Evidence map›Paper›PMID 9451006›Full record

ArticleThe EMBO journal1998

HMG box proteins bind to four-way DNA junctions in their open conformation.

J R P-ohler, D G Norman, J Bramham, M E Bianchi, D M Lilley

Abstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Yeast HMO1: Linker Histone Reinvented.Microbiology and molecular biology reviews : MMBR · 2017
    Review
  9. Article
  10. Review
  11. Article
  12. Interaction of HMG proteins and H1 with hybrid PNA-DNA junctions.Protein science : a publication of the Protein Society · 2013
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  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

5 authors.

J R P-ohlerCRC Nucleic Acid Structure Research Group, Department of Biochemistry, The University of Dundee, Dundee DD1 4HN, UK.
D G Norman
J Bramham
M E Bianchi
D M Lilley

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The HMG box is an 80 amino acid domain found in a variety of eukaryotic chromosomal proteins and transcription factors. Binding to DNA is associated with recognition of structural distortion or manipulation of DNA structure. All the HMG box domains bind to four-way DNA junctions, which must therefore present some feature that is common to the binding targets of this wide variety of proteins. Since the four-way junction can itself adopt a variety of structures depending upon conditions, it is important to determine in which form it exists in complexes with HMG boxes. We find that a single HMG box domain is bound exclusively to the open square form of the junction and that conditions that stabilize the stacked X structure significantly lower affinity for the HMG box. We suggest that the HMG domain binds to one arm of the junction in the minor groove at the point of strand exchange and we present a model for the structure of the complex.

Indexed as

AnimalsCarrier ProteinsDNADNA-Binding ProteinsGene ExpressionHigh Mobility Group ProteinsMacromolecular SubstancesMagnesiumMaltose-Binding ProteinsMolecular ProbesNucleic Acid ConformationProtein ConformationProtein Structure, TertiaryRatsRecombinant Fusion ProteinsThymineCarrier ProteinsDNADNA-Binding ProteinsHigh Mobility Group ProteinsMacromolecular SubstancesMagnesiumMaltose-Binding ProteinsMolecular ProbesRecombinant Fusion ProteinsThymine

Identifiers

PMID9451006
PMCPMC1170430

What OpenQuestion holds

Textmetadata
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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.