Evidence map›Paper›PMID 29430303›Full record

ArticleMolecular systems design & engineering2017

Modulating the Catalytic Activity of Enzyme-like Nanoparticles Through their Surface Functionalization.

Roberto Cao-Milán, Luke D He, Spencer Shorkey, Gulen Y Tonga, Li-Sheng Wang, Xianzhi Zhang, Imad Uddin, Riddha Das, Mine Sulak, Vincent M Rotello

Abstract read
In one paragraph

Article in Molecular systems design & engineering, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Exploring New Bioorthogonal Catalysts: Scaffold Diversity in Catalysis for Chemical Biology.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  5. Article
  6. Modular Fabrication of Bioorthogonal Nanozymes for Biomedical Applications.Advanced materials (Deerfield Beach, Fla.) · 2024
    Review
  7. Article
  8. Bioorthogonal nanozymes for breast cancer imaging and therapy.Journal of controlled release : official journal of the Controlled Release Society · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Inside a Shell-Organometallic Catalysis Inside Encapsulin Nanoreactors.Angewandte Chemie (International ed. in English) · 2021
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. 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

10 authors.

Roberto Cao-MilánDepartment of Chemistry, University of Massachusetts Amherst, 710 North Pleasant Street, Amherst, Massachusetts 01003, USA.
Luke D HeDepartment of Chemistry, University of Massachusetts Amherst, 710 North Pleasant Street, Amherst, Massachusetts 01003, USA.
Spencer ShorkeyDepartment of Chemistry, University of Massachusetts Amherst, 710 North Pleasant Street, Amherst, Massachusetts 01003, USA.
Gulen Y TongaDepartment of Chemistry, University of Massachusetts Amherst, 710 North Pleasant Street, Amherst, Massachusetts 01003, USA.
Li-Sheng WangDepartment of Chemistry, University of Massachusetts Amherst, 710 North Pleasant Street, Amherst, Massachusetts 01003, USA.
Xianzhi ZhangDepartment of Chemistry, University of Massachusetts Amherst, 710 North Pleasant Street, Amherst, Massachusetts 01003, USA.
Imad UddinDepartment of Chemistry, Hazara University, Mansehra 21120, Pakistan.
Riddha DasDepartment of Chemistry, University of Massachusetts Amherst, 710 North Pleasant Street, Amherst, Massachusetts 01003, USA.
Mine SulakSchool of Applied Science, Pamukkale University, 20600, Çivril, Denizli, Turkey.
Vincent M RotelloDepartment of Chemistry, University of Massachusetts Amherst, 710 North Pleasant Street, Amherst, Massachusetts 01003, USA.

Funding

Targeting of Bio-orthogonal Chemotherapeutic Nanozymes to Tumor-Associated MacrophagesR01EB022641 · NIBIB · UNIVERSITY OF MASSACHUSETTS AMHERST · PI ROTELLO, VINCENT M. · 2017 to 2024
$3.0M
NIBIB NIH HHS R01 EB022641
6 · The paper itself

Abstract

The inclusion of transition metal catalysts into nanoparticle scaffolds permits the creation of catalytic nanosystems (nanozymes) able to imitate the behaviour of natural enzymes. Here we report the fabrication of a family of nanozymes comprised of bioorthogonal ruthenium catalysts inserted in the protective monolayer of gold nanoparticles. By introducing simple modifications to the functional groups at the surface of the nanozymes, we have demonstrated control over the kinetic mechanism of our system. Cationic nanozymes with hydrophobic surface functionalities tend to replicate the classical Michaelis Menten model, while those with polar groups display substrate inhibition behaviour, a key mechanism present in 20 % of natural enzymes. The structural parameters described herein can be used for creating artificial nanosystems that mimic the complexity observed in cell machinery.

Identifiers

PMID29430303
PMCPMC5805145

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.