Evidence map›Paper›PMID 30157272›Full record

ArticlePloS one2018

Single-stranded binding proteins and helicase enhance the activity of prokaryotic argonautes in vitro.

Eric A Hunt, Thomas C Evans, Nathan A Tanner

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 20% of its field
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

14 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. NgAgo possesses guided DNA nicking activity.Nucleic acids research · 2021
    Article
  9. Article
  10. ProfilingFrontiers in molecular biosciences · 2021
    Article
  11. A Hyperthermophilic Argonaute FromFrontiers in microbiology · 2021
    Article
  12. Article
  13. Article
  14. Review
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

3 authors at 1 institution in 1 country.

Eric A HuntNew England Biolabs, Inc., Ipswich, Massachusetts, United States of America.ORCID 0000-0002-6891-8294
Thomas C EvansNew England Biolabs, Inc., Ipswich, Massachusetts, United States of America.ORCID 0000-0001-5406-0146
Nathan A TannerNew England Biolabs, Inc., Ipswich, Massachusetts, United States of America.
New England Biolabs (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prokaryotic argonautes are a unique class of nucleic acid-guided endonucleases putatively involved in cellular defense against foreign genetic elements. While their eukaryotic homologs and Cas protein counterparts require single-stranded RNAs as guides, some prokaryotic argonautes are able to utilize short single-stranded DNAs as guides for sequence-specific endonuclease activity. Many complications currently prevent the use of prokaryotic argonautes for in vivo gene-editing applications; however, they do exhibit potential as a new class of in vitro molecular tools if certain challenges can be overcome, specifically the limitations on substrate accessibility which leads to unequal levels of activity across a broad palate of substrates and the inability to act on double-stranded DNA substrates. Here we demonstrate the use of accessory factors, including thermostable single-stranded DNA binding proteins and UvrD-like helicase, in conjunction with prokaryotic argonautes to significantly improve enzymatic activity and enable functionality with a broader range of substrates, including linear double-stranded DNA substrates. We also demonstrate the use of Thermus thermophilus argonaute with accessory factors as a programmable restriction enzyme to generate long, unique single-stranded overhangs from linear double-stranded substrates compatible with downstream ligation.

Indexed as

Argonaute ProteinsBacterial ProteinsDNA-Binding ProteinsDNA Breaks, Double-StrandedDNA HelicasesDNA, Single-StrandedEnzyme StabilityEscherichia coliNanoarchaeotaTemperatureThermus thermophilusArgonaute ProteinsBacterial ProteinsDNA-Binding ProteinsDNA HelicasesDNA, Single-Stranded

Identifiers

PMID30157272
PMCPMC6114923
OpenAlexW2888810076

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.