Evidence map›Paper›PMID 2187178›Full record

ArticleNucleic acids research1990

Characterisation of the DNA binding domain of the yeast RAP1 protein.

Y A Henry, A Chambers, J S Tsang, A J Kingsman, S M Kingsman

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Nucleic acids research, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

36 citing papers in PubMed, 70 citations in OpenAlex.

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  11. Multiple domains of repressor activator protein 1 contribute to facilitated binding of glycolysis regulatory protein 1.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
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  20. Promotion of parallel DNA quadruplexes by a yeast telomere binding protein: a circular dichroism study.Proceedings of the National Academy of Sciences of the United States of America · 1994
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Y A HenryDepartment of Biochemistry, Oxford University, UK.
A Chambers
J S Tsang
A J Kingsman
S M Kingsman
University of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 827 amino acid yeast RAP1 protein interacts with DNA to regulate gene expression at numerous unrelated loci in the yeast genome. By a combination of amino, carboxy and internal deletions, we have defined an internal 235 amino acid fragment of the yeast RAP1 protein that can bind efficiently to the RAP1 binding site of the PGK Upstream Activation Sequence (UAS). This domain spans residues 361 to 596 of the full length protein and lacks any homology to the DNA binding 'zinc finger' or 'helix-turn-helix' structural motifs. All the RAP1 binding sites we have tested bind domain 361-596, arguing that RAP1 binds all its chromosomal sites via this domain. The domain could not be further reduced in size suggesting that it represents the minimal functional DNA binding domain. The relevance of potential regions of secondary structure within the minimal binding domain is discussed.

Indexed as

Regulatory Sequences, Nucleic AcidTranscription FactorsBase SequenceDNA-Binding ProteinsDNA, FungalElectrophoresis, Polyacrylamide GelFungal ProteinsMolecular Sequence DataProtein ConformationRestriction MappingSaccharomyces cerevisiaeDNA-Binding ProteinsDNA, FungalFungal ProteinsTranscription Factors

Identifiers

PMID2187178
PMCPMC330744
OpenAlexW1998107630

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.