Evidence map›Paper›PMID 25748703›Full record

ReviewThe Korean journal of parasitology2015

Serine proteases of parasitic helminths.

Yong Yang, Yun jun Wen, Ya Nan Cai, Isabelle Vallée, Pascal Boireau, Ming Yuan Liu, Shi Peng Cheng

Open access · diamondAbstract readReview
In one paragraph

Review in The Korean journal of parasitology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed, 1 pooled it
8.1field-weighted citation impact, top 2% 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

69 citing papers in PubMed, 1 synthesis or guideline pooled it, 130 citations in OpenAlex.

  1. Pooled it
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  13. Early diagnosis ofVeterinary world · 2024
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9 more citing papers are in PubMed but not listed here.

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 5 institutions in 2 countries.

Yong YangState Key Laboratory for Molecular Biology of Special Economic Animals, Institute of Special Economic Animal and Plant Sciences, Chinese Academy of Agricultural Sciences, Changchun, China ; ANSES, ENVA, UPVM, PRES Paris Est, JRU BIPAR, Animal Health Laboratory, Maisons-Alfort, France.
Yun jun WenState Key Laboratory for Molecular Biology of Special Economic Animals, Institute of Special Economic Animal and Plant Sciences, Chinese Academy of Agricultural Sciences, Changchun, China.
Ya Nan CaiCollege of Animal Science and Technology, Jilin Agricultural University, Changchun, China.
Isabelle ValléeANSES, ENVA, UPVM, PRES Paris Est, JRU BIPAR, Animal Health Laboratory, Maisons-Alfort, France.
Pascal BoireauANSES, ENVA, UPVM, PRES Paris Est, JRU BIPAR, Animal Health Laboratory, Maisons-Alfort, France.
Ming Yuan LiuKey Laboratory of Zoonosis Research, Ministry of Education, Institute of Zoonosis, Jilin University, Changchun, China ; Jiangsu Co-innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou 225009, China.
Shi Peng ChengState Key Laboratory for Molecular Biology of Special Economic Animals, Institute of Special Economic Animal and Plant Sciences, Chinese Academy of Agricultural Sciences, Changchun, China.
Chinese Academy of Agricultural Sciences · CNAgence Nationale de Sécurité Sanitaire de l’Alimentation, de l’Environnement et du Travail · FRDépartement Santé Animale · FRJilin Agricultural University · CNJilin University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Serine proteases form one of the most important families of enzymes and perform significant functions in a broad range of biological processes, such as intra- and extracellular protein metabolism, digestion, blood coagulation, regulation of development, and fertilization. A number of serine proteases have been identified in parasitic helminths that have putative roles in parasite development and nutrition, host tissues and cell invasion, anticoagulation, and immune evasion. In this review, we described the serine proteases that have been identified in parasitic helminths, including nematodes (Trichinella spiralis, T. pseudospiralis, Trichuris muris, Anisakis simplex, Ascaris suum, Onchocerca volvulus, O. lienalis, Brugia malayi, Ancylostoma caninum, and Steinernema carpocapsae), cestodes (Spirometra mansoni, Echinococcus granulosus, and Schistocephalus solidus), and trematodes (Fasciola hepatica, F. gigantica, and Schistosoma mansoni). Moreover, the possible biological functions of these serine proteases in the endogenous biological phenomena of these parasites and in the host-parasite interaction were also discussed.

Indexed as

AnimalsCestodaHost-Parasite InteractionsLife Cycle StagesNematodaSerine ProteasesTrematodaSerine Proteasesbiological functioncestodenematodeparasitic helminthSerine proteasetrematode

Identifiers

PMID25748703
PMCPMC4384789
OpenAlexW2166598432

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.