Evidence map›Paper›PMID 9094626›Full record

ArticleJournal of virology1997

Phosphorylation within the transactivation domain of adenovirus E1A protein by mitogen-activated protein kinase regulates expression of early region 4.

S G Whalen, R C Marcellus, A Whalen, N G Ahn, R P Ricciardi, P E Branton

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1997. 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
2.7field-weighted citation impact, top 10% 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, 63 citations in OpenAlex.

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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 at 1 institution in 1 country.

S G WhalenDepartment of Biochemistry, McGill University, Montreal, Quebec, Canada.
R C Marcellus
A Whalen
N G Ahn
R P Ricciardi
P E Branton
McGill University · CA

Funding

ORGANIZATION &EXPRESSION OF ADENOVIRUS GENESR01CA029797 · NCI · WISTAR INSTITUTE · PI RICCIARDI, ROBERT PAUL · 1985 to 2006
$2.2M
NCI NIH HHS CA29797
6 · The paper itself

Abstract

A critical role of the 289-residue (289R) E1A protein of human adenovirus type 5 during productive infection is to transactivate expression of all early viral transcription. Sequences within and proximal to conserved region 3 (CR3) promote expression of these viral genes through interactions with a variety of transcription factors requiring the zinc binding motif in CR3 and in some cases a region at the carboxy-terminal end of CR3, including residues 183 to 188. It is known that 3',5' cyclic AMP (cAMP) reduces the level of phosphorylation of the 289R E1A protein through the activation of protein phosphatase 2A by the E4orf4 protein. This study was designed to identify the E1A phosphorylation sites affected by E4orf4 expression and to determine their importance in regulation of E1A activity. We report here that two previously unidentified sites at Ser-185 and Ser-188 are the targets for decreased phosphorylation in response to cAMP. At least one of these sites, presumably Ser-185, is phosphorylated in vitro by purified mitogen-activated protein kinase (MAPK), and both are hyperphosphorylated in cells which express a constitutively active form of MAPK kinase. Analysis of E1A-mediated transactivation activity indicated that elevated phosphorylation at these sites increased expression of the E4 promoter but not that of E3. We have recently shown that one or more E4 products induce cell death due to p53-independent apoptosis, and thus it seems likely that one role of the E4orf4 protein is to limit production of toxic E4 products by limiting expression of the E4 promoter.

Indexed as

Gene Expression Regulation, ViralTranscriptional ActivationAdenovirus E1A ProteinsAdenovirus E4 ProteinsAmino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein KinasesCHO CellsCricetinaeCyclic AMPHeLa CellsHumansMiceMitogen-Activated Protein Kinase KinasesMolecular Sequence DataPhosphorylationAdenovirus E1A ProteinsAdenovirus E4 ProteinsCalcium-Calmodulin-Dependent Protein KinasesCyclic AMPMitogen-Activated Protein Kinase KinasesProtein Kinases

Identifiers

PMID9094626
PMCPMC191501
OpenAlexW1924891182

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.