Evidence map›Paper›PMID 41605955›Full record

ArticleNature communications2026

Cycling molecular assemblies for Golgi imaging and disruption.

Weiyi Tan, Qiuxin Zhang, Zhiyu Liu, Kangqiang Qiu, Divyanshu Mahajan, Thomas Gerton, Noah Copperman, Erica C Dresselhaus, Chaoshuang Xia, Cheng Lin and 12 more

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

22 authors.

Weiyi TanDepartment of Chemistry, Brandeis University, Waltham, MA, USA.ORCID 0000-0001-5316-8278
Qiuxin ZhangDepartment of Chemistry, Brandeis University, Waltham, MA, USA.ORCID 0000-0002-8659-3569
Zhiyu LiuDepartment of Chemistry, Brandeis University, Waltham, MA, USA.
Kangqiang QiuDepartment of Cancer Biology, University of Cincinnati College of Medicine, Cincinnati, OH, USA.
Divyanshu MahajanSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Thomas GertonDepartment of Pathology, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, USA.
Noah CoppermanDepartment of Developmental & Molecular Biology and Department of Pediatrics, Albert Einstein College of Medicine, Bronx, NY, USA.
Erica C DresselhausDepartment of Biology, Brandeis University, Waltham, MA, USA.
Chaoshuang XiaDepartment of Biochemistry & Cell Biology, Center for Biomedical Mass Spectrometry, Boston University Chobanian & Avedisian School of Medicine, Boston, MA, USA.
Cheng LinDepartment of Biochemistry & Cell Biology, Center for Biomedical Mass Spectrometry, Boston University Chobanian & Avedisian School of Medicine, Boston, MA, USA.
William LauDepartment of Chemistry, Brandeis University, Waltham, MA, USA.
Mikki LeeDepartment of Chemistry, Brandeis University, Waltham, MA, USA.
Isabela Ashton-RickardtDepartment of Chemistry, Brandeis University, Waltham, MA, USA.
Pengyu HongDepartment of Computer Science, Brandeis University, Waltham, MA, USA.ORCID 0000-0002-3177-2754
Daniela DinulescuDepartment of Pathology, Brigham and Women's Hospital, Harvard Medical School, Boston, MA, USA.
Jer-Tsong HsiehDepartment of Urology, Southwestern Medical Center, University of Texas, Dallas, TX, USA.ORCID 0000-0002-1919-6010
Avital A RodalDepartment of Biology, Brandeis University, Waltham, MA, USA.ORCID 0000-0002-2051-8304
David M LoebDepartment of Developmental & Molecular Biology and Department of Pediatrics, Albert Einstein College of Medicine, Bronx, NY, USA.
Ronny DrapkinOvarian Cancer Research Center, University of Pennsylvania, Perelman School of Medicine, Philadelphia, PA, USA.ORCID 0000-0002-6912-6977
Jiajie DiaoDepartment of Cancer Biology, University of Cincinnati College of Medicine, Cincinnati, OH, USA.ORCID 0000-0003-4288-3203
Lei LuSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.ORCID 0000-0002-8192-1471
Bing XuDepartment of Chemistry, Brandeis University, Waltham, MA, USA. bxu@brandeis.edu.ORCID 0000-0002-4639-387X

Funding

Subcellular Enzyme-instructed self-assembly for molecular anticancer nanomedicinesR01CA142746 · NCI · BRANDEIS UNIVERSITY · PI Bing Xu · 2010 to 2026
$6.4M
Selectively eliminating residual human induced pluripotent stem cells (iPSCs) in cell mixtures for cell therapyR21EY036512 · NEI · BRANDEIS UNIVERSITY · PI XU, BING · 2024 to 2025
$375k
Ministry of Education - Singapore (MOE) MOE-T2EP30221-0001National Science Foundation (NSF) DMR-2011846NCI NIH HHS R01 CA142746NEI NIH HHS R21 EY036512NSF | Directorate for Mathematical & Physical Sciences | Division of Materials Research (DMR) DMR-2011846U.S. Department of Health & Human Services | NIH | National Cancer Institute (NCI) CA142746U.S. Department of Health & Human Services | NIH | National Eye Institute (NEI) EY036512U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) GM134210U.S. Department of Health & Human Services | NIH | National Institute of Neurological Disorders and Stroke (NINDS) NS103967
6 · The paper itself

Abstract

The Golgi apparatus is a central hub for protein trafficking and signaling, yet its rapid imaging and cell-selective disruption remain challenging. Here, we report cycling molecular assemblies (CyMA) for fast Golgi imaging and cell-selective interference. CyMA precursors are acetylated amphiphilic thiopeptides that traverse plasma membrane and are deacetylated by intracellular thioesterases. This exposes thiols that undergo palmitoylation by Golgi-resident palmitoyl acyltransferases utilizing palmitoyl-CoA. The resulting palmitoylated peptides self-assemble into dynamic nanostructures (i.e., CyMA) localized at the Golgi. Their continuous, reversible S-acylation enables near-instantaneous Golgi imaging. Replacing fluorophore with a biphenyl motif promotes CyMA accumulation and disrupts functions such as protein modifications, trafficking, and secretion, leading to cell death. This study establishes dynamic supramolecular assembly as an active and selective strategy for Golgi-targeting, pleiotropically interfering with Golgi functions, which may be applicable to targeting other organelles by utilizing alternative enzyme switches to enable kinetic trapping.

Indexed as

Golgi ApparatusAcylationAnimalsCell MembraneHeLa CellsHumansLipoylationPeptidesProtein TransportPeptides

Identifiers

PMID41605955
PMCPMC12954121

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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.