Evidence map›Paper›PMID 27357083›Full record

ArticleMolecular medicine reports2016

CMP‑N‑acetylneuraminic acid synthetase interacts with fragile X related protein 1.

Yun Ma, Shuai Tian, Zongbao Wang, Changbo Wang, Xiaowei Chen, Wei Li, Yang Yang, Shuya He

Open access · hybridAbstract read
In one paragraph

Article in Molecular medicine reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 19% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Modeling Fragile X Syndrome inFrontiers in molecular neuroscience · 2018
    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

8 authors at 1 institution in 1 country.

Yun MaDepartment of Biochemistry & Biology, University of South China, Hengyang, Hunan 421001, P.R. China.
Shuai TianDepartment of Biochemistry & Biology, University of South China, Hengyang, Hunan 421001, P.R. China.
Zongbao WangHunan Province Cooperative Innovation Center for Molecular Target New Drug Study, Institute of Pharmaceutical and Biological Sciences, University of South China, Hengyang, Hunan 421001, P.R. China.
Changbo WangDepartment of Biochemistry & Biology, University of South China, Hengyang, Hunan 421001, P.R. China.
Xiaowei ChenDepartment of Biochemistry & Biology, University of South China, Hengyang, Hunan 421001, P.R. China.
Wei LiDepartment of Biochemistry & Biology, University of South China, Hengyang, Hunan 421001, P.R. China.
Yang YangDepartment of Biochemistry & Biology, University of South China, Hengyang, Hunan 421001, P.R. China.
Shuya HeDepartment of Biochemistry & Biology, University of South China, Hengyang, Hunan 421001, P.R. China.
University of South China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fragile X mental retardation protein (FMRP), fragile X related 1 protein (FXR1P) and FXR2P are the members of the FMR protein family. These proteins contain two KH domains and a RGG box, which are characteristic of RNA binding proteins. The absence of FMRP, causes fragile X syndrome (FXS), the leading cause of hereditary mental retardation. FXR1P is expressed throughout the body and important for normal muscle development, and its absence causes cardiac abnormality. To investigate the functions of FXR1P, a screen was performed to identify FXR1P‑interacting proteins and determine the biological effect of the interaction. The current study identified CMP‑N‑acetylneuraminic acid synthetase (CMAS) as an interacting protein using the yeast two‑hybrid system, and the interaction between FXR1P and CMAS was validated in yeast using a β‑galactosidase assay and growth studies with selective media. Furthermore, co‑immunoprecipitation was used to analyze the FXR1P/CMAS association and immunofluorescence microscopy was performed to detect expression and intracellular localization of the proteins. The results of the current study indicated that FXR1P and CMAS interact, and colocalize in the cytoplasm and the nucleus of HEK293T and HeLa cells. Accordingly, a fragile X related 1 (FXR1) gene overexpression vector was constructed to investigate the effect of FXR1 overexpression on the level of monosialotetrahexosylganglioside 1 (GM1). The results of the current study suggested that FXR1P is a tissue‑specific regulator of GM1 levels in SH‑SY5Y cells, but not in HEK293T cells. Taken together, the results initially indicate that FXR1P interacts with CMAS, and that FXR1P may enhance the activation of sialic acid via interaction with CMAS, and increase GM1 levels to affect the development of the nervous system, thus providing evidence for further research into the pathogenesis of FXS.

Indexed as

Fragile X Messenger Ribonucleoprotein 1Fragile X SyndromeGene ExpressionHEK293 CellsHeLa CellsHumansImmunoprecipitationN-Acylneuraminate CytidylyltransferaseOligosaccharidesProtein BindingProtein Interaction Domains and MotifsProtein Interaction MappingProtein TransportTwo-Hybrid System TechniquesFMR1 protein, humanFragile X Messenger Ribonucleoprotein 1GM1 pentasaccharideN-Acylneuraminate CytidylyltransferaseOligosaccharides

Identifiers

PMID27357083
PMCPMC4940058
OpenAlexW2462123914

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.