Evidence map›Paper›PMID 39201549›Full record

ReviewInternational journal of molecular sciences2024

Binding to the Other Side: The AT-Hook DNA-Binding Domain Allows Nuclear Factors to Exploit the DNA Minor Groove.

Sabrina Battista, Monica Fedele, Luca Secco, Alberto Maria Davide Ingo, Riccardo Sgarra, Guidalberto Manfioletti

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Cross-species incompatibilities offer new insights into the functional consequences of satellite DNA evolution.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2026
    Review
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  9. Genome-Wide Analysis of the AT-Hook Gene Family inPlants (Basel, Switzerland) · 2025
    Article
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  11. Article
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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.

Sabrina BattistaInstitute of Experimental Endocrinology and Oncology "G. Salvatore" (IEOS), National Research Council (CNR), 80131 Naples, Italy.ORCID 0000-0001-5899-9759
Monica FedeleInstitute of Experimental Endocrinology and Oncology "G. Salvatore" (IEOS), National Research Council (CNR), 80131 Naples, Italy.ORCID 0000-0002-9171-1312
Luca SeccoDepartment of Life Sciences, University of Trieste, 34127 Trieste, Italy.ORCID 0000-0001-5268-3198
Alberto Maria Davide IngoDepartment of Life Sciences, University of Trieste, 34127 Trieste, Italy.
Riccardo SgarraDepartment of Life Sciences, University of Trieste, 34127 Trieste, Italy.
Guidalberto ManfiolettiDepartment of Life Sciences, University of Trieste, 34127 Trieste, Italy.ORCID 0000-0001-7913-2601

Funding

CNR NUTRAGENational Center for Gene Therapy and Drug based on RNA Technology CN00000041PRIN-Bando 2022 PNRR P202288PXS
6 · The paper itself

Abstract

The "AT-hook" is a peculiar DNA-binding domain that interacts with DNA in the minor groove in correspondence to AT-rich sequences. This domain has been first described in the HMGA protein family of architectural factors and later in various transcription factors and chromatin proteins, often in association with major groove DNA-binding domains. In this review, using a literature search, we identified about one hundred AT-hook-containing proteins, mainly chromatin proteins and transcription factors. After considering the prototypes of AT-hook-containing proteins, the HMGA family, we review those that have been studied in more detail and that have been involved in various pathologies with a particular focus on cancer. This review shows that the AT-hook is a domain that gives proteins not only the ability to interact with DNA but also with RNA and proteins. This domain can have enzymatic activity and can influence the activity of the major groove DNA-binding domain and chromatin docking modules when present, and its activity can be modulated by post-translational modifications. Future research on the function of AT-hook-containing proteins will allow us to better decipher their function and contribution to the different pathologies and to eventually uncover their mutual influences.

Indexed as

DNAProtein BindingAnimalsAT-Hook MotifsBinding SitesChromatinDNA-Binding ProteinsHMGA ProteinsHumansNucleic Acid ConformationProtein DomainsChromatinDNADNA-Binding ProteinsHMGA ProteinsAKNAAT-hookBRG1EBNA1HMGALEDGF/p75MeCP2MLL1PATZ1ZFAT

Identifiers

PMID39201549
PMCPMC11354804

What Socratic 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 Socratic graph.