Evidence map›Paper›PMID 17252278›Full record

ArticleParasitology research2007

Molecular cloning and characterization of a cytosolic heat shock protein 70 from Naegleria fowleri.

Kyoung-Ju Song, Kyung-Hui Song, Byoung-Kuk Na, Jong-Hyun Kim, Daeho Kwon, Sun Park, Jhang-Ho Pak, Kyung-Il Im, Ho-Joon Shin

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Article in Parasitology research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

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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.

Kyoung-Ju SongDepartment of Microbiology, Ajou University School of Medicine, Suwon 443-721, South Korea.
Kyung-Hui Song
Byoung-Kuk Na
Jong-Hyun Kim
Daeho Kwon
Sun Park
Jhang-Ho Pak
Kyung-Il Im
Ho-Joon Shin

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A gene encoding a cytosolic heat shock protein 70 from pathogenic Naegleria fowleri (Nf-cHSP70) was identified. The Nf-cHSP70 was 2,062 bp in length with an open reading frame of 1,980 bp encoding 659 amino acid residues. The deduced amino acid sequence of the gene shared high sequence identities with HSP70s from other parasitic organisms and mammals. The characteristic domains, including N-terminal ATPase domain, calmodulin-binding domain, and EE(D)VD motif, found in HSP70s were also well conserved in this gene. The recombinant Nf-cHSP70 protein showed strong antigenicity against the sera from mice experimentally infected with N. fowleri. Immunofluorescence assay showed that Nf-cHSP70 localized in cytosol of the parasite. The results from semi-quantitative RT-PCR and Western blot analyses demonstrated the expression levels of gene transcripts, and its products were significantly increased at high temperature (42 degrees C). The definitive biological roles of Nf-cHSP70 are not clear, but it may protect the parasite under environmental changes especially high temperature.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsCloning, MolecularConserved SequenceCytosolDNA, ProtozoanGene Expression RegulationHSP70 Heat-Shock ProteinsMicroscopy, FluorescenceMolecular Sequence DataNaegleria fowleriOpen Reading FramesProtein Structure, TertiaryProtozoan ProteinsReverse Transcriptase Polymerase Chain ReactionDNA, ProtozoanHSP70 Heat-Shock ProteinsProtozoan ProteinsRNA, MessengerRNA, Protozoan

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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.