Evidence map›Paper›PMID 15640446›Full record

ArticleNucleic acids research2005

DNA-binding properties of ARID family proteins.

Antonia Patsialou, Deborah Wilsker, Elizabeth Moran

Abstract read
In one paragraph

Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
137citing papers in PubMed, 1 pooled it
–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

137 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
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  13. Review
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  18. Article
  19. The role of the polybromo-associated BAF complex in development.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2025
    Review
  20. Article

77 more citing papers are in PubMed but not listed here.

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

3 authors.

Antonia PatsialouFels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine Philadelphia, PA 19140, USA.
Deborah Wilsker
Elizabeth Moran

Funding

SHARED RESOURCES FOR CANCER RESEARCHR24CA088261 · NCI · TEMPLE UNIVERSITY · PI REDDY, E PREMKUMAR · 2001 to 2005
$1.3M
PROTEIN INTERACTIONS AND REPRESSION IN FUNCTION OF THE ER01CA053592 · NCI · TEMPLE UNIVERSITY · PI MORAN, ELIZABETH · 1991 to 2000
$332k
NCI NIH HHS CA53592NCI NIH HHS CA88261NCI NIH HHS R01 CA053592NCI NIH HHS R24 CA088261
6 · The paper itself

Abstract

The ARID (A-T Rich Interaction Domain) is a helix-turn-helix motif-based DNA-binding domain, conserved in all eukaryotes and diagnostic of a family that includes 15 distinct human proteins with important roles in development, tissue-specific gene expression and proliferation control. The 15 human ARID family proteins can be divided into seven subfamilies based on the degree of sequence identity between individual members. Most ARID family members have not been characterized with respect to their DNA-binding behavior, but it is already apparent that not all ARIDs conform to the pattern of binding AT-rich sequences. To understand better the divergent characteristics of the ARID proteins, we undertook a survey of DNA-binding properties across the entire ARID family. The results indicate that the majority of ARID subfamilies (i.e. five out of seven) bind DNA without obvious sequence preference. DNA-binding affinity also varies somewhat between subfamilies. Site-specific mutagenesis does not support suggestions made from structure analysis that specific amino acids in Loop 2 or Helix 5 are the main determinants of sequence specificity. Most probably, this is determined by multiple interacting differences across the entire ARID structure.

Indexed as

Amino Acids, AromaticAmino Acid SequenceBinding SitesDNADNA-Binding ProteinsDrosophila ProteinsHelix-Turn-Helix MotifsHomeodomain ProteinsHumansMolecular Sequence DataMutationNuclear ProteinsNucleic Acid ConformationProtein Structure, TertiarySequence AlignmentTranscription FactorsAmino Acids, AromaticARID1A protein, humanDNADNA-Binding ProteinsDrosophila ProteinsHomeodomain ProteinsNuclear ProteinsRetn protein, DrosophilaTranscription Factors

Identifiers

PMID15640446
PMCPMC546134

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.