Evidence map›Paper›PMID 28990765›Full record

ArticleJournal of the American Chemical Society2017

Self-Assembling Ability Determines the Activity of Enzyme-Instructed Self-Assembly for Inhibiting Cancer Cells.

Zhaoqianqi Feng, Huaimin Wang, Xiaoyi Chen, Bing Xu

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

55 citing papers in PubMed, 144 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Intrinsically Disordered Peptide Nanofibers from a Structured Motif Within Proteins.Angewandte Chemie (International ed. in English) · 2025
    Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Journal of the American Chemical Society · 2024
    Article
  15. Article
  16. Article
  17. Enzyme-Instructed Intracellular Peptide Assemblies.Accounts of chemical research · 2023
    Article
  18. Review
  19. Review
  20. Peptide Self-Assembled Nanocarriers for Cancer Drug Delivery.The journal of physical chemistry. B · 2023
    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

4 authors at 1 institution in 1 country.

Zhaoqianqi FengDepartment of Chemistry, Brandeis University , 415 South Street, Waltham, Massachusetts 02453, United States.
Huaimin WangDepartment of Chemistry, Brandeis University , 415 South Street, Waltham, Massachusetts 02453, United States.ORCID 0000-0002-8796-0367
Xiaoyi ChenDepartment of Chemistry, Brandeis University , 415 South Street, Waltham, Massachusetts 02453, United States.
Bing XuDepartment of Chemistry, Brandeis University , 415 South Street, Waltham, Massachusetts 02453, United States.ORCID 0000-0002-4639-387X
Brandeis University · US

Funding

Subcellular Enzyme-instructed self-assembly for molecular anticancer nanomedicinesR01CA142746 · NCI · BRANDEIS UNIVERSITY · PI Bing Xu · 2010 to 2026
$6.4M
NCI NIH HHS R01 CA142746
6 · The paper itself

Abstract

Enzyme-instructed self-assembly (EISA) represents a dynamic continuum of supramolecular nanostructures that selectively inhibits cancer cells via simultaneously targeting multiple hallmark capabilities of cancer, but how to design the small molecules for EISA from the vast molecular space remains an unanswered question. Here we show that the self-assembling ability of small molecules controls the anticancer activity of EISA. Examining the EISA precursor analogues consisting of an N-capped d-tetrapeptide, a phosphotyrosine residue, and a diester or a diamide group, we find that, regardless of the stereochemistry and the regiochemistry of their tetrapeptidic backbones, the anticancer activities of these precursors largely match their self-assembling abilities. Additional mechanistic studies confirm that the assemblies of the small peptide derivatives result in cell death, accompanying significant rearrangement of cytoskeletal proteins and plasma membranes. These results imply that the diester or diamide derivatives of the d-tetrapeptides self-assemble pericellularly, as well as intracellularly, to result in cell death. As the first case to correlate thermodynamic properties (e.g., self-assembling ability) of small molecules with the efficacy of a molecule process against cancer cells, this work provides an important insight for developing a molecular dynamic continuum for potential cancer therapy, as well as understanding the cytotoxicity of pathogenic assemblies.

Indexed as

Cell DeathCell Line, TumorCell MembraneCell SurvivalCytoskeletal ProteinsHumansMolecular Dynamics SimulationNanostructuresNeoplasmsPeptidesThermodynamicsCytoskeletal ProteinsPeptides

Identifiers

PMID28990765
PMCPMC5669277
OpenAlexW2764189746

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.