Evidence map›Paper›PMID 10757798›Full record

ArticleMolecular and cellular biology2000

The human SWI-SNF complex protein p270 is an ARID family member with non-sequence-specific DNA binding activity.

P B Dallas, S Pacchione, D Wilsker, V Bowrin, R Kobayashi, E Moran

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

67 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
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  3. Muscle-specific pyruvate kinase isoforms, PKM1 and PKM2, regulate mammalian SWI/SNF proteins and histone 3 phosphorylation during myoblast differentiation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
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7 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

6 authors at 2 institutions in 1 country.

P B DallasFels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, Pennsylvania 19140, USA.
S Pacchione
D Wilsker
V Bowrin
R Kobayashi
E Moran
Temple University · USCold Spring Harbor Laboratory · US

Funding

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 R01 CA053592
6 · The paper itself

Abstract

p270 is an integral member of human SWI-SNF complexes, first identified through its shared antigenic specificity with p300 and CREB binding protein. The deduced amino acid sequence of p270 reported here indicates that it is a member of an evolutionarily conserved family of proteins distinguished by the presence of a DNA binding motif termed ARID (AT-rich interactive domain). The ARID consensus and other structural features are common to both p270 and yeast SWI1, suggesting that p270 is a human counterpart of SWI1. The approximately 100-residue ARID sequence is present in a series of proteins strongly implicated in the regulation of cell growth, development, and tissue-specific gene expression. Although about a dozen ARID proteins can be identified from database searches, to date, only Bright (a regulator of B-cell-specific gene expression), dead ringer (a Drosophila melanogaster gene product required for normal development), and MRF-2 (which represses expression from the cytomegalovirus enhancer) have been analyzed directly in regard to their DNA binding properties. Each binds preferentially to AT-rich sites. In contrast, p270 shows no sequence preference in its DNA binding activity, thereby demonstrating that AT-rich binding is not an intrinsic property of ARID domains and that ARID family proteins may be involved in a wider range of DNA interactions.

Indexed as

Nuclear ProteinsAmino Acid SequenceBase SequenceBlotting, NorthernDNA-Binding ProteinsDNA, ComplementaryHumansModels, GeneticMolecular Sequence DataMultigene FamilyMutationProtein BiosynthesisRecombinant Fusion ProteinsSequence Analysis, ProteinSequence Homology, Amino AcidTissue DistributionARID1A protein, humanDNA-Binding ProteinsDNA, ComplementaryNuclear ProteinsRecombinant Fusion ProteinsTranscription Factors

Identifiers

PMID10757798
PMCPMC85608
OpenAlexW2105905346

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.