Evidence map›Paper›PMID 12612084›Full record

ArticleMolecular and cellular biology2003

Electrostatic modulation in steroid receptor recruitment of LXXLL and FXXLF motifs.

Bin He, Elizabeth M Wilson

Abstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. The challenges of androgen insensitivity syndrome.Archives of medical science : AMS · 2022
    Article
  5. Computer-Aided Ligand Discovery for Estrogen Receptor Alpha.International journal of molecular sciences · 2020
    Review
  6. Modulation of androgen receptor DNA binding activity through direct interaction with the ETS transcription factor ERG.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Endostatin: A novel inhibitor of androgen receptor function in prostate cancer.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Analysis of interdomain interactions of the androgen receptor.Methods in molecular biology (Clifton, N.J.) · 2011
    Article
  19. Article
  20. Article
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

2 authors.

Bin HeLaboratories for Reproductive Biology, Department of Biochemistry and Biophysics, University of North Carolina, 374 Medical Sciences Research Building, Chapel Hill, NC 27599-7500, USA.
Elizabeth M Wilson

Funding

TESTIS SPECIFIC HISTONE BINDING PROTEIN (NASP)U54HD035041 · NICHD · UNIV OF NORTH CAROLINA CHAPEL HILL · PI PETRUSZ, PETER · 1997 to 2011
$16.1M
ANDROGEN RECEPTOR REGULATION OF REPRODUCTIVE FUNCTIONR01HD016910 · NICHD · UNIV OF NORTH CAROLINA CHAPEL HILL · PI WILSON, ELIZABETH M. · 1985 to 2010
$2.8M
ANDROGEN RECEPTOR REGULATION OF REPRODUCTIVE FUNCTIONR37HD016910 · NICHD · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI WILSON, ELIZABETH M. · 1993 to 2002
$1.1M
NICHD NIH HHS HD 16910NICHD NIH HHS R01 HD016910NICHD NIH HHS R37 HD016910NICHD NIH HHS U54 HD035041NICHD NIH HHS U54 HD 35041
6 · The paper itself

Abstract

Coactivator recruitment by activation function 2 (AF2) in the steroid receptor ligand binding domain takes place through binding of an LXXLL amphipathic alpha-helical motif at the AF2 hydrophobic surface. The androgen receptor (AR) and certain AR coregulators are distinguished by an FXXLF motif that interacts selectively with the AR AF2 site. Here we show that LXXLL and FXXLF motif interactions with steroid receptors are modulated by oppositely charged residues flanking the motifs and charge clusters bordering AF2 in the ligand binding domain. An increased number of charged residues flanking AF2 in the ligand binding domain complement the two previously characterized charge clamp residues in coactivator recruitment. The data suggest a model whereby coactivator recruitment to the receptor AF2 surface is initiated by complementary charge interactions that reflect a reversal of the acidic activation domain-coactivator interaction model.

Indexed as

Protein Interaction MappingAcetyltransferasesAmino Acid MotifsAmino Acid SequenceAnimalsBinding SitesCarcinoma, HepatocellularChlorocebus aethiopsCOS CellsHistone AcetyltransferasesHumansLigandsLiver NeoplasmsModels, MolecularMolecular Sequence DataNuclear Receptor Coactivator 1AcetyltransferasesHistone AcetyltransferasesLigandsNCOA1 protein, humanNCOA3 protein, humanNuclear Receptor Coactivator 1Nuclear Receptor Coactivator 2Nuclear Receptor Coactivator 3Oncogene ProteinsPeptide FragmentsReceptors, AndrogenReceptors, SteroidRecombinant Fusion ProteinsTrans-ActivatorsTranscription Factors

Identifiers

PMID12612084
PMCPMC149467

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.