Evidence map›Paper›PMID 23054027›Full record

ArticleMolecular biology reports2013

Characterization of the open reading frame 7a from Bombyx mori nucleopolyhedrovirus.

Yong Liu, Feng Yu, Huiling Wu, Qing Cao, Yu Wu, Yan Wu, Wenbing Wang

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In one paragraph

Article in Molecular biology reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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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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3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 0 citations in OpenAlex.

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4 · The record

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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 1 institution in 1 country.

Yong LiuInstitute of Life Science, Jiangsu University, Zhenjiang, China.
Feng Yu
Huiling Wu
Qing Cao
Yu Wu
Yan Wu
Wenbing Wang
Jiangsu University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The open reading frame 7a of the Bombyx mori nucleopolyhedrovirus (BmNPV orf7a, Bm7a) encodes a predicted polypeptide consisting of 53 amino acid residues. While this polypeptide's homologues were found in certain baculoviruses, its function has not yet been studied. A protein structural assay revealed that the polypeptide expressed from this gene contained a predicted signal peptide at its N-terminus. To investigate the expression of Bm7a, 3'rapid amplification of cDNA ends was used to detect its transcript. A series of recombinant viruses were also constructed to analyze the cellular localization of the Bm7a products. The results indicated that the Bm7a gene is co-transcribed with bv/odv-e26 and orf9. The function of BM7a was studied by using fused enhanced green fluorescence protein (eGFP) as a visual marker to trace the localization of the protein during infection. Fluorescence was observed in the cellular membrane of the infected cells by confocal microscopy. Western blot analysis using an eGFP-antibody also showed that the BM7a-eGFP fusion protein was present in the budded virions (BVs). These data implied that BM7a is a component of the BV. In this work, we identified the function of the Bm7a gene and suggested that it may play a role in BV packaging.

Indexed as

Open Reading FramesAmino Acid SequenceAnimalsBombyxCell MembraneGene ExpressionGene Expression Regulation, ViralGreen Fluorescent ProteinsMicroscopy, ConfocalMicroscopy, FluorescenceMolecular Sequence DataNucleopolyhedrovirusesProtein TransportRecombinant Fusion ProteinsSequence Analysis, ProteinSequence Homology, Amino Acidenhanced green fluorescent proteinGreen Fluorescent ProteinsRecombinant Fusion ProteinsViral Structural Proteins

Identifiers

PMID23054027
OpenAlexW1991034300

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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.