Evidence map›Paper›PMID 25157102›Full record

ArticleThe Journal of biological chemistry2014

Prion-like nanofibrils of small molecules (PriSM) selectively inhibit cancer cells by impeding cytoskeleton dynamics.

Yi Kuang, Marcus J C Long, Jie Zhou, Junfeng Shi, Yuan Gao, Chen Xu, Lizbeth Hedstrom, Bing Xu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

28 citing papers in PubMed, 49 citations in OpenAlex.

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  19. Supramolecular biomaterials.Nature materials · 2016
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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 1 institution in 2 countries.

Yi KuangFrom the Department of Chemistry.
Marcus J C LongGraduate Program in Biochemistry and Biophysics.
Jie ZhouFrom the Department of Chemistry.
Junfeng ShiFrom the Department of Chemistry.
Yuan GaoFrom the Department of Chemistry.
Chen XuRosenstiel Basic Medical Sciences Research Center, and.
Lizbeth HedstromFrom the Department of Chemistry, Department of Biology, Brandeis University, Waltham, Massachusetts 02454.
Bing XuFrom the Department of Chemistry, bxu@brandeis.edu.
Brandeis University · US

Funding

Single particle reconstructionP01GM062580 · NIGMS · HARVARD MEDICAL SCHOOL · PI HARRISON, STEPHEN COPLAN · 2001 to 2016
$23.7M
Subcellular Enzyme-instructed self-assembly for molecular anticancer nanomedicinesR01CA142746 · NCI · BRANDEIS UNIVERSITY · PI Bing Xu · 2010 to 2026
$6.4M
Howard Hughes Medical InstituteNCI NIH HHS R01 CA142746NCI NIH HHS R01CA142746NIGMS NIH HHS P01 GM062580NIGMS NIH HHS P01 GM 62580
6 · The paper itself

Abstract

Emerging evidence reveals that prion-like structures play important roles to maintain the well-being of cells. Although self-assembly of small molecules also affords prion-like nanofibrils (PriSM), little is known about the functions and mechanisms of PriSM. Previous works demonstrated that PriSM formed by a dipeptide derivative selectively inhibiting the growth of glioblastoma cells over neuronal cells and effectively inhibiting xenograft tumor in animal models. Here we examine the protein targets, the internalization, and the cytotoxicity pathway of the PriSM. The results show that the PriSM selectively accumulate in cancer cells via macropinocytosis to impede the dynamics of cytoskeletal filaments via promiscuous interactions with cytoskeletal proteins, thus inducing apoptosis. Intriguingly, Tau proteins are able to alleviate the effect of the PriSM, thus protecting neuronal cells. This work illustrates PriSM as a new paradigm for developing polypharmacological agents that promiscuously interact with multiple proteins yet result in a primary phenotype, such as cancer inhibition.

Indexed as

Antineoplastic AgentsApoptosisCytoskeletonEndocytosisGlioblastomaHeLa CellsHep G2 CellsHumansMCF-7 CellsNanoparticlesNanotechnologyNeoplasmsNeoplasm TransplantationNocodazolePaclitaxelPeptidesAntineoplastic AgentsNocodazolePaclitaxelPeptidesPrionstau ProteinsTubulinAggregationAnticancer DrugApoptosisCancerNanotechnology

Identifiers

PMID25157102
PMCPMC4200273
OpenAlexW2018970532

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.