Evidence map›Paper›PMID 30782840›Full record

ArticleThe Journal of biological chemistry2019

Cyclins B1, T1, and H differ in their molecular mode of interaction with cytomegalovirus protein kinase pUL97.

Mirjam Steingruber, Lena Keller, Eileen Socher, Sabrina Ferre, Anne-Marie Hesse, Yohann Couté, Friedrich Hahn, Nicole Büscher, Bodo Plachter, Heinrich Sticht and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 23 citations in OpenAlex.

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  13. Overview of Human Cytomegalovirus Pathogenesis.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
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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

11 authors at 5 institutions in 4 countries.

Mirjam SteingruberFrom the Institute for Clinical and Molecular Virology, 91054 Erlangen, Germany. Electronic address: mirjam.steingruber@uk-erlangen.de.
Lena KellerFrom the Institute for Clinical and Molecular Virology, 91054 Erlangen, Germany.
Eileen SocherDivision of Bioinformatics, Institute of Biochemistry Friedrich-Alexander University of Erlangen-Nürnberg, 91054 Erlangen, Germany.
Sabrina Ferrethe Université Grenoble Alpes, CEA, Inserm, BIG-BGE, 38000 Grenoble, France.
Anne-Marie Hessethe Université Grenoble Alpes, CEA, Inserm, BIG-BGE, 38000 Grenoble, France.
Yohann Coutéthe Université Grenoble Alpes, CEA, Inserm, BIG-BGE, 38000 Grenoble, France.
Friedrich HahnFrom the Institute for Clinical and Molecular Virology, 91054 Erlangen, Germany.
Nicole Büscherthe Institute for Virology, University Medical Center of the Johannes Gutenberg-University Mainz, 55131 Mainz, Germany.
Bodo Plachterthe Institute for Virology, University Medical Center of the Johannes Gutenberg-University Mainz, 55131 Mainz, Germany.
Heinrich StichtDivision of Bioinformatics, Institute of Biochemistry Friedrich-Alexander University of Erlangen-Nürnberg, 91054 Erlangen, Germany. Electronic address: heinrich.sticht@fau.de.
Manfred MarschallFrom the Institute for Clinical and Molecular Virology, 91054 Erlangen, Germany. Electronic address: manfred.marschall@fau.de.
Inserm · FRFriedrich-Alexander-Universität Erlangen-Nürnberg · DEJohannes Gutenberg University Mainz · DEInstitute of Virology of the Slovak Academy of Sciences · SKInternational Council on Mining and Metals · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human cytomegalovirus (HCMV) is a common β-herpesvirus causing life-long latent infections. HCMV replication interferes with cell cycle regulation in host cells because the HCMV-encoded cyclin-dependent kinase (CDK) ortholog pUL97 extensively phosphorylates the checkpoint regulator retinoblastoma protein. pUL97 also interacts with cyclins B1, T1, and H, and recent findings have strongly suggested that these interactions influence pUL97 substrate recognition. Interestingly, here we detected profound mechanistic differences among these pUL97-cyclin interactions. Our study revealed the following. (i) pUL97 interacts with cyclins B1 and H in a manner dependent on pUL97 activity and HCMV-specific cyclin modulation, respectively. (ii) The phosphorylated state of both proteins is an important determinant of the pUL97-cyclin B1 interaction. (iii) Activated phospho-Thr-315 cyclin H is up-regulated during HCMV replication. (iv) Thr-315 phosphorylation is independent of intracellular pUL97 or CDK7 activity. (v) pUL97-mediated

Indexed as

Cyclin B1Cyclin HCyclin TCytomegalovirusHEK293 CellsHumansPhosphorylationProtein DomainsProtein Structure, QuaternaryViral ProteinsVirus ReplicationCCNB1 protein, humanCCNH protein, humanCCNT1 protein, humanCyclin B1Cyclin HCyclin TpUL97 protein, cytomegalovirusViral Proteinscyclincyclins B1, T1, and Hhuman cytomegalovirusphosphorylationprotein assemblyprotein kinaseprotein phosphorylationregulatory interactionreprogrammingviral kinase pUL97–cyclin complexesviral replication

Identifiers

PMID30782840
PMCPMC6463711
OpenAlexW2917727340

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.