Evidence map›Paper›PMID 12953115›Full record

ArticleThe Plant cell2003

Phosphorylation of the potyvirus capsid protein by protein kinase CK2 and its relevance for virus infection.

Konstantin I Ivanov, Pietri Puustinen, Rasa Gabrenaite, Helena Vihinen, Lars Rönnstrand, Leena Valmu, Nisse Kalkkinen, Kristiina Mäkinen

Open access · greenAbstract readComparative Study
In one paragraph

Article in The Plant cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
11.3field-weighted citation impact, top 2% 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

51 citing papers in PubMed, 140 citations in OpenAlex.

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  16. The conserved aromatic residue WMolecular plant pathology · 2021
    Article
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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

8 authors at 2 institutions in 2 countries.

Konstantin I IvanovInstitute of Biotechnology, University of Helsinki, FIN-00014 Helsinki, Finland. konstantin.ivanov@helsinki.fi
Pietri Puustinen
Rasa Gabrenaite
Helena Vihinen
Lars Rönnstrand
Leena Valmu
Nisse Kalkkinen
Kristiina Mäkinen
University of Helsinki · FILudwig Cancer Research · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We reported previously that the capsid protein (CP) of Potato virus A (PVA) is phosphorylated both in virus-infected plants and in vitro. In this study, an enzyme that phosphorylates PVA CP was identified as the protein kinase CK2. The alpha-catalytic subunit of CK2 (CK2alpha) was purified from tobacco and characterized using in-gel kinase assays and liquid chromatography-tandem mass spectrometry. The tobacco CK2alpha gene was cloned and expressed in bacterial cells. Specific antibodies were raised against the recombinant enzyme and used to demonstrate the colocalization of PVA CP and CK2alpha in infected tobacco protoplasts. A major site of CK2 phosphorylation in PVA CP was identified by a combination of mass spectrometric analysis, radioactive phosphopeptide sequencing, and mutagenesis as Thr-242 within a CK2 consensus sequence. Amino acid substitutions that affect the CK2 consensus sequence in CP were introduced into a full-length infectious cDNA clone of PVA tagged with green fluorescent protein. Analysis of the mutant viruses showed that they were defective in cell-to-cell and long-distance movement. Using in vitro assays, we demonstrated that CK2 phosphorylation inhibited the binding of PVA CP to RNA, suggesting a molecular mechanism of CK2 action. These results suggest that the phosphorylation of PVA CP by CK2 plays an important regulatory role in virus infection.

Indexed as

Amino Acid SequenceCapsid ProteinsCasein Kinase IICatalysisDichlororibofuranosylbenzimidazoleGene Expression Regulation, EnzymologicGene Expression Regulation, PlantMolecular Sequence DataMutationNicotianaPhosphorylationPlant ProteinsPotyvirusProtein Serine-Threonine KinasesProtoplastsRecombinant ProteinsCapsid ProteinsCasein Kinase IIDichlororibofuranosylbenzimidazolePlant ProteinsProtein Serine-Threonine KinasesRecombinant ProteinsRNA-Binding ProteinsThreonine

Identifiers

PMID12953115
PMCPMC181335
OpenAlexW2112564006

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.