Evidence map›Paper›PMID 18242161›Full record

ArticleArchives of biochemistry and biophysics2008

The mouse and human Ah receptor differ in recognition of LXXLL motifs.

Colin Flaveny, Rashmeet K Reen, Ann Kusnadi, Gary H Perdew

Open access · greenAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

32 citing papers in PubMed, 48 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

4 authors at 1 institution in 1 country.

Colin FlavenyCenter for Molecular Toxicology and Carcinogenesis, Department of Veterinary and Biomedical Sciences, Pennsylvania State University, 309A Life Sciences Building, University Park, PA 16802, USA.
Rashmeet K Reen
Ann Kusnadi
Gary H Perdew
Pennsylvania State University · US

Funding

REGULATION OF THE AH RECEPTORR01ES004869 · NIEHS · PURDUE UNIVERSITY WEST LAFAYETTE · PI PERDEW, GARY H. · 1994 to 2017
$5.3M
Biochemical analysis of the human vs. mouse Ah receptorR01ES011834 · NIEHS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI PERDEW, GARY H · 2004 to 2007
$1.0M
BIOCHEMICAL CHARACTERIZATION OF THE AH RECEPTORR29ES004869 · NIEHS · PURDUE UNIVERSITY WEST LAFAYETTE · PI PERDEW, GARY H · 1989 to 1993
–
NIEHS NIH HHS ES011834NIEHS NIH HHS ES04869NIEHS NIH HHS R01 ES004869NIEHS NIH HHS R01 ES011834
6 · The paper itself

Abstract

The aryl hydrocarbon receptor (AhR) is a ligand inducible transcription factor that exhibits interspecies differences, with the human and mouse AhR C-terminal transactivation domain sharing only 58% amino acid sequence identity. The AhR has a transactivation domain comprised of proline/serine/threonine-rich, glutamine-rich, and acidic amino acid subdomains. A truncated mAhR and hAhR containing only the acidic subdomain displayed widely differing transactivation potentials. Whether the glutamine-rich subdomain of the mouse AhR and the human AhR differentially recruit LXXLL-motif coactivators was investigated. Transiently expressed GAL4 DNA binding domain (GAL4DBD)-LXXLL-motif fusion proteins were used to map the critical LXXLL binding sequence of the hAhR to amino acid residues 663-688. Several LXXLL-motif GAL4DBD fusion proteins dramatically differed in their ability to influence the transactivation potential of the mAhR and hAhR. These findings suggest that the human and mouse AhR may display differential recruitment of coactivators and hence may exhibit divergent regulation of target genes.

Indexed as

Amino Acid MotifsAmino Acids, AcidicAmino Acid SequenceAnimalsBase SequenceBasic Helix-Loop-Helix ProteinsDNA-Binding ProteinsGlutamineHumansMiceMolecular Sequence DataProlineReceptors, Aryl HydrocarbonRecombinant Fusion ProteinsRecombinant ProteinsSaccharomyces cerevisiae ProteinsAHR protein, humanAhr protein, mouseAmino Acids, AcidicBasic Helix-Loop-Helix ProteinsDNA-Binding ProteinsGAL4 (1-147) protein, S cerevisiaeGlutamineProlineReceptors, Aryl HydrocarbonRecombinant Fusion ProteinsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSerineThreonineTranscription Factors

Identifiers

PMID18242161
PMCPMC2293825
OpenAlexW2009928548

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.