Evidence map›Paper›PMID 11071933›Full record

ArticleNucleic acids research2000

A network of yeast basic helix-loop-helix interactions.

K A Robinson, J I Koepke, M Kharodawala, J M Lopes

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

31 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Cytokinin-responsive P-type cyclins control Arabidopsis radial style morphology.The Plant journal : for cell and molecular biology · 2025
    Article
  3. The Direct and Individual Transcriptional Function of the Human Homodimeric and Heterodimeric Basic Helix-Loop-Helix Transcription Factors E47 and Scleraxis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  4. Article
  5. Essential Role of theMycobiology · 2025
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  8. Overexpression of the Apple (International journal of molecular sciences · 2021
    Article
  9. Review
  10. AMPK-Mediated Regulation of Alpha-Arrestins and Protein Trafficking.International journal of molecular sciences · 2019
    Review
  11. Article
  12. Frontiers in plant science · 2017
    Article
  13. Article
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  15. Article
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  17. Article
  18. 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

4 authors at 1 institution in 1 country.

K A RobinsonDepartment of Biological Sciences, Wayne State University, 5047 Gullen Mall, Detroit, MI 48202, USA.
J I Koepke
M Kharodawala
J M Lopes
Wayne State University · US

Funding

HSRD VA TPP 97-002
6 · The paper itself

Abstract

The Ino4 protein belongs to the basic helix-loop-helix (bHLH) family of proteins. It is known to form a dimer with Ino2p, which regulates phospholipid biosynthetic genes. Mammalian bHLH proteins have been shown to form multiple dimer combinations. However, this flexibility in dimerization had not been documented for yeast bHLH proteins. Using the yeast two-hybrid assay and a biochemical assay we show that Ino4p dimerizes with the Pho4p, Rtg1p, Rtg3p and Sgc1p bHLH proteins. Screening a yeast cDNA library identified three additional proteins that interact with Ino4p: Bck2p, YLR422W and YNR064C. The interaction with Bck2p prompted us to examine if any of the Bck2p-associated functions affect expression of phospholipid biosynthetic genes. We found that hyperosmotic growth conditions altered the growth phase regulation of a phospholipid biosynthetic gene, CHO1. There are two recent reports of initial whole genome yeast two-hybrid interactions. Interestingly, one of these reports identified five proteins that interact with Ino4p: Ino2p, Hcs1p, Apl2p, YMR317W and YNL279W. Ino2p is the only protein in common with the data presented here. Our finding that Ino4p interacts with five bHLH proteins suggests that Ino4p is likely to be a central player in the coordination of multiple biological processes.

Indexed as

Helix-Loop-Helix MotifsSaccharomyces cerevisiae ProteinsTrans-ActivatorsDNA-Binding ProteinsFungal ProteinsGene Expression Regulation, FungalLac OperonMethyltransferasesPhosphatidylethanolamine N-MethyltransferasePlasmidsProtein BindingRecombinant Fusion ProteinsSaccharomyces cerevisiaeTranscriptional ActivationTranscription FactorsTwo-Hybrid System TechniquesDNA-Binding ProteinsFungal ProteinsGAL4 protein, S cerevisiaeINO4 protein, S cerevisiaeMethyltransferasesPhosphatidylethanolamine N-MethyltransferaseRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsTrans-ActivatorsTranscription Factors

Identifiers

PMID11071933
PMCPMC113870
OpenAlexW2082397309

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.