ArticleNature communications2019
Trodusquemine enhances Aβ
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In one paragraph
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
–field-weighted citation impact
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.
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.
Who cites it
81 citing papers in PubMed.
- Tunable acoustic rotation for deep biophysical phenotyping of preclinical Alzheimer's disease.Materials today. Bio · 2026Article
- Glucagon-Like Peptide-1 Receptor Agonists Inhibit the Initiation of Toxic Amyloid-β42 Aggregation.Journal of the American Chemical Society · 2026Article
- Toxic mechanisms of amyloid oligomers and therapeutic strategies.Protein science : a publication of the Protein Society · 2026Review
- Design strategies, structural insights, and biological potential of amyloid-beta inhibitors in Alzheimer's disease.Molecular diversity · 2026Review
- Ganglioside GM1 slows down Aβ(1-42) aggregation by a primary nucleation inhibitory mechanism that is modulated by sphingomyelin and cholesterol.Communications chemistry · 2025Article
- Attenuation of blood-brain barrier dysfunction by functionalized gold nanoparticles against amyloid-β peptide in an Alzheimer's disease-on-a-chip model.Materials today. Bio · 2025Article
- Role of Mitochondrial Calcium Dysregulation in Alzheimer's Disease Pathogenesis.Molecular neurobiology · 2025Review
- From Pathology to Materials Science and Engineering: Harnessing the Amyloid State for Biotechnological Applications.ACS applied materials & interfaces · 2025Review
- Nanoscale Analysis beyond Imaging by Atomic Force Microscopy: Molecular Perspectives on Oncology and Neurodegeneration.Small science · 2025Review
- Polyphenol-Mediated Peptide Assembly Modulates Melittin Toxicity: A Structure-Activity Strategy for Neutralizing the Interface Affinity of Pore-Forming Toxins to Cell Membranes.ACS applied materials & interfaces · 2025Article
- An aminosterol breaks the autocatalytic cycle of AβProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Natural aminosterols inhibit NMDA receptors with low nanomolar potency.The FEBS journal · 2025Article
- Optimization of a High-Throughput Screen for Monitoring Disease-Associated Protein Misfolding and Aggregation in Bacteria.ACS synthetic biology · 2025Article
- Lipid-induced condensate formation from the Alzheimer's Aβ peptide triggers amyloid aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Nanomaterials in targeting amyloid-β oligomers: current advances and future directions for Alzheimer's disease diagnosis and therapy.Beilstein journal of nanotechnology · 2025Review
- Anti-aging properties of the aminosterols of the dogfish shark.npj aging · 2024Review
- Modulation of Biological Membranes Using Small-Molecule Compounds to Counter Toxicity Caused by Amyloidogenic Proteins.Membranes · 2024Review
- Interactions of alpha-synuclein with membranes in Parkinson's disease: Mechanisms and therapeutic strategies.Neurobiology of disease · 2024Review
- Aggregation of the amyloid-β peptide (Aβ40) within condensates generated through liquid-liquid phase separation.Scientific reports · 2024Article
- Leveraging Machine Learning-Guided Molecular Simulations Coupled with Experimental Data to Decipher Membrane Binding Mechanisms of Aminosterols.Journal of chemical theory and computation · 2024Article
21 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
25 authors.
Ryan LimbockerCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Sean ChiaCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Francesco S RuggeriCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Michele PerniCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.ORCID http://orcid.org/0000-0001-7593-8376
Roberta CascellaDepartment of Experimental and Clinical Biomedical Science, University of Florence, Florence, 50134, Italy.
Gabriella T HellerCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Georg MeislCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.ORCID http://orcid.org/0000-0002-6562-7715
Benedetta ManniniCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.ORCID http://orcid.org/0000-0001-6812-7348
Johnny HabchiCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Thomas C T MichaelsCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Pavan K ChallaCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Minkoo AhnCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.ORCID http://orcid.org/0000-0001-9131-7334
Samuel T CasfordCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Nilumi FernandoCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Catherine K XuCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Nina D KlossCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Samuel I A CohenCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Janet R KumitaCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.ORCID http://orcid.org/0000-0002-3887-4964
Cristina CecchiDepartment of Experimental and Clinical Biomedical Science, University of Florence, Florence, 50134, Italy.
Michael ZasloffMedStar-Georgetown Transplant Institute, Georgetown University School of Medicine, Washington, DC, 20010, USA.
Sara LinseDepartment of Biochemistry and Structural Biology, Lund University, SE221 00, Lund, Sweden.ORCID http://orcid.org/0000-0001-9629-7109
Tuomas P J KnowlesCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Fabrizio ChitiDepartment of Experimental and Clinical Biomedical Science, University of Florence, Florence, 50134, Italy. fabrizio.chiti@unifi.it.ORCID http://orcid.org/0000-0002-1330-1289
Michele VendruscoloCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK. mv245@cam.ac.uk.
Christopher M DobsonCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK. cmd44@cam.ac.uk.ORCID http://orcid.org/0000-0002-3616-1610
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transient oligomeric species formed during the aggregation process of the 42-residue form of the amyloid-β peptide (Aβ
Indexed as
Alzheimer DiseaseAmyloid beta-PeptidesAnimalsCaenorhabditis elegansCell Line, TumorCholestanesDrug Evaluation, PreclinicalPeptide FragmentsSpermine3-N-1(spermine)-7, 24-dihydroxy-5-cholestane 24-sulfateAmyloid beta-Peptidesamyloid beta-protein (1-42)CholestanesPeptide FragmentsSpermine
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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.