Evidence map›Paper›PMID 25849048›Full record

ArticlePloS one2015

Quantitative profiling of brain lipid raft proteome in a mouse model of fragile X syndrome.

Magdalena Kalinowska, Catherine Castillo, Anna Francesconi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

13 citing papers in PubMed, 25 citations in OpenAlex.

  1. A New GlyT2 Variant Associated with Hyperekplexia.International journal of molecular sciences · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Of Men and Mice: Modeling the Fragile X Syndrome.Frontiers in molecular neuroscience · 2018
    Article
  11. The role of cholesterol metabolism and various steroid abnormalities in autism spectrum disorders: A hypothesis paper.Autism research : official journal of the International Society for Autism Research · 2017
    Review
  12. Article
  13. Glial Contributions to Neural Function and Disease.Molecular & cellular proteomics : MCP · 2016
    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

3 authors at 1 institution in 1 country.

Magdalena KalinowskaDominick P. Purpura Department of Neuroscience, Albert Einstein College of Medicine, Bronx, New York, New York, United States of America.
Catherine CastilloDominick P. Purpura Department of Neuroscience, Albert Einstein College of Medicine, Bronx, New York, New York, United States of America.
Anna FrancesconiDominick P. Purpura Department of Neuroscience, Albert Einstein College of Medicine, Bronx, New York, New York, United States of America.
Albert Einstein College of Medicine · US

Funding

Regulation of Metabotropic glutamate Receptor Signaling by Caveolar RaftsR01MH082870 · NIMH · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI FRANCESCONI, ANNA · 2009 to 2013
$2.0M
NIMH NIH HHS MH082870NIMH NIH HHS R01 MH082870
6 · The paper itself

Abstract

Fragile X Syndrome, a leading cause of inherited intellectual disability and autism, arises from transcriptional silencing of the FMR1 gene encoding an RNA-binding protein, Fragile X Mental Retardation Protein (FMRP). FMRP can regulate the expression of approximately 4% of brain transcripts through its role in regulation of mRNA transport, stability and translation, thus providing a molecular rationale for its potential pleiotropic effects on neuronal and brain circuitry function. Several intracellular signaling pathways are dysregulated in the absence of FMRP suggesting that cellular deficits may be broad and could result in homeostatic changes. Lipid rafts are specialized regions of the plasma membrane, enriched in cholesterol and glycosphingolipids, involved in regulation of intracellular signaling. Among transcripts targeted by FMRP, a subset encodes proteins involved in lipid biosynthesis and homeostasis, dysregulation of which could affect the integrity and function of lipid rafts. Using a quantitative mass spectrometry-based approach we analyzed the lipid raft proteome of Fmr1 knockout mice, an animal model of Fragile X syndrome, and identified candidate proteins that are differentially represented in Fmr1 knockout mice lipid rafts. Furthermore, network analysis of these candidate proteins reveals connectivity between them and predicts functional connectivity with genes encoding components of myelin sheath, axonal processes and growth cones. Our findings provide insight to aid identification of molecular and cellular dysfunctions arising from Fmr1 silencing and for uncovering shared pathologies between Fragile X syndrome and other autism spectrum disorders.

Indexed as

AnimalsBrainDisease Models, AnimalFragile X Messenger Ribonucleoprotein 1Fragile X SyndromeHumansMembrane MicrodomainsMembrane ProteinsMiceMice, KnockoutProteomeFmr1 protein, mouseFragile X Messenger Ribonucleoprotein 1Membrane ProteinsProteome

Identifiers

PMID25849048
PMCPMC4388542
OpenAlexW2000186718

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.