Evidence map›Paper›PMID 22015384›Full record

ArticleParasitology research2012

Identification and characterization of a novel 21.6-kDa tegumental protein from Clonorchis sinensis.

Yu-Jung Kim, Won Gi Yoo, Myoung-Ro Lee, Dae-Won Kim, Won-Ja Lee, Jung-Mi Kang, Byoung-Kuk Na, Jung-Won Ju

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Article in Parasitology research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

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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

12 citing papers in PubMed.

  1. Article
  2. Frontiers in cellular and infection microbiology · 2023
    Article
  3. Article
  4. Article
  5. Proteomics Analysis ofFrontiers in veterinary science · 2020
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
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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

8 authors.

Yu-Jung KimDivision of Malaria and Parasitic Diseases, Korea National Institute of Health, Osong, 363-951, Republic of Korea. hoiyui25@gmail.com
Won Gi Yoo
Myoung-Ro Lee
Dae-Won Kim
Won-Ja Lee
Jung-Mi Kang
Byoung-Kuk Na
Jung-Won Ju

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tegumental proteins form a membrane-bound outer surface and are thus involved in host-parasite interactions and parasite survival. A complementary DNA clone encoding a novel 21.6-kDa tegumental protein (CsTegu21.6, accession number JF911532) was identified in a sequence library for the adult Clonorchis sinensis liver fluke. The complete coding sequence was 564 bp and encoded a protein of 188 amino acids. A BLASTX search revealed identities from 43 to 47% with previously identified tegumental proteins in C. sinensis and other helminthic parasites. Multiple alignment of the amino acids of CsTegu21.6 with those of four other C. sinensis tegumental proteins, CsTegu21.1, CsTegu22.3, CsTegu20.8 and CsTegu31.8, revealed pair-wise sequence identities ranging from 24 to 31.8%. A calcium-binding EF-hand domain containing a basic helix-loop-helix structure at the N terminus and a dynein light chain domain at the C terminus were found in CsTegu21.6; these motifs are common in tegumental proteins. CsTegu21.6 was specifically observed on the tegument of adult worms using immunolocalization analysis.

Indexed as

Amino Acid MotifsAnimalsClonorchis sinensisDNA, ComplementaryHelminth ProteinsHumansMembrane ProteinsMicroscopy, FluorescenceMolecular Sequence DataMolecular WeightProtein ConformationProtein Structure, TertiarySequence AlignmentSequence Analysis, DNASequence Homology, Amino AcidDNA, ComplementaryHelminth ProteinsMembrane Proteins

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Registered trials

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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.