Evidence map›Paper›PMID 11095727›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Identification of the residues in the Myb domain of maize C1 that specify the interaction with the bHLH cofactor R.

E Grotewold, M B Sainz, L Tagliani, J M Hernandez, B Bowen, V L Chandler

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 166 papers.

0numbers the graph read from it
0cells of the map it votes in
166citing papers in PubMed
2.8field-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

166 citing papers in PubMed, 350 citations in OpenAlex.

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  12. Proanthocyanidin biosynthesis and postharvest seed coat darkening in pinto bean.Phytochemistry reviews : proceedings of the Phytochemical Society of Europe · 2025
    Review
  13. Rapid recovery of homozygousFrontiers in plant science · 2025
    Article
  14. Article
  15. Article
  16. Evolutionary trajectory of transcription factors and selection of targets for metabolic engineering.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  17. Genome-Wide Identification of the bHLH Gene Family inInternational journal of molecular sciences · 2024
    Article
  18. An Isoflavone Synthase Gene inPlants (Basel, Switzerland) · 2024
    Article
  19. Overexpression of a 'Plants (Basel, Switzerland) · 2024
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  20. Article

106 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.

E GrotewoldDepartment of Plant Biology and Plant Biotechnology Center, Ohio State University, Columbus, OH 43210, USA. 1Wosu.edu
M B Sainz
L Tagliani
J M Hernandez
B Bowen
V L Chandler
Pioneer Hi-Bred · USUniversity of Arizona · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The maize Myb transcription factor C1 depends on the basic helix-loop-helix (bHLH) proteins R or B for regulatory function, but the closely related Myb protein P does not. We have used the similarity between the Myb domains of C1 and P to identify residues that specify the interaction between the Myb domain of C1 and the N-terminal region of R. Substitution of four predicted solvent-exposed residues in the first helix of the second Myb repeat of P with corresponding residues from C1 is sufficient to confer on P the ability to physically interact with R. However, two additional Myb domain amino acid changes are needed to make the P regulatory activity partially dependent on R in maize cells. Interestingly, when P is altered so that it interacts with R, it can activate the Bz1 promoter, normally regulated by C1 + R but not by P. Together, these findings demonstrate that the change of a few amino acids within highly similar Myb domains can mediate differential interactions with a transcriptional coregulator that plays a central role in the regulatory specificity of C1, and that Myb domains play important roles in combinatorial transcriptional regulation.

Indexed as

Amino Acid SequenceBasic Helix-Loop-Helix ProteinsDNA-Binding ProteinsModels, MolecularMolecular Sequence DataProtein BindingProto-Oncogene Proteins c-mybSequence Homology, Amino AcidTranscription FactorsTwo-Hybrid System TechniquesZea maysBasic Helix-Loop-Helix ProteinsDNA-Binding ProteinsProto-Oncogene Proteins c-mybTranscription Factors

Identifiers

PMID11095727
PMCPMC17618
OpenAlexW2075503913

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.