Evidence map›Paper›PMID 26143914›Full record

ArticleActa crystallographica. Section D, Biological crystallography2015

Two high-mobility group box domains act together to underwind and kink DNA.

R Sánchez-Giraldo, F J Acosta-Reyes, C S Malarkey, N Saperas, M E A Churchill, J L Campos

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

30 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Role of Calmodulin in Neurodegeneration and Neuroprotection.Mini reviews in medicinal chemistry · 2025
    Review
  7. Article
  8. Structure and Functions of HMGB3 Protein.International journal of molecular sciences · 2024
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  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

6 authors at 2 institutions in 2 countries.

R Sánchez-GiraldoDepartament d'Enginyeria Quimica, Universitat Politecnica de Catalunya, 08028 Barcelona, Spain.
F J Acosta-ReyesDepartament d'Enginyeria Quimica, Universitat Politecnica de Catalunya, 08028 Barcelona, Spain.
C S MalarkeyDepartment of Pharmacology and the Program in Structural Biology and Biochemistry, University of Colorado School of Medicine, Aurora, CO 80045, USA.
N SaperasDepartament d'Enginyeria Quimica, Universitat Politecnica de Catalunya, 08028 Barcelona, Spain.
M E A ChurchillDepartment of Pharmacology and the Program in Structural Biology and Biochemistry, University of Colorado School of Medicine, Aurora, CO 80045, USA.
J L CamposDepartament d'Enginyeria Quimica, Universitat Politecnica de Catalunya, 08028 Barcelona, Spain.
Universitat Politècnica de Catalunya · ESUniversity of Colorado Denver · US

Funding

University of Colorado Cancer Center Support Grant - Lung Cancer Patient-Derived Xenografts with Autologous Human Immune SystemsP30CA046934 · NCI · UNIVERSITY OF COLORADO DENVER · PI James V Degregori · 1988 to 2026
$117.0M
Molecular Mechanism of Histone H3/H4 Chaperone FunctionR01GM079154 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI CHURCHILL, MAIR E · 2007 to 2010
$1.3M
Structural and Functional Studies of the Histone Chaperone CAF-1R01GM111902 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI CHURCHILL, MAIR E · 2014 to 2017
$1.2M
NCI NIH HHS P30 CA046934NCI NIH HHS P30CA046934NIGMS NIH HHS R01 GM079154NIGMS NIH HHS R01 GM111902
6 · The paper itself

Abstract

High-mobility group protein 1 (HMGB1) is an essential and ubiquitous DNA architectural factor that influences a myriad of cellular processes. HMGB1 contains two DNA-binding domains, box A and box B, which have little sequence specificity but have remarkable abilities to underwind and bend DNA. Although HMGB1 box A is thought to be responsible for the majority of HMGB1-DNA interactions with pre-bent or kinked DNA, little is known about how it recognizes unmodified DNA. Here, the crystal structure of HMGB1 box A bound to an AT-rich DNA fragment is reported at a resolution of 2 Å. Two box A domains of HMGB1 collaborate in an unusual configuration in which the Phe37 residues of both domains stack together and intercalate the same CG base pair, generating highly kinked DNA. This represents a novel mode of DNA recognition for HMGB proteins and reveals a mechanism by which structure-specific HMG boxes kink linear DNA.

Indexed as

HMG-Box DomainsAmino Acid SequenceAnimalsCrystallography, X-RayDNAHMGB1 ProteinModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein ConformationRatsSequence AlignmentDNAHMGB1 Proteinkinked DNADNA bindinghigh-mobility group proteinHMGB1X-ray crystallography

Identifiers

PMID26143914
PMCPMC4498601
OpenAlexW2137435257

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.