Evidence map›Paper›PMID 20633584›Full record

ArticleVirus research2010

Molecular anatomy of subcellular localization of HSV-1 tegument protein US11 in living cells.

Junji Xing, Fuqing Wu, Weiwei Pan, Chunfu Zheng

Abstract read
In one paragraph

Article in Virus research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact
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

22 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

4 authors.

Junji XingMolecular Virology and Viral Immunology Research Group, State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, 44 Xiaohongshan, Wuchang, Wuhan 430071, PR China.
Fuqing Wu
Weiwei Pan
Chunfu Zheng

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The herpes simplex virus type I (HSV-1) US11 protein is an RNA-binding multifunctional regulator that specifically and stably associates with nucleoli. Although the C-terminal part of US11 was responsible for its nucleolar localization, the precise nucleolar localization signal (NoLS) and nuclear export signal (NES) of US11 and its nuclear import and export mechanisms are still elusive. In this study, fluorescence microscopy was employed to investigate the subcellular localization of US11 and characterize its transport mechanism in living cells. By constructing a series of deletion mutants fused with enhanced yellow fluorescent protein (EYFP), three novel NoLSs of US11 were for the first time mapped to amino acids 84-125, 126-152, and 89-146, respectively. Additionally, the NES was identified to locate between amino acids 89 and 119. Furthermore, the US11 protein was demonstrated to target to the cytoplasm through the NES by chromosomal region maintenance 1 (CRM1)-independent pathway, and to the nucleolus through Ran and importin beta-dependent mechanism that does not require importin alpha 5.

Indexed as

Amino Acid SequenceAnimalsArtificial Gene FusionBacterial ProteinsChlorocebus aethiopsHerpesvirus 1, HumanLuminescent ProteinsMicroscopy, FluorescenceMolecular Sequence DataProtein Sorting SignalsProtein TransportRecombinant Fusion ProteinsRNA-Binding ProteinsSequence AlignmentSequence Analysis, DNASequence DeletionBacterial ProteinsLuminescent ProteinsProtein Sorting SignalsRecombinant Fusion ProteinsRNA-Binding ProteinsUS11 protein, herpesvirusViral Proteinsyellow fluorescent protein, Bacteria

Identifiers

PMID20633584
PMCPMC7114396

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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.