Evidence map›Paper›PMID 12490719›Full record

ArticleNucleic acids research2002

Cooperative binding of Sox10 to DNA: requirements and consequences.

Beate Schlierf, Andreas Ludwig, Karin Klenovsek, Michael Wegner

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

33 citing papers in PubMed, 64 citations in OpenAlex.

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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

4 authors.

Beate SchlierfInstitut für Biochemie, Fahrstrasse 17, 91054 Erlangen, Germany.
Andreas Ludwig
Karin Klenovsek
Michael Wegner

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The high-mobility-group (HMG) domain containing transcription factor Sox10 is an important regulator of various processes including the development of neural crest cells and glial cells. Target gene promoters contain multiple Sox10-binding sites, which either support monomeric or cooperative, dimeric binding. The latter is unusual for Sox proteins and might contribute to functional specificity of Sox10. We find that specific amino acid residues in a conserved region immediately preceding the HMG domain of Sox10 are required for cooperative binding. These residues cooperate with the HMG domain during dimeric binding in a manner dependent on specific determinants within the first two alpha-helices of the HMG domain. Cooperativity of DNA binding is surprisingly refractory to changes in the overall conformation of the DNA-bound dimer. Whereas maintenance of cooperativity is essential for full activation of the promoter of the myelin protein zero target gene, dimer-dependent conformational changes such as the exact bending angle introduced into the promoter appear to be less important, shedding new light on the architectural function of Sox proteins.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCOS CellsDNADNA-Binding ProteinsElectrophoretic Mobility Shift AssayHigh Mobility Group ProteinsLuciferasesMiceMolecular Sequence DataMutationOligonucleotidesPromoter Regions, GeneticProtein BindingRatsDNADNA-Binding ProteinsHigh Mobility Group ProteinsLuciferasesOligonucleotidesRecombinant Fusion ProteinsSox10 protein, mouseSox10 protein, ratSOXE Transcription FactorsTranscription Factors

Identifiers

PMID12490719
PMCPMC140074
OpenAlexW2152811319

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.