ArticleBiophysical journal2015
Dominant Driving Forces in Human Telomere Quadruplex Binding-Induced Structural Alterations.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- A fluorescent probe under the microscope showing dual recognition of B-DNA and G-quadruplex DNA.Communications chemistry · 2026Article
- Phen-DCAngewandte Chemie (International ed. in English) · 2022Article
- Binding-Induced Diversity of a Human Telomeric G-Quadruplex Stability Phase Space.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Major Achievements in the Design of Quadruplex-Interactive Small Molecules.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Thermodynamic Stability of G-Quadruplexes: Impact of Sequence and Environment.Chembiochem : a European journal of chemical biology · 2021Review
- G-Quadruplexes and Their Ligands: Biophysical Methods to Unravel G-Quadruplex/Ligand Interactions.Pharmaceuticals (Basel, Switzerland) · 2021Review
- PhenQE8, a Novel Ligand of the Human Telomeric Quadruplex.International journal of molecular sciences · 2021Article
- Intercalation of a Heterocyclic Ligand between Quartets in a G-Rich Tetrahelical Structure.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Folding and misfolding pathways of G-quadruplex DNA.Nucleic acids research · 2016Article
- Unraveling the Thermodynamics of the Folding and Interconversion of Human Telomere G-Quadruplexes.Angewandte Chemie (International ed. in English) · 2016Article
- Thermodynamic fingerprints of ligand binding to human telomeric G-quadruplexes.Nucleic acids research · 2015Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recently various pathways of human telomere (ht) DNA folding into G-quadruplexes and of ligand binding to these structures have been proposed. However, the key issue as to the nature of forces driving the folding and recognition processes remains unanswered. In this study, structural changes of 22-mer ht-DNA fragment (Tel22), induced by binding of ions (K(+), Na(+)) and specific bisquinolinium ligands, were monitored by calorimetric and spectroscopic methods and by gel electrophoresis. Using the global model analysis of a wide variety of experimental data, we were able to characterize the thermodynamic forces that govern the formation of stable Tel22 G-quadruplexes, folding intermediates, and ligand-quadruplex complexes, and then predict Tel22 behavior in aqueous solutions as a function of temperature, salt concentration, and ligand concentration. On the basis of the above, we believe that our work sets the framework for better understanding the heterogeneity of ht-DNA folding and binding pathways, and its structural polymorphism.
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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.