Evidence map›Paper›PMID 9443961›Full record

ArticleNucleic acids research1998

A cysteine residue in helixII of the bHLH domain is essential for homodimerization of the yeast transcription factor Pho4p.

D Shao, C L Creasy, L W Bergman

Abstract read
In one paragraph

Article in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Knockout of the Hmt1p Arginine Methyltransferase inMolecular & cellular proteomics : MCP · 2018
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. DNA bending by bHLH charge variants.Nucleic acids research · 2006
    Article
  9. Article
  10. Review
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.

D ShaoDepartment of Microbiology and Immunology, Allegheny University of the Health Sciences, 2900 Queen Lane, Philadelphia, PA 19102, USA.
C L Creasy
L W Bergman

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast transcription factor Pho4p is required for expression of the phosphate-repressible acid phosphatase encoded by the PHO5 gene. Functional studies have shown that the molecule is composed of an N-terminal acidic activation domain, a central region which is necessary for interaction with a negative regulatory factor (the cyclin Pho80) and a C-terminal basic helix-loop-helix domain, which mediates DNA binding and homodimerization. In this study the homodimerization domain maps specifically to helixII of this region and a cysteine residue within this region is essential for this function. Experiments support the role of an intermolecular disulfide bond in stabilization of homodimerization, which is critical for DNA binding.

Indexed as

DNA-Binding ProteinsHelix-Loop-Helix MotifsSaccharomyces cerevisiae ProteinsAmino Acid SequenceCysteineDimerizationDisulfidesFungal ProteinsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein DenaturationProtein Structure, SecondaryProto-Oncogene Proteins c-mycRecombinant Fusion ProteinsSaccharomyces cerevisiaeCysteineDisulfidesDNA-Binding ProteinsFungal ProteinsPHO4 protein, S cerevisiaeProto-Oncogene Proteins c-mycRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID9443961
PMCPMC147311

What OpenQuestion holds

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Registered trials

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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.