Evidence map›Paper›PMID 23053938›Full record

ArticleMolecular biology reports2012

Molecular cloning, expression and characterization of a novel vacuolar protein sorting 4 gene in silkworm, Bombyx mori.

Hengchuan Xia, Chunxia Zhang, Fan Feng, Yi Yuan, Yang Zhou, Xiaoyong Liu, Keming Zhu, Qin Yao, Keping Chen

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Article in Molecular biology reports, 2012. 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
0.4field-weighted citation impact, top 28% of its field
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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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, 4 citations in OpenAlex.

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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 at 1 institution in 1 country.

Hengchuan XiaInstitute of Life Sciences, Jiangsu University, 301 Xuefu Road, Zhenjiang, Jiangsu 212013, People's Republic of China.
Chunxia Zhang
Fan Feng
Yi Yuan
Yang Zhou
Xiaoyong Liu
Keming Zhu
Qin Yao
Keping Chen
Jiangsu University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The vacuolar protein sorting 4 (Vps4) protein is essential for the multivesicular body (MVB) pathway, virus budding process and cytokinesis. Vps4 has been identified and characterized from many species, but not from silkworm Bombyx mori. In this study, we firstly identified and cloned the silkworm homologous gene for VPS4, expressed it in Escherichia coli, purified and characterized the protein designated as BmVps4. The BmVps4 cDNA contains an open reading frame of 1,314 bp, and encodes a protein of 438 amino acid residues. BmVps4 is of high sequence-similarity to Vps4 proteins from other species. The recombinant BmVps4 shows ATPase activity, which can be stimulated by Mg(2+) and inhibited by dominant mutations. Together, our data suggest BmVps4 is the genuine silkworm homologue of Vps4. To our knowledge, this is the first-time characterization of any silkworm MVB proteins. This study will facilitate further investigation of silkworm MVB pathway and its possible roles in the infection and budding of B. mori nuclear polyhedrosis virus (BmNPV), which is one of the most common and severe pathogens for silkworms. The cloned BmVps4 sequence is deposited in GenBank (Accession number GQ995504).

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceAmino Acid SubstitutionAnimalsBase SequenceBombyxCloning, MolecularConserved SequenceEndosomal Sorting Complexes Required for TransportEscherichia coliGene ExpressionInsect ProteinsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPhylogenyAdenosine TriphosphatasesEndosomal Sorting Complexes Required for TransportInsect Proteins

Identifiers

PMID23053938
OpenAlexW2072237437

What OpenQuestion holds

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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.