Evidence map›Paper›PMID 34084370›Full record

ArticleChemical science2019

Isothermal kinase-triggered supramolecular assemblies as drug sensitizers.

Dongdong Liu, Zhe Miao, Chengling Wu, Fangfei He, Peng Ren, Shuo Bai, Xingyu Jiang, Yuan Gao

Open access · diamondAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chemical science, 2019. 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
0.9field-weighted citation impact, top 30% 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, 14 citations in OpenAlex.

  1. Article
  2. Enzymatic Delivery of Magnetic Nanoparticles into Mitochondria of Live Cells.ChemNanoMat : chemistry of nanomaterials for energy, biology and more · 2021
    Article
  3. Enzymatic Noncovalent Synthesis.Chemical reviews · 2020
    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

8 authors at 2 institutions in 3 countries.

Dongdong LiuCAS Center for Excellence in Nanoscience, CAS Key Laboratory of Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology Beijing 100190 P. R. China gaoy@nanoctr.cn.
Zhe MiaoCAS Center for Excellence in Nanoscience, CAS Key Laboratory of Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology Beijing 100190 P. R. China gaoy@nanoctr.cn.
Chengling WuCAS Center for Excellence in Nanoscience, CAS Key Laboratory of Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology Beijing 100190 P. R. China gaoy@nanoctr.cn.
Fangfei HeCAS Center for Excellence in Nanoscience, CAS Key Laboratory of Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology Beijing 100190 P. R. China gaoy@nanoctr.cn.
Peng RenInstitute of Process Engineering, Chinese Academy of Sciences Beijing 100190 P. R. China.
Shuo BaiInstitute of Process Engineering, Chinese Academy of Sciences Beijing 100190 P. R. China.ORCID https://orcid.org/0000-0001-5360-3399
Xingyu JiangCAS Center for Excellence in Nanoscience, CAS Key Laboratory of Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology Beijing 100190 P. R. China gaoy@nanoctr.cn.ORCID https://orcid.org/0000-0002-5008-4703
Yuan GaoCAS Center for Excellence in Nanoscience, CAS Key Laboratory of Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology Beijing 100190 P. R. China gaoy@nanoctr.cn.ORCID https://orcid.org/0000-0001-9714-4219
Center for NanoScience · DEChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinases, the main regulators of a vast map of cellular processes, are the most attractive targets in drug discovery. Despite a few successful examples of protein kinase inhibitors, the drug discovery strategy of downregulating protein kinase activity has been quite limited and often fails even in animal models. Here, we utilize protein kinase A (PKA) activity to design PKA-triggered supramolecular assemblies with anticancer activities. Grafting a suitable peptide to PNIPAM raises the critical temperature of the LCST polymer above body temperature. Interestingly, the corresponding phosphorylated polymer has a critical temperature below body temperature, making this peptide-appended PNIPAM a suitable polymer for the PKA-triggered supramolecular assembly process. PKA-triggered assembly occurs selectively in PKA-upregulated MCF-7 cells, which disturbs the cytoskeleton and sensitizes cancer cells against doxorubicin. The chemosensitization is also observed

Identifiers

PMID34084370
PMCPMC8145944
OpenAlexW2992539316

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.