Evidence map›Paper›PMID 23082193›Full record

ArticlePloS one2012

Restoration of proper trafficking to the cell surface for membrane proteins harboring cysteine mutations.

Angelica Lopez-Rodriguez, Miguel Holmgren

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. 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 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, 7 citations in OpenAlex.

  1. Neurology. Genetics · 2024
    Article
  2. Article
  3. 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 2 institutions in 1 country.

Angelica Lopez-RodriguezNeurophysiology Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke (NINDS), National Institutes of Health (NIH), Bethesda, Maryland, USA.
Miguel Holmgren
National Institute of Neurological Disorders and Stroke · USNational 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
Intramural NIH HHS
6 · The paper itself

Abstract

A common phenotype for many genetic diseases is that the cell is unable to deliver full-length membrane proteins to the cell surface. For some forms of autism, hereditary spherocytosis and color blindness, the culprits are single point mutations to cysteine. We have studied two inheritable cysteine mutants of cyclic nucleotide-gated channels that produce achromatopsia, a common form of severe color blindness. By taking advantage of the reactivity of cysteine's sulfhydryl group, we modified these mutants with chemical reagents that attach moieties with similar chemistries to the wild-type amino acids' side chains. We show that these modifications restored proper delivery to the cell membrane. Once there, the channels exhibited normal functional properties. This strategy might provide a unique opportunity to assess the chemical nature of membrane protein traffic problems.

Indexed as

Amino Acid SubstitutionAnimalsCattleCell MembraneCyclic Nucleotide-Gated Cation ChannelsCysteineEthyl MethanesulfonateGreen Fluorescent ProteinsHumansMembrane ProteinsMutant ProteinsMutationRecombinant Fusion ProteinsTime FactorsXenopusCyclic Nucleotide-Gated Cation ChannelsCysteineEthyl MethanesulfonateGreen Fluorescent ProteinsMembrane Proteinsmethanethiosulfonate ethylammoniumMutant ProteinsRecombinant Fusion Proteins

Identifiers

PMID23082193
PMCPMC3474720
OpenAlexW2029954732

What OpenQuestion holds

Textmetadata
LicenceCC0
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.