Evidence map›Paper›PMID 23153957›Full record

ReviewTrends in biochemical sciences2012

The high mobility group box: the ultimate utility player of a cell.

Christopher S Malarkey, Mair E A Churchill

Open access · greenAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

118 citing papers in PubMed, 218 citations in OpenAlex.

  1. Review
  2. Article
  3. Cysteine thiol-to-sulfonate oxidation induces unfolding for the functional switching of the extracellular HMGB1 protein.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. International journal of ophthalmology · 2025
    Article
  11. Article
  12. Mar1, a high mobility group box protein, regulatesApplied and environmental microbiology · 2024
    Article
  13. Structure and Functions of HMGB3 Protein.International journal of molecular sciences · 2024
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Mechanisms and regulation of human mitochondrial transcription.Nature reviews. Molecular cell biology · 2024
    Review
  19. Insights intoFrontiers in plant science · 2024
    Article
  20. Article

58 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

2 authors at 1 institution in 1 country.

Christopher S MalarkeyDepartment of Pharmacology, University of Colorado Denver, School of Medicine, 12801 E. 17th Ave, Aurora, CO 80045-0511, USA.
Mair E A Churchill
University 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
NCI NIH HHS P30 CA046934NIGMS NIH HHS R01 GM079154
6 · The paper itself

Abstract

High mobility group (HMG) box proteins are abundant and ubiquitous DNA binding proteins with a remarkable array of functions throughout the cell. The structure of the HMG box DNA binding domain and general mechanisms of DNA binding and bending have been known for more than a decade. However, new mechanisms that regulate HMG box protein intracellular translocation, and by which HMG box proteins recognize DNA with and without sequence specificity, have only recently been uncovered. This review focuses primarily on the Sry-like HMG box family, HMGB1, and mitochondrial transcription factor A. For these proteins, structural and biochemical studies have shown that HMG box protein modularity, interactions with other DNA binding proteins and cellular receptors, and post-translational modifications are key regulators of their diverse functions.

Indexed as

Amino Acid SequenceAnimalsDNA-Binding ProteinsHigh Mobility Group ProteinsHumansMitochondrial ProteinsModels, MolecularMolecular Sequence DataProtein ConformationProtein Processing, Post-TranslationalSequence Homology, Amino AcidTranscription FactorsDNA-Binding ProteinsHigh Mobility Group ProteinsMitochondrial Proteinsmitochondrial transcription factor ATranscription Factors

Identifiers

PMID23153957
PMCPMC4437563
OpenAlexW2066452507

What OpenQuestion holds

Textmetadata
LicenceTDM
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.