Evidence map›Paper›PMID 35774459›Full record

ArticleFrontiers in microbiology2022

Structural Design and Assessing of Recombinantly Expressed African Swine Fever Virus p72 Trimer in

Kaiwen Meng, Yueping Zhang, Qi Liu, Yangnan Huyan, Wenzhuang Zhu, Ye Xiang, Geng Meng

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

6 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. 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

7 authors at 2 institutions in 1 country.

Kaiwen MengCollege of Veterinary Medicine, China Agricultural University, Beijing, China.
Yueping ZhangCollege of Veterinary Medicine, China Agricultural University, Beijing, China.
Qi LiuSchool of Medicine, Tsinghua University, Beijing, China.
Yangnan HuyanCollege of Veterinary Medicine, China Agricultural University, Beijing, China.
Wenzhuang ZhuCollege of Veterinary Medicine, China Agricultural University, Beijing, China.
Ye XiangSchool of Medicine, Tsinghua University, Beijing, China.
Geng MengCollege of Veterinary Medicine, China Agricultural University, Beijing, China.
China Agricultural University · CNTsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In an effort to control the outbreak of the African Swine Fever Virus (ASFV), there is an urgent need to develop an effective method to prevent the pandemic, including vaccines and diagnostic methods. The major capsid protein of ASFV p72 (B646L), which forms a trimer with each monomer adopting a double jelly roll fold, is the main component of the virus particle and major antigen of ASFV. Thus, the p72 protein may be considered an antigen candidate for vaccine and diagnostic development. However, the development of ASFV p72 trimer for the industry application, including veterinary usage, faces unavoidable challenges: firstly, the low cost of the antigen production is required in vaccine and diagnostic application; and, secondly, whether produced antigen folds in its native conformation. Here, based on the information provided by the atomic structure of p72, we have successfully performed rational mutagenesis on p72 trimers and expressed it in

Indexed as

African swine fever virusantigenmajor capsidp72 trimerprotein design

Identifiers

PMID35774459
PMCPMC9239254
OpenAlexW4282946578

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.