Evidence map›Paper›PMID 29978050›Full record

ArticleJournal of veterinary research2017

Exploration of the Main Sites for the Transformation of Normal Prion Protein (PrP

Xi-Lin Liu, Xiao-Li Feng, Guang-Ming Wang, Bin-Bin Gong, Waqas Ahmad, Nan-Nan Liu, Yuan-Yuan Zhang, Li Yang, Hong-Lin Ren, Shu-Sen Cui

Open access · goldAbstract read
In one paragraph

Article in Journal of veterinary research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact, top 97% 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

2 citing papers in PubMed, 1 citations in OpenAlex.

  1. Review
  2. 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

10 authors at 2 institutions in 2 countries.

Xi-Lin LiuChina-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China.
Xiao-Li FengChina-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China.
Guang-Ming WangChina-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China.
Bin-Bin GongChina-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China.
Waqas AhmadChina-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China.
Nan-Nan LiuChina-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China.
Yuan-Yuan ZhangChina-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China.
Li YangChina-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China.
Hong-Lin RenChina-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China.
Shu-Sen CuiChina-Japan Union Hospital of Jilin University, Key Laboratory of Zoonosis Research, Ministry of Education/Institute of Zoonosis, Jilin University, Changchun 130062, China.
Jilin University · CNKunming Institute of Zoology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

introductionThe functions and mechanisms of prion proteins (PrP MATERIAL AND

methodsBALB/c mice were challenged with prion RML strain and from 90 days post-challenge (dpc) mice were sacrificed weekly until all of them had been at 160 dpc. The ultra-structure and pathological changes of the brain of experimental mice were observed and recorded by transmission electron microscopy.

resultsThere were a large number of pathogen-like particles aggregated in the myelin sheath of the brain nerves, followed by delamination, hyperplasia, swelling, disintegration, phagocytic vacuolation, and other pathological lesions in the myelin sheath. The aggregated particles did not overflow from the myelin in unstained samples. The phenomenon of particle aggregation persisted all through the disease course, and was the earliest observed pathological change.

conclusionIt was deduced that the myelin sheath and lipid rafts in brain nerves, including axons and dendrites, were the main sites for the conversion of PrP

Indexed as

brainmicemyelin sheathparticle aggregationprion proteins

Identifiers

PMID29978050
PMCPMC5894410
OpenAlexW2605020139

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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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.