Evidence map›Paper›PMID 42564398›Full record

ReviewFrontiers in immunology2026

Barrier-to-Autointegration Factor 1: a key regulator of nuclear envelope integrity, genome stability, and disease progression.

Pengyu Shi, Shanpeng Wang, Zixuan Zang, Dalin Wang, Cuiyuan Yang, Jinghan Tao, Jing Liu, Jinpeng Sun, Wenzhi Shen, Rong Wang and 1 more

Abstract readReview
In one paragraph

Review in Frontiers in immunology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

11 authors.

Pengyu Shi *College of Clinical Medicine, Jining Medical University, Jining, Shandong, China.
Shanpeng Wang *College of Clinical Medicine, Jining Medical University, Jining, Shandong, China.
Zixuan ZangCollege of Stomatology, Jining Medical University, Jining, Shandong, China.
Dalin WangCollege of Clinical Medicine, Jining Medical University, Jining, Shandong, China.
Cuiyuan YangCollege of Integrative Chinese and Western Medicine, Jining Medical University, Shandong, Jining, China.
Jinghan TaoCollege of Clinical Medicine, Jining Medical University, Jining, Shandong, China.
Jing LiuCollege of Clinical Medicine, Jining Medical University, Jining, Shandong, China.
Jinpeng SunCollege of Integrative Chinese and Western Medicine, Jining Medical University, Shandong, Jining, China.
Wenzhi ShenShandong Provincial Precision Medicine Laboratory for Chronic Non-communicable Diseases, Institute of Precision Medicine, Jining Medical University, Jining, China.
Rong WangCollege of Integrative Chinese and Western Medicine, Jining Medical University, Shandong, Jining, China.
Min SunCollege of Integrative Chinese and Western Medicine, Jining Medical University, Shandong, Jining, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Barrier-to-Autointegration Factor 1 (BANF1) is a self-associating protein encoded within the q13.1 locus of chromosome 11. It is integral to multiple cellular processes, including cell cycle regulation, chromatin organization, gene expression modulation, nuclear envelope (NE) repair, DNA damage repair (DDR), innate immune function, and viral infection control. While prior investigations have provided preliminary phenotypic and bioinformatic characterizations of BANF1 across various disease states, comprehensive analyses detailing its functional roles and mechanistic underpinnings in diverse pathological contexts remain scarce. In cancer, BANF1 is frequently upregulated, with cancer cells leveraging its functions to preserve NE integrity, inhibit activation of the cyclic GMP-AMP synthase-stimulator of interferon genes (cGAS-STING) immune pathway, and facilitate epithelial-mesenchymal transition (EMT). These activities contribute to enhanced genomic stability and promote tumor cell proliferation and migration, thereby conferring oncogenic properties. In neurodegenerative diseases, BANF1 is implicated in disease pathogenesis, exemplified by its mediation of glutamate-induced oxidative stress and apoptosis in neuronal cells, as observed in Alzheimer's disease (AD). Additionally, rare mutations in BANF1 are associated with hereditary conditions: the recessive Ala12Thr (A12T) variant causes Néstor-Guillermo progeria syndrome (NGPS), whereas the dominant Gly16Arg (G16R) mutation results in dominant motor neuronopathy. This review further synthesizes recent progress in exploring BANF1 as a therapeutic target, encompassing the development of small-molecule inhibitors, immunomodulatory approaches, and its potential applications in cancer treatment. Overall, this article provides a comprehensive overview of BANF1's structural features, cellular functions, and involvement in disease initiation and progression, with particular emphasis on its expression profiles in malignancies and the therapeutic promise of BANF1-directed interventions.

Indexed as

DNA-Binding ProteinsGenomic InstabilityNuclear EnvelopeNuclear ProteinsAnimalscGAS-STING Signaling PathwayDisease ProgressionDNA RepairHumansNeoplasmsNeurodegenerative DiseasesBANF1 protein, humanDNA-Binding ProteinsNuclear ProteinsBANF1DNA bindingDNA damage repairimmune regulationmitosisnuclear envelope rupturetumorigenesis

Identifiers

PMID42564398
PMCPMC13443024

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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.