Evidence map›Paper›PMID 30217128›Full record

ArticleNucleus (Austin, Tex.)2018

Nanoparticle mediated delivery and small molecule triggered activation of proteins in the nucleus.

Hsin-Yi Chiu, Jack A Bates, Jonas Helma, Hanna Engelke, Hartmann Harz, Thomas Bein, Heinrich Leonhardt

Open access · goldAbstract read
In one paragraph

Article in Nucleus (Austin, Tex.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.1field-weighted citation impact, top 51% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

7 authors at 1 institution in 1 country.

Hsin-Yi Chiua Department of Chemistry and Center for NanoScience (CeNS) , Ludwig-Maximilians-Universität München (LMU) , Munich , Germany.ORCID 0000-0002-2922-2606
Jack A Batesb Department of Biology II and Center for NanoScience (CeNS) , Ludwig-Maximilians-Universität München (LMU) , Planegg-Martinsried , Germany.ORCID 0000-0003-2910-6485
Jonas Helmab Department of Biology II and Center for NanoScience (CeNS) , Ludwig-Maximilians-Universität München (LMU) , Planegg-Martinsried , Germany.
Hanna Engelkea Department of Chemistry and Center for NanoScience (CeNS) , Ludwig-Maximilians-Universität München (LMU) , Munich , Germany.
Hartmann Harzb Department of Biology II and Center for NanoScience (CeNS) , Ludwig-Maximilians-Universität München (LMU) , Planegg-Martinsried , Germany.ORCID 0000-0003-1218-2107
Thomas Beina Department of Chemistry and Center for NanoScience (CeNS) , Ludwig-Maximilians-Universität München (LMU) , Munich , Germany.ORCID 0000-0001-7248-5906
Heinrich Leonhardtb Department of Biology II and Center for NanoScience (CeNS) , Ludwig-Maximilians-Universität München (LMU) , Planegg-Martinsried , Germany.ORCID 0000-0002-5086-6449
Center for NanoScience · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein transfection is a versatile tool to study or manipulate cellular processes and also shows great therapeutic potential. However, the repertoire of cost effective techniques for efficient and minimally cytotoxic delivery remains limited. Mesoporous silica nanoparticles (MSNs) are multifunctional nanocarriers for cellular delivery of a wide range of molecules, they are simple and economical to synthesize and have shown great promise for protein delivery. In this work we present a general strategy to optimize the delivery of active protein to the nucleus. We generated a bimolecular Venus based optical sensor that exclusively detects active and bioavailable protein for the performance of multi-parameter optimization of protein delivery. In conjunction with cell viability tests we maximized MSN protein delivery and biocompatibility and achieved highly efficient protein transfection rates of 80%. Using the sensor to measure live-cell protein delivery kinetics, we observed heterogeneous timings within cell populations which could have a confounding effect on function studies. To address this problem we fused a split or dimerization dependent protein of interest to chemically induced dimerization (CID) components, permitting control over its activity following cellular delivery. Using the split Venus protein we directly show that addition of a small molecule dimerizer causes synchronous activation of the delivered protein across the entire cell population. This combination of cellular delivery and triggered activation provides a defined starting point for functional studies and could be applied to other protein transfection methods.

Indexed as

Drug Delivery SystemsCell NucleusHeLa CellsHumansNanoparticlesParticle SizePorosityProteinsSilicon DioxideSmall Molecule LibrariesSurface PropertiesProteinsSilicon DioxideSmall Molecule LibrariesBiomolecular complementationbiosensorcontrolled releasedrug induciblitymesoporous silica nanoparticlesnuclear proteinsprotein deliverysmall molecule controlsplit venus

Identifiers

PMID30217128
PMCPMC6244737
OpenAlexW2891432015

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.