ArticleNucleic acids research2019
Insights into telomeric G-quadruplex DNA recognition by HMGB1 protein.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 64 citations in OpenAlex.
- HMGB1 promotes intracranial aneurysm progression by regulating vascular smooth muscle cell phenotypic switching and ferroptosis.Journal of molecular histology · 2026Article
- Promoting the nuclear retention of HMGB1 attenuates astrocyte senescence.Journal of neuroinflammation · 2026Article
- Revealing G4 Structures as Drug Targets: Exploring the Potential of Novel Therapeutic Agents.Research (Washington, D.C.) · 2026Review
- HMGB1 downregulates DDX3 to activate the MAPK pathway, promoting the progression of colorectal cancer.Cancer gene therapy · 2025Article
- Effects of hydrazone-based G-quadruplex ligands onNAR cancer · 2025Article
- Identifying G-quadruplex-interacting proteins in cancer-related gene promoters.Communications chemistry · 2025Article
- Expanding the Functions of KHSRP Protein: Insights into DNA G-Quadruplex Binding.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- The Ambiguous Role of HMGB1 Across the Hallmarks of Aging: A Narrative Review.Clinical interventions in aging · 2025Review
- Profiling of i-motif-binding proteins reveals functional roles of nucleolin in regulation of high-order DNA structures.Nucleic acids research · 2024Article
- An i-motif-regulated enhancer, eRNA and adjacent lncRNA affect Lhb expression through distinct mechanisms in a sex-specific context.Cellular and molecular life sciences : CMLS · 2024Article
- Phosphorylation by Protein Kinase C Weakens DNA-Binding Affinity and Folding Stability of the HMGB1 Protein.Biochemistry · 2024Article
- Unlocking the potential of protein-derived peptides to target G-quadruplex DNA: from recognition to anticancer activity.Nucleic acids research · 2024Article
- Structural Motifs at the Telomeres and Their Role in Regulatory Pathways.Biochemistry · 2024Review
- Investigating HMGB1 as a potential serum biomarker for early diabetic nephropathy monitoring by quantitative proteomics.iScience · 2024Article
- High-mobility group box 1 emerges as a therapeutic target for asthma.Immunity, inflammation and disease · 2023Review
- Tumor-associated neutrophils upregulate PANoptosis to foster an immunosuppressive microenvironment of non-small cell lung cancer.Cancer immunology, immunotherapy : CII · 2023Article
- Telomere and subtelomere high polymorphism might contribute to the specificity of homologous recognition and pairing during meiosis in barley in the context of breeding.BMC genomics · 2023Article
- Exploring the G-quadruplex binding and unwinding activity of the bacterial FeS helicase DinG.Scientific reports · 2023Article
- Negatively charged, intrinsically disordered regions can accelerate target search by DNA-binding proteins.Nucleic acids research · 2023Article
- The telomeric protein TERF2/TRF2 impairs HMGB1-driven autophagy.Autophagy · 2023Article
Corrections and comments
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Authors and funding
14 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HMGB1 is a ubiquitous non-histone protein, which biological effects depend on its expression and subcellular location. Inside the nucleus, HMGB1 is engaged in many DNA events such as DNA repair, transcription and telomere maintenance. HMGB1 has been reported to bind preferentially to bent DNA as well as to noncanonical DNA structures like 4-way junctions and, more recently, to G-quadruplexes. These are four-stranded conformations of nucleic acids involved in important cellular processes, including telomere maintenance. In this frame, G-quadruplex recognition by specific proteins represents a key event to modulate physiological or pathological pathways. Herein, to get insights into the telomeric G-quadruplex DNA recognition by HMGB1, we performed detailed biophysical studies complemented with biological analyses. The obtained results provided information about the molecular determinants for the interaction and showed that the structural variability of human telomeric G-quadruplex DNA may have significant implications in HMGB1 recognition. The biological data identified HMGB1 as a telomere-associated protein in both telomerase-positive and -negative tumor cells and showed that HMGB1 gene silencing in such cells induces telomere DNA damage foci. Altogether, these findings provide a deeper understanding of telomeric G-quadruplex recognition by HMGB1 and suggest that this protein could actually represent a new target for cancer therapy.
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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.