Evidence map›Paper›PMID 18614635›Full record

ArticleJournal of virology2008

Distinct requirements of adenovirus E1b55K protein for degradation of cellular substrates.

Rachel A Schwartz, Seema S Lakdawala, Heather D Eshleman, Matthew R Russell, Christian T Carson, Matthew D Weitzman

Abstract 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 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
–field-weighted citation impact
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

43 citing papers in PubMed.

  1. Article
  2. Review
  3. The Pathology of Viral Infections.Advances in experimental medicine and biology · 2026
    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

6 authors.

Rachel A SchwartzLaboratory of Genetics, The Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
Seema S Lakdawala
Heather D Eshleman
Matthew R Russell
Christian T Carson
Matthew D Weitzman

Funding

Viral Modulation of Genetic StabilityR01CA097093 · NCI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI WEITZMAN, MATTHEW D. · 2003 to 2019
$5.2M
NCI NIH HHS CA97093NCI NIH HHS R01 CA097093
6 · The paper itself

Abstract

The E1b55K and E4orf6 proteins of adenovirus type 5 (Ad5) assemble into a complex together with cellular proteins including cullin 5, elongins B and C, and Rbx1. This complex possesses E3 ubiquitin ligase activity and targets cellular proteins for proteasome-mediated degradation. The ligase activity has been suggested to be responsible for all functions of E1b55K/E4orf6, including promoting efficient viral DNA replication, preventing a cellular DNA damage response, and stimulating late viral mRNA nuclear export and late protein synthesis. The known cellular substrates for degradation by E1b55K/E4orf6 are the Mre11/Rad50/Nbs1 DNA repair complex, the tumor suppressor p53, and DNA ligase IV. Here we show that the degradation of individual targets can occur independently of other substrates. Furthermore, we identify separation-of-function mutant forms of E1b55K that can distinguish substrates for binding and degradation. Our results identify distinct regions of E1b55K that are involved in substrate recognition but also imply that there are additional requirements beyond protein association. These mutant proteins will facilitate the determination of the relevance of specific substrates to the functions of E1b55K in promoting infection and inactivating host defenses.

Indexed as

Adenovirus E1B ProteinsAdenovirus E4 ProteinsAdenoviruses, HumanCell Cycle ProteinsCell LineDNA-Binding ProteinsDNA Ligase ATPDNA LigasesDown-RegulationGenes, Tumor SuppressorHeLa CellsHumansMRE11 Homologue ProteinMutationNuclear ProteinsProteasome Endopeptidase ComplexAdenovirus E1B ProteinsAdenovirus E4 ProteinsCell Cycle ProteinsDNA-Binding ProteinsDNA Ligase ATPDNA LigasesLIG4 protein, humanMRE11 Homologue ProteinMRE11 protein, humanNBN protein, humanNuclear ProteinsProteasome Endopeptidase ComplexProteinsRNA, MessengerTumor Suppressor Protein p53Ubiquitin-Protein LigasesViral Proteins

Identifiers

PMID18614635
PMCPMC2546875

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.