Evidence map›Paper›PMID 29880580›Full record

ArticleThe Journal of general physiology2018

Deglycosylation of Shaker K

Angelica Lopez-Rodriguez, Miguel Holmgren

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 53% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Potassium Channels, Glucose Metabolism and Glycosylation in Cancer Cells.International journal of molecular sciences · 2023
    Review
  2. 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 1 institution in 2 countries.

Angelica Lopez-RodriguezNeurophysiology Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD angelica.lopez@ujed.mx.ORCID 0000-0003-4411-8441
Miguel HolmgrenNeurophysiology Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD holmgren@ninds.nih.gov.ORCID 0000-0001-8285-4242
National Institutes of Health · US

Funding

Structure and Function of Membrane ProteinsZIANS002993 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI HOLMGREN, MIGUEL · 2009 to 2025
$24.0M
6 · The paper itself

Abstract

Most membrane proteins are subject to posttranslational glycosylation, which influences protein function, folding, solubility, stability, and trafficking. This modification has been proposed to protect proteins from proteolysis and modify protein-protein interactions. Voltage-activated ion channels are heavily glycosylated, which can result in up to 30% of the mature molecular mass being contributed by glycans. Normally, the functional consequences of glycosylation are assessed by comparing the function of fully glycosylated proteins with those in which glycosylation sites have been mutated or by expressing proteins in model cells lacking glycosylation enzymes. Here, we study the functional consequences of deglycosylation by PNGase F within the same population of voltage-activated potassium (K

Indexed as

Ion Channel GatingProtein Processing, Post-TranslationalAnimalsGlycosylationMembrane PotentialsMiceProtein DomainsShaker Superfamily of Potassium ChannelsXenopusShaker Superfamily of Potassium Channels

Identifiers

PMID29880580
PMCPMC6028503
OpenAlexW2806356686

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.