Evidence map›Paper›PMID 26528969›Full record

ArticleInternational journal of molecular sciences2015

Proteomics Analysis of Cellular Proteins Co-Immunoprecipitated with Nucleoprotein of Influenza A Virus (H7N9).

Ningning Sun, Wanchun Sun, Shuiming Li, Jingbo Yang, Longfei Yang, Guihua Quan, Xiang Gao, Zijian Wang, Xin Cheng, Zehui Li and 2 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 39 citations in OpenAlex.

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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

12 authors at 3 institutions in 1 country.

Ningning SunCentral Laboratory, Jilin University Second Hospital, Changchun 130041, China. sunnn13@mails.jlu.edu.cn.
Wanchun SunKey Laboratory of Zoonosis Research, Ministry of Education, Institute of Zoonosis, Jilin University, Changchun 130062, China. Wanchunsun@jlu.edu.cn.
Shuiming LiCollege of Life Sciences, Shenzhen University, Shenzhen 518057, China. shuimingli@szu.edu.cn.
Jingbo YangCentral Laboratory, Jilin University Second Hospital, Changchun 130041, China. yang.jb@live.cn.
Longfei YangCentral Laboratory, Jilin University Second Hospital, Changchun 130041, China. yanglongfei@jlu.edu.cn.
Guihua QuanCentral Laboratory, Jilin University Second Hospital, Changchun 130041, China. qgh0521@jlu.edu.cn.
Xiang GaoCentral Laboratory, Jilin University Second Hospital, Changchun 130041, China. gaoxiang13@mails.jlu.edu.cn.
Zijian WangCentral Laboratory, Jilin University Second Hospital, Changchun 130041, China. jiuwzj1989@sina.com.
Xin ChengCentral Laboratory, Jilin University Second Hospital, Changchun 130041, China. chengxin14@mails.jlu.edu.cn.
Zehui LiCentral Laboratory, Jilin University Second Hospital, Changchun 130041, China. lizh7013@mails.jlu.edu.cn.
Qisheng PengKey Laboratory of Zoonosis Research, Ministry of Education, Institute of Zoonosis, Jilin University, Changchun 130062, China. pengqs@jlu.edu.cn.
Ning LiuCentral Laboratory, Jilin University Second Hospital, Changchun 130041, China. liu_ning@jlu.edu.cn.
Second Affiliated Hospital of Jilin University · CNJilin University · CNShenzhen University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Avian influenza A viruses are serious veterinary pathogens that normally circulate among avian populations, causing substantial economic impacts. Some strains of avian influenza A viruses, such as H5N1, H9N2, and recently reported H7N9, have been occasionally found to adapt to humans from other species. In order to replicate efficiently in the new host, influenza viruses have to interact with a variety of host factors. In the present study, H7N9 nucleoprotein was transfected into human HEK293T cells, followed by immunoprecipitated and analyzed by proteomics approaches. A series of host proteins co-immunoprecipitated were identified with high confidence, some of which were found to be acetylated at their lysine residues. Bioinformatics analysis revealed that spliceosome might be the most relevant pathway involved in host response to nucleoprotein expression, increasing our emerging knowledge of host proteins that might be involved in influenza virus replication activities.

Indexed as

AcetylationCarrier ProteinsComputational BiologyGene ExpressionHEK293 CellsHumansImmunoprecipitationInfluenza A Virus, H7N9 SubtypeInfluenza, HumanLysineNucleocapsid ProteinsProtein BindingProtein Interaction MappingProtein Interaction MapsRNA-Binding ProteinsTandem Mass SpectrometryCarrier ProteinsLysineNP protein, Influenza A virusNucleocapsid ProteinsRNA-Binding ProteinsViral Core Proteinsco-immunoprecipitationinfluenza A viruslysine acetylationmass spectrometrynucleoprotein

Identifiers

PMID26528969
PMCPMC4661793
OpenAlexW2124951831

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.