Evidence map›Paper›PMID 19464371›Full record

ArticleNeurobiology of disease2009

Ultrastructural analysis of the functional domains in FMRP using primary hippocampal mouse neurons.

Josien Levenga, Ronald A M Buijsen, Maria Rifé, Hervé Moine, David L Nelson, Ben A Oostra, Rob Willemsen, Femke M S de Vrij

Open access · greenAbstract read
In one paragraph

Article in Neurobiology of disease, 2009. 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
3.1field-weighted citation impact, top 8% 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, 28 citations in OpenAlex.

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  13. Fragile X protein FMRP is required for homeostatic plasticity and regulation of synaptic strength by retinoic acid.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010
    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

8 authors at 4 institutions in 3 countries.

Josien LevengaCBG Department of Clinical Genetics, Erasmus MC, Dr. Molewaterplein 50, 3015 GE, P.O. Box 2040, Rotterdam 3000 CA, The Netherlands.
Ronald A M Buijsen
Maria Rifé
Hervé Moine
David L Nelson
Ben A Oostra
Rob Willemsen
Femke M S de Vrij
Erasmus University Rotterdam · NLErasmus MC · NLBaylor College of Medicine · USInstitut de génétique et de biologie moléculaire et cellulaire · FR

Funding

Fragile X Related Genes Mental Retardiation/DevelopmentR01HD038038 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI NELSON, DAVID LOREN · 1999 to 2009
$3.1M
NICHD NIH HHS R01 HD038038NICHD NIH HHS R01 HD38038
6 · The paper itself

Abstract

Fragile X syndrome is caused by lack of the protein FMRP. FMRP mediates mRNA binding, dendritic mRNA transport and translational control at spines. We examined the role of functional domains of FMRP in neuronal RNA-granule formation and dendritic transport using different FMRP variants, including the mutant FMRP_I304N and the splice-variant FMRP_Iso12. Both variants are absent from dendritic RNA-granules in Fmr1 knockout neurons. Co-transfection experiments showed that wild-type FMRP recruits both FMRP variants into dendritic RNA-granules. Co-transfection of FXR2, an FMRP homologue, also resulted in redistribution of both variants into dendritic RNA-granules. Furthermore, the capacity of the variants to transport their mRNAs and the mRNA localization of an FMR1 construct containing silent point-mutations affecting only the G-quartet-structure were investigated. In conclusion, we show that wild-type FMRP and FXR2P are able to recruit FMRP variants into RNA-granules and that the G-quartet-structure in FMR1 mRNA is not essential for its incorporation in RNA-granules.

Indexed as

RNA TransportAnimalsCells, CulturedDendritesFragile X Messenger Ribonucleoprotein 1HippocampusImmunohistochemistryIn Situ HybridizationMiceMice, KnockoutMicroscopy, ConfocalMutationNeuronsNucleic Acid ConformationProtein IsoformsProtein Structure, TertiaryFmr1 protein, mouseFragile X Messenger Ribonucleoprotein 1FXR2 protein, mouseProtein IsoformsRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID19464371
PMCPMC2757577
OpenAlexW2080787823

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.