Evidence map›Paper›PMID 25225404›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Single-molecule investigation of G-quadruplex folds of the human telomere sequence in a protein nanocavity.

Na An, Aaron M Fleming, Eric G Middleton, Cynthia J Burrows

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Folding Landscape of a Parallel G-Quadruplex.The journal of physical chemistry letters · 2019
    Article
  12. Article
  13. Dynamics of a Molecular Plug Docked onto a Solid-State Nanopore.The journal of physical chemistry letters · 2018
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Single-Molecule Studies of Telomeres and Telomerase.Annual review of biophysics · 2017
    Review
  19. Article
  20. Article
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

4 authors.

Na AnDepartment of Chemistry, University of Utah, Salt Lake City, UT 84112.
Aaron M FlemingDepartment of Chemistry, University of Utah, Salt Lake City, UT 84112.
Eric G MiddletonDepartment of Chemistry, University of Utah, Salt Lake City, UT 84112.
Cynthia J BurrowsDepartment of Chemistry, University of Utah, Salt Lake City, UT 84112 burrows@chem.utah.edu.

Funding

Nanopore Detection of DNA DamageR01GM093099 · NIGMS · UNIVERSITY OF UTAH · PI BURROWS, CYNTHIA J · 2011 to 2021
$3.0M
NIGMS NIH HHS GM093099NIGMS NIH HHS R01 GM093099
6 · The paper itself

Abstract

Human telomeric DNA consists of tandem repeats of the sequence 5'-TTAGGG-3' that can fold into various G-quadruplexes, including the hybrid, basket, and propeller folds. In this report, we demonstrate use of the α-hemolysin ion channel to analyze these subtle topological changes at a nanometer scale by providing structure-dependent electrical signatures through DNA-protein interactions. Whereas the dimensions of hybrid and basket folds allowed them to enter the protein vestibule, the propeller fold exceeds the size of the latch region, producing only brief collisions. After attaching a 25-mer poly-2'-deoxyadenosine extension to these structures, unraveling kinetics also were evaluated. Both the locations where the unfolding processes occur and the molecular shapes of the G-quadruplexes play important roles in determining their unfolding profiles. These results provide insights into the application of α-hemolysin as a molecular sieve to differentiate nanostructures as well as the potential technical hurdles DNA secondary structures may present to nanopore technology.

Indexed as

G-QuadruplexesBase SequenceDNAHemolysin ProteinsHumansKineticsModels, MolecularNanostructuresNanotechnologyNucleic Acid ConformationOligonucleotidesProtein BindingProteinsProtein Structure, TertiaryTandem Repeat SequencesTelomereDNAHemolysin ProteinsOligonucleotidesProteinssingle-molecule detectionα-hemolysin nanopore

Identifiers

PMID25225404
PMCPMC4209999

What OpenQuestion holds

Textmetadata
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.