Evidence map›Paper›PMID 35546407›Full record

ArticleBMC veterinary research2022

A novel amino acid site of N protein could affect the PRRSV-2 replication by regulating the viral RNA transcription.

Hua Deng, Ning Xin, Fancong Zeng, Feng Wen, Heyou Yi, Chunquan Ma, Shujian Huang, Guihong Zhang, Yao Chen

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC veterinary research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.0field-weighted citation impact, top 30% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
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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

9 authors at 2 institutions in 1 country.

Hua Deng *School of Life Science and Engineering, Foshan University, Foshan, 528000, People's Republic of China.
Ning Xin *School of Life Science and Engineering, Foshan University, Foshan, 528000, People's Republic of China.
Fancong Zeng *School of Life Science and Engineering, Foshan University, Foshan, 528000, People's Republic of China.
Feng WenSchool of Life Science and Engineering, Foshan University, Foshan, 528000, People's Republic of China.
Heyou YiMOA Key Laboratory of Animal Vaccine Development, Ministry of Agriculture, College of Veterinary Medicine, South China Agricultural University, Guangzhou, 510642, People's Republic of China.
Chunquan MaSchool of Life Science and Engineering, Foshan University, Foshan, 528000, People's Republic of China.
Shujian HuangSchool of Life Science and Engineering, Foshan University, Foshan, 528000, People's Republic of China.
Guihong ZhangMOA Key Laboratory of Animal Vaccine Development, Ministry of Agriculture, College of Veterinary Medicine, South China Agricultural University, Guangzhou, 510642, People's Republic of China. guihongzh@scau.edu.cn.
Yao ChenSchool of Life Science and Engineering, Foshan University, Foshan, 528000, People's Republic of China. yaochenvet@fosu.edu.cn.
Foshan University · CNSouth China Agricultural University · CN

Funding

GuangDong Basic and Applied Basic Research Foundation No.2019A1515110056National Natural Science Foundation of China No. 31872489
6 · The paper itself

Abstract

backgroundFinding the key amino acid sites that could affect viral biological properties or protein functions has always been a topic of substantial interest in virology. The nucleocapsid (N) protein is one of the principal proteins of the porcine reproductive and respiratory syndrome virus (PRRSV) and plays a vital role in the virus life cycle. The N protein has only 123 or 128 amino acids, some of key amino acid sites which could affect the protein functions or impair the viral biological characteristics have been identified. In this research, our objective was to find out whether there are other novel amino acid sites of the N protein can affect N protein functions or PRRSV-2 replication.

resultsIn this study, we found mutated the serine

conclusionsOur results suggest that the serine

Indexed as

Porcine Reproductive and Respiratory SyndromePorcine respiratory and reproductive syndrome virusSwine DiseasesAmino AcidsAnimalsCell LineNucleocapsid ProteinsRNA, ViralSerineSwineVirus ReplicationAmino AcidsNucleocapsid ProteinsRNA, ViralSerineIL-10Nucleocapsid proteinPorcine reproductive and respiratory syndrome virus (PRRSV)Replication ability

Identifiers

PMID35546407
PMCPMC9092334
OpenAlexW4280523615

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.