Evidence map›Paper›PMID 27348862›Full record

ArticlePloS one2016

ICP35 Is a TREX-Like Protein Identified in White Spot Syndrome Virus.

Panapat Phairoh, Thana Suthibatpong, Triwit Rattanarojpong, Nujarin Jongruja, Saengchan Senapin, Kiattawee Choowongkomon, Pongsak Khunrae

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.4field-weighted citation impact, top 27% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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 3 institutions in 1 country.

Panapat PhairohDepartment of Microbiology, Faculty of Science, King Mongkut's University of Technology Thonburi, Bangmod, Bangkok, 10140, Thailand.
Thana SuthibatpongDepartment of Physics, Faculty of Science, King Mongkut's University of Technology Thonburi, Bangmod, Bangkok, 10140, Thailand.
Triwit RattanarojpongDepartment of Microbiology, Faculty of Science, King Mongkut's University of Technology Thonburi, Bangmod, Bangkok, 10140, Thailand.
Nujarin JongrujaDepartment of Microbiology, Faculty of Science, King Mongkut's University of Technology Thonburi, Bangmod, Bangkok, 10140, Thailand.
Saengchan SenapinNational Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Pathumthani, 12120, Thailand.
Kiattawee ChoowongkomonDepartment of Biochemistry Faculty of Science Kasetsart University, Bangkok, 10900, Thailand.
Pongsak KhunraeDepartment of Microbiology, Faculty of Science, King Mongkut's University of Technology Thonburi, Bangmod, Bangkok, 10140, Thailand.
King Mongkut's University of Technology Thonburi · THKasetsart University · THNational Science and Technology Development Agency · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ICP35 is a non-structural protein from White spot syndrome virus believed to be important in viral replication. Since ICP35 was found to localize in the host nucleus, it has been speculated that the function of ICP35 might be involved in the interaction of DNA. In this study, we overexpressed, purified and characterized ICP35. The thioredoxin-fused ICP35 (thio-ICP35) was strongly expressed in E. coli and be able to form itself into dimers. Investigation of the interaction between ICP35 and DNA revealed that ICP35 can perform DNase activity. Structural model of ICP35 was successfully built on TREX1, suggesting that ICP35 might adopt the folding similar to that of TREX1 protein. Several residues important for dimerization in TREX1 are also conserved in ICP35. Residue Asn126 and Asp132, which are seen to be in close proximity to metal ions in the ICP35 model, were shown through site-directed mutagenesis to be critical for DNase activity.

Indexed as

Cloning, MolecularEnzyme ActivationExodeoxyribonucleasesGene ExpressionHydrogen BondingModels, MolecularMutagenesisPhosphoproteinsProtein ConformationProtein MultimerizationRecombinant ProteinsViral Nonstructural ProteinsWhite spot syndrome virus 1ExodeoxyribonucleasesPhosphoproteinsRecombinant Proteinsthree prime repair exonuclease 1Viral Nonstructural Proteins

Identifiers

PMID27348862
PMCPMC4922627
OpenAlexW2461441982

What OpenQuestion holds

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LicenceCC BY
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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.