Evidence map›Paper›PMID 10835359›Full record

ArticleThe EMBO journal2000

Solution structure of the MEF2A-DNA complex: structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors.

K Huang, J M Louis, L Donaldson, F L Lim, A D Sharrocks, G M Clore

Open access · greenAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

34 citing papers in PubMed, 126 citations in OpenAlex.

  1. Review
  2. Cracking the Floral Quartet Code: How Do Multimers of MIKCInternational journal of molecular sciences · 2023
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  12. MEF2D haploinsufficiency downregulates the NRF2 pathway and renders photoreceptors susceptible to light-induced oxidative stress.Proceedings of the National Academy of Sciences of the United States of America · 2017
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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 1 institution in 1 country.

K HuangLaboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0510, USA.
J M Louis
L Donaldson
F L Lim
A D Sharrocks
G M Clore
National Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The solution structure of the 33 kDa complex between the dimeric DNA-binding core domain of the transcription factor MEF2A (residues 1-85) and a 20mer DNA oligonucleotide comprising the consensus sequence CTA(A/T)(4)TAG has been solved by NMR. The protein comprises two domains: a MADS-box (residues 1-58) and a MEF2S domain (residues 59-73). Recognition and specificity are achieved by interactions between the MADS-box and both the major and minor grooves of the DNA. A number of critical differences in protein-DNA contacts observed in the MEF2A-DNA complex and the DNA complexes of the related MADS-box transcription factors SRF and MCM1 provide a molecular explanation for modulation of sequence specificity and extent of DNA bending ( approximately 15 versus approximately 70 degrees ). The structure of the MEF2S domain is entirely different from that of the equivalent SAM domain in SRF and MCM1, accounting for the absence of cross-reactivity with other proteins that interact with these transcription factors.

Indexed as

Amino Acid SequenceCross ReactionsDimerizationDNADNA-Binding ProteinsHumansMacromolecular SubstancesMADS Domain ProteinsMagnetic Resonance SpectroscopyMEF2 Transcription FactorsMinichromosome Maintenance 1 ProteinModels, MolecularMolecular Sequence DataMyogenic Regulatory FactorsNuclear ProteinsNucleic Acid ConformationDNADNA-Binding ProteinsMacromolecular SubstancesMADS Domain ProteinsMEF2A protein, humanMEF2 Transcription FactorsMinichromosome Maintenance 1 ProteinMyogenic Regulatory FactorsNuclear ProteinsRecombinant Fusion ProteinsSerum Response FactorSolutionsTranscription Factors

Identifiers

PMID10835359
PMCPMC212754
OpenAlexW2079070002

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.