Members of the Kv1 and Kv4 families are known to associate with auxiliary intracellular Kvβ subunits, which belong to the aldo-keto reductase superfamily. Electrophysiological studies have shown that these proteins regulate the gating properties of Kv channels. Although the three gene products encoding Kvβ proteins are functional enzymes in that they catalyze the nicotinamide adenine dinucleotide phosphate (NAD[P]H)-dependent reduction of a wide range of aldehyde and ketone substrates, the physiological role for these proteins and how each subtype may perform unique roles in coupling membrane excitability with cellular metabolic processes remains unclear. Here, we discuss current knowledge of the enzymatic properties of Kvβ proteins from biochemical studies with their described and purported physiological and pathophysiological influences.

Indexed as

AldehydesAnimalsHumansImmune SystemKetonesKineticsMyocardiumNADPNervous SystemPotassium Channels, Voltage-GatedAldehydesKetonesNADPPotassium Channels, Voltage-GatedAldehyde metabolismAldo-keto reductaseCarbonyl metabolismKv channelsMembrane potential

Identifiers

PMID30926318
PMCPMC6584034
OpenAlexW2924466907

What OpenQuestion holds

Textmetadata
LicenceTDM
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.