Evidence map›Paper›PMID 25161284›Full record

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

Viral nanoparticle-encapsidated enzyme and restructured DNA for cell delivery and gene expression.

Jinny L Liu, Aparna Banerjee Dixit, Kelly L Robertson, Eric Qiao, Lindsay W Black

Open access · bronzeAbstract 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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
5.0field-weighted citation impact, top 5% 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

17 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Basics for Improved Use of Phages for Therapy.Antibiotics (Basel, Switzerland) · 2021
    Article
  9. Light: A Magical Tool for Controlled Drug Delivery.Advanced functional materials · 2020
    Article
  10. Article
  11. Review
  12. Multi-Enzyme Assembly on T4 Phage Scaffold.Frontiers in bioengineering and biotechnology · 2020
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. 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

5 authors at 4 institutions in 1 country.

Jinny L LiuCenter for Bio/Molecular Science and Engineering, US Naval Research Laboratory, Washington, DC 20375; jinny.liu@nrl.navy.mil lblack@umaryland.edu.
Aparna Banerjee DixitDepartment of Biochemistry, School of Medicine, University of Maryland at Baltimore, Baltimore, MD 21201;
Kelly L RobertsonEngility Corporation, Alexandria, VA 22314; and.
Eric QiaoScience and Engineering Apprenticeship Program, US Naval Research Laboratory, Washington, DC 20375.
Lindsay W BlackDepartment of Biochemistry, School of Medicine, University of Maryland at Baltimore, Baltimore, MD 21201; jinny.liu@nrl.navy.mil lblack@umaryland.edu.
University of Maryland, Baltimore · USEngility (United States) · USNaval Research Laboratory Center for Bio/Molecular Science and EngineeringUnited States Naval Research Laboratory · US

Funding

Phase T4 Head Assembly and Initiation of InfectionR01AI011676 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI BLACK, LINDSAY W · 1985 to 2013
$4.1M
NIAID NIH HHS R01 AI011676
6 · The paper itself

Abstract

Packaging specific exogenous active proteins and DNAs together within a single viral-nanocontainer is challenging. The bacteriophage T4 capsid (100 × 70 nm) is well suited for this purpose, because it can hold a single long DNA or multiple short pieces of DNA up to 170 kb packed together with more than 1,000 protein molecules. Any linear DNA can be packaged in vitro into purified procapsids. The capsid-targeting sequence (CTS) directs virtually any protein into the procapsid. Procapsids are assembled with specific CTS-directed exogenous proteins that are encapsidated before the DNA. The capsid also can display on its surface high-affinity eukaryotic cell-binding peptides or proteins that are in fusion with small outer capsid and head outer capsid surface-decoration proteins that can be added in vivo or in vitro. In this study, we demonstrate that the site-specific recombinase cyclic recombination (Cre) targeted into the procapsid is enzymatically active within the procapsid and recircularizes linear plasmid DNA containing two terminal loxP recognition sites when packaged in vitro. mCherry expression driven by a cytomegalovirus promoter in the capsid containing Cre-circularized DNA is enhanced over linear DNA, as shown in recipient eukaryotic cells. The efficient and specific packaging into capsids and the unpackaging of both DNA and protein with release of the enzymatically altered protein-DNA complexes from the nanoparticles into cells have potential in numerous downstream drug and gene therapeutic applications.

Indexed as

Gene ExpressionGene Transfer TechniquesAttachment Sites, MicrobiologicalBacteriophage T4Base SequenceCapsidCell DeathCell Line, TumorCell SurvivalDNADNA, CircularDNA PackagingFlow CytometryFluorescenceHumansIntegrasesCre recombinaseDNADNA, CircularIntegrasescapsid decoration proteinsDNA packagingHocSocterminase

Identifiers

PMID25161284
PMCPMC4169922
OpenAlexW2100431738

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.