ArticleVirology2008
Nuclear trafficking of the human cytomegalovirus pp71 (ppUL82) tegument protein.
Article in Virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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.
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.
Who cites it
17 citing papers in PubMed.
- Human cytomegalovirus UL82 promotes colorectal cancer cell proliferation through inhibiting the ubiquitination of OGDH via ANGPT2.Tumour virus research · 2025Article
- Isolation of a Monoclonal Human scFv Against Cytomegalovirus pp71 Antigen Using Yeast Display.Antibodies (Basel, Switzerland) · 2025Article
- Crystal structure of the tegument protein UL82 (pp71) from human cytomegalovirus.Protein science : a publication of the Protein Society · 2024Article
- Duck enteritis virus pUL47, as a late structural protein localized in the nucleus, mainly depends on residues 40 to 50 and 768 to 777 and inhibits IFN-β signalling by interacting with STAT1.Veterinary research · 2020Article
- Phosphorylation of tegument protein pp28 contributes to trafficking to the assembly compartment in human cytomegalovirus infection.Journal of microbiology (Seoul, Korea) · 2020Article
- Expanding the Known Functional Repertoire of the Human Cytomegalovirus pp71 Protein.Frontiers in cellular and infection microbiology · 2020Review
- Coevolution pays off: Herpesviruses have the license to escape the DNA sensing pathway.Medical microbiology and immunology · 2019Review
- The life cycle and pathogenesis of human cytomegalovirus infection: lessons from proteomics.Expert review of proteomics · 2014Article
- Review
- Granzyme M targets host cell hnRNP K that is essential for human cytomegalovirus replication.Cell death and differentiation · 2013Article
- Tale of a tegument transactivator: the past, present and future of human CMV pp71.Future virology · 2012Article
- BclAF1 restriction factor is neutralized by proteasomal degradation and microRNA repression during human cytomegalovirus infection.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Regulation of nucleocytoplasmic trafficking of viral proteins: an integral role in pathogenesis?Biochimica et biophysica acta · 2011Review
- Nuclear localization of tegument-delivered pp71 in human cytomegalovirus-infected cells is facilitated by one or more factors present in terminally differentiated fibroblasts.Journal of virology · 2010Article
- Functional properties of the human cytomegalovirus IE86 protein required for transcriptional regulation and virus replication.Journal of virology · 2010Article
- Cellular and viral control over the initial events of human cytomegalovirus experimental latency in CD34+ cells.Journal of virology · 2010Article
- Properties of virion transactivator proteins encoded by primate cytomegaloviruses.Virology journal · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
Abstract
The human cytomegalovirus tegument protein pp71 localizes to the nucleus immediately upon infection, and functions to initiate viral gene expression. Analysis of a series of random insertion mutations revealed that sequences within the mid region (MR) of pp71 are important for localization to the nucleus. Fusion of MR sequences with eGFP revealed that amino acids 94 to 300 were sufficient to target proteins to the nucleus. Random substitution mutagenesis within this domain resulted in two double substitution mutants, pp71P203T/T223M and pp71T228M/L275Q, with a predominantly cytoplasmic localization. Disruption of nuclear targeting resulted in relocalization of the fusion proteins to a distinct perinuclear region. Using tandem mass spectrometry, we determined that threonine 223 can be phosphorylated. Mutation of this residue to a phosphomimetic amino acid resulted in abrogation of nuclear targeting. These results strongly suggest that the intracellular trafficking of pp71 is regulated by phosphorylation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.