Evidence map›Paper›PMID 19226129›Full record

ArticleACS nano2009

Vault nanoparticles containing an adenovirus-derived membrane lytic protein facilitate toxin and gene transfer.

Cheng-Yu Lai, Chris M Wiethoff, Valerie A Kickhoefer, Leonard H Rome, Glen R Nemerow

Open access · greenAbstract read
In one paragraph

Article in ACS nano, 2009. 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
3.8field-weighted citation impact, top 6% 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, 46 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. International journal of molecular sciences · 2022
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Vault nanoparticles engineered with the protein transduction domain, TAT48, enhances cellular uptake.Integrative biology : quantitative biosciences from nano to macro · 2013
    Article
  11. Article
  12. Applications of viral nanoparticles in medicine.Current opinion in biotechnology · 2011
    Review
  13. Article
  14. Vaults engineered for hydrophobic drug delivery.Small (Weinheim an der Bergstrasse, Germany) · 2011
    Article
  15. Article
  16. Article
  17. 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

5 authors at 4 institutions in 1 country.

Cheng-Yu LaiDepartment of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California 92037, USA.
Chris M Wiethoff
Valerie A Kickhoefer
Leonard H Rome
Glen R Nemerow
California NanoSystems Institute · USDuPont (United States) · USLoyola University Chicago · USScripps Research Institute · US

Funding

AV INTEGRINS AND ADENOVIRUS INTERNALIZATIONR01HL054352 · NHLBI · SCRIPPS RESEARCH INSTITUTE, THE · PI NEMEROW, GLEN R · 1995 to 2016
$7.5M
ROLE OF CELL INTEGRINS IN ADENOVIRAL CONJUNCTIVITISR01EY011431 · NEI · SCRIPPS RESEARCH INSTITUTE, THE · PI NEMEROW, GLEN R · 1997 to 2012
$4.9M
Vaults as Nonviral Nucleic Acid Delivery VehiclesR01EB004553 · NIBIB · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ROME, LEONARD H · 2005 to 2008
$1.3M
NEI NIH HHS EY011431NEI NIH HHS R01 EY011431NHLBI NIH HHS HL054352NHLBI NIH HHS R01 HL054352NIBIB NIH HHS EB004553NIBIB NIH HHS R01 EB004553
6 · The paper itself

Abstract

Nonviral methods of gene delivery possess several advantages over that of viral-based vectors, including having increased safety. However, the ability to achieve effective transport of therapeutic molecules across host cell membranes via nonviral methods remains a significant goal. Cell-derived nanoparticles known as vaults have been proposed as novel candidate transfer vehicles for various foreign molecules. Recombinant vault particles enter cells via macropinocytosis or phagocytosis but lack demonstrable membrane penetrating activity. To explore the feasibility of improving vault penetration into target cells, we incorporated the membrane lytic domain of adenovirus protein VI (pVI) into the interior of recombinant vault particles via fusion to the vault poly(ADP-ribose) polymerase (VPARP) interaction domain. The membrane lytic activity of the pVI domain was retained upon incorporation into vault particles. Moreover, internalization of vault-pVI complexes into murine macrophages promoted co-delivery of a soluble ribotoxin or a cDNA plasmid encoding GFP. These findings indicate that vault particles can be modified to enhance cell transfer of selected biomolecules.

Indexed as

Gene Transfer TechniquesAdenoviridaeAnimalsBacterial ToxinsCell LineDNAHumansMiceNanoparticlesPeptide FragmentsPoly(ADP-ribose) PolymerasesProtein Structure, TertiaryVault Ribonucleoprotein ParticlesViral ProteinsBacterial ToxinsDNAglycyl-valyl-glutaminyl-seryl-leucyl-lysyl-arginyl-arginyl-arginyl-cysteinyl-phenylalaninePeptide FragmentsPoly(ADP-ribose) Polymerasesvault poly(ADP-ribose) polymeraseVault Ribonucleoprotein ParticlesViral Proteins

Identifiers

PMID19226129
PMCPMC2707358
OpenAlexW1998490724

What OpenQuestion holds

Textmetadata
LicenceTDM
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.