Evidence map›Paper›PMID 29078357›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Revealing dynamics of helicase translocation on single-stranded DNA using high-resolution nanopore tweezers.

Jonathan M Craig, Andrew H Laszlo, Henry Brinkerhoff, Ian M Derrington, Matthew T Noakes, Ian C Nova, Benjamin I Tickman, Kenji Doering, Noah F de Leeuw, Jens H Gundlach

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Nanopore tweezers show fractional-nucleotide translocation in sequence-dependent pausing by RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Real-time label-free detection of dynamic aptamer-small molecule interactions using a nanopore nucleic acid conformational sensor.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Jonathan M CraigDepartment of Physics, University of Washington, Seattle, WA 98195 jomcraig@uw.edu.
Andrew H LaszloDepartment of Physics, University of Washington, Seattle, WA 98195.
Henry BrinkerhoffDepartment of Physics, University of Washington, Seattle, WA 98195.
Ian M DerringtonDepartment of Physics, University of Washington, Seattle, WA 98195.
Matthew T NoakesDepartment of Physics, University of Washington, Seattle, WA 98195.
Ian C NovaDepartment of Physics, University of Washington, Seattle, WA 98195.
Benjamin I TickmanDepartment of Physics, University of Washington, Seattle, WA 98195.
Kenji DoeringDepartment of Physics, University of Washington, Seattle, WA 98195.
Noah F de LeeuwDepartment of Physics, University of Washington, Seattle, WA 98195.
Jens H GundlachDepartment of Physics, University of Washington, Seattle, WA 98195.

Funding

Nanopore sequencing of DNA with MspAR01HG005115 · NHGRI · UNIVERSITY OF WASHINGTON · PI GUNDLACH, JENS, LASZLO, ANDREW · 2009 to 2024
$14.0M
NHGRI NIH HHS R01 HG005115
6 · The paper itself

Abstract

Enzymes that operate on DNA or RNA perform the core functions of replication and expression in all of biology. To gain high-resolution access to the detailed mechanistic behavior of these enzymes, we developed single-molecule picometer-resolution nanopore tweezers (SPRNT), a single-molecule technique in which the motion of polynucleotides through an enzyme is measured by a nanopore. SPRNT reveals two mechanical substates of the ATP hydrolysis cycle of the superfamily 2 helicase Hel308 during translocation on single-stranded DNA (ssDNA). By analyzing these substates at millisecond resolution, we derive a detailed kinetic model for Hel308 translocation along ssDNA that sheds light on how superfamily 1 and 2 helicases turn ATP hydrolysis into motion along DNA. Surprisingly, we find that the DNA sequence within Hel308 affects the kinetics of helicase translocation.

Indexed as

Optical TweezersAdenosine DiphosphateAdenosine TriphosphateDNA HelicasesDNA ReplicationDNA, Single-StrandedHumansKineticsSingle Molecule ImagingTranslocation, GeneticAdenosine DiphosphateAdenosine TriphosphateDNA HelicasesDNA, Single-StrandedHELQ protein, humanbiophysicshelicasesnanoporesnanotechnologysingle-molecule enzymology

Identifiers

PMID29078357
PMCPMC5692567

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.