Evidence map›Paper›PMID 18715931›Full record

ArticleJournal of virology2008

Epstein-barr virus encodes three bona fide ubiquitin-specific proteases.

Ramakrishna Sompallae, Stefano Gastaldello, Sebastian Hildebrand, Nikolay Zinin, Gerco Hassink, Kristina Lindsten, Juergen Haas, Bengt Persson, Maria G Masucci

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

29 citing papers in PubMed, 38 citations in OpenAlex.

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  18. Viral takeover of the host ubiquitin system.Frontiers in microbiology · 2011
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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 4 institutions in 4 countries.

Ramakrishna SompallaeDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden. maria.masucci@ki.se
Stefano Gastaldello
Sebastian Hildebrand
Nikolay Zinin
Gerco Hassink
Kristina Lindsten
Juergen Haas
Bengt Persson
Maria G Masucci
Karolinska Institutet · SELinköping University · SEUniversity of Edinburgh · GBUniversity of Padua · IT

Funding

Medical Research Council G0501453Medical Research Council G0501453(76475)
6 · The paper itself

Abstract

Manipulation of the ubiquitin proteasome system (UPS) is emerging as a common theme in viral pathogenesis. Some viruses have been shown to encode functional homologs of UPS enzymes, suggesting that a systematic identification of these products may provide new insights into virus-host cell interactions. Ubiquitin-specific proteases, collectively known as deubiquitinating enzymes (DUBs), regulate the activity of the UPS by hydrolyzing ubiquitin peptide or isopeptide bonds. The prediction of viral DUBs based on sequence similarity with known enzymes is hampered by the diversity of viral genomes. In this study sequence alignments, pattern searches, and hidden Markov models were developed for the conserved C- and H-boxes of the known DUB families and used to search the open reading frames (ORFs) of Epstein-Barr virus (EBV), a large gammaherpesvirus that has been implicated in the pathogenesis of a broad spectrum of human malignancies of lymphoid and epithelial cell origin. The searches identified a limited number of EBV ORFs that contain putative DUB catalytic domains. DUB activity was confirmed by functional assays and mutation analysis for three high scoring candidates, supporting the usefulness of this bioinformatics approach in predicting distant homologues of cellular enzymes.

Indexed as

Amino Acid MotifsAmino Acid SubstitutionArtificial Gene FusionComputational BiologyConserved SequenceEndopeptidasesGenes, ReporterGreen Fluorescent ProteinsHerpesvirus 4, HumanMutagenesis, Site-DirectedRecombinant Fusion ProteinsSequence AlignmentSequence Homology, Amino AcidUbiquitin-Specific ProteasesViral ProteinsEndopeptidasesGreen Fluorescent ProteinsRecombinant Fusion ProteinsUbiquitin-Specific ProteasesViral Proteins

Identifiers

PMID18715931
PMCPMC2573217
OpenAlexW2121272602

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.