Evidence map›Paper›PMID 33289481›Full record

ArticleeLife2020

Correlating STED and synchrotron XRF nano-imaging unveils cosegregation of metals and cytoskeleton proteins in dendrites.

Florelle Domart, Peter Cloetens, Stéphane Roudeau, Asuncion Carmona, Emeline Verdier, Daniel Choquet, Richard Ortega

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Metallothionein III Mediates CaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
  3. A primer on copper biology in the brain.Neurobiology of disease · 2025
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. 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

7 authors at 2 institutions in 1 country.

Florelle DomartChemical Imaging and Speciation, CENBG, Univ. Bordeaux, Gradignan, France.ORCID 0000-0001-5938-1731
Peter CloetensESRF, the European Synchrotron, Grenoble, France.ORCID 0000-0002-4129-9091
Stéphane RoudeauChemical Imaging and Speciation, CENBG, Univ. Bordeaux, Gradignan, France.ORCID 0000-0002-4539-9380
Asuncion CarmonaChemical Imaging and Speciation, CENBG, Univ. Bordeaux, Gradignan, France.ORCID 0000-0002-9253-4581
Emeline VerdierUniv. Bordeaux, CNRS, Interdisciplinary Institute for Neuroscience, IINS, UMR 5297, Bordeaux, France.
Daniel Choquet *Univ. Bordeaux, CNRS, Interdisciplinary Institute for Neuroscience, IINS, UMR 5297, Bordeaux, France.ORCID 0000-0003-4726-9763
Richard Ortega *Chemical Imaging and Speciation, CENBG, Univ. Bordeaux, Gradignan, France.ORCID 0000-0003-1692-5406
Centre National de la Recherche Scientifique · FREuropean Synchrotron Radiation Facility · FR

Funding

European Research Council 339541European Research Council 787340
6 · The paper itself

Abstract

Zinc and copper are involved in neuronal differentiation and synaptic plasticity but the molecular mechanisms behind these processes are still elusive due in part to the difficulty of imaging trace metals together with proteins at the synaptic level. We correlate stimulated-emission-depletion microscopy of proteins and synchrotron X-ray fluorescence imaging of trace metals, both performed with 40 nm spatial resolution, on primary rat hippocampal neurons. We reveal the co-localization at the nanoscale of zinc and tubulin in dendrites with a molecular ratio of about one zinc atom per tubulin-αβ dimer. We observe the co-segregation of copper and F-actin within the nano-architecture of dendritic protrusions. In addition, zinc chelation causes a decrease in the expression of cytoskeleton proteins in dendrites and spines. Overall, these results indicate new functions for zinc and copper in the modulation of the cytoskeleton morphology in dendrites, a mechanism associated to neuronal plasticity and memory formation.

Indexed as

AnimalsCopperCytoskeletal ProteinsDendritic SpinesMetalsMicroscopy, ConfocalMicroscopy, FluorescenceMicrotubulesNanostructuresRatsRats, Sprague-DawleySpectrometry, X-Ray EmissionSynchrotronsZincCopperCytoskeletal ProteinsMetalsZincactincopperdendriteneuroscienceratsynchrotrontubulinzinc

Identifiers

PMID33289481
PMCPMC7787660
OpenAlexW3112483470

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.