Evidence map›Paper›PMID 30401748›Full record

ArticleThe Journal of biological chemistry2019

Live-cell super-resolution microscopy reveals a primary role for diffusion in polyglutamine-driven aggresome assembly.

Meng Lu, Luca Banetta, Laurence J Young, Edward J Smith, Gillian P Bates, Alessio Zaccone, Gabriele S Kaminski Schierle, Alan Tunnacliffe, Clemens F Kaminski

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Super-Resolution Vibrational Imaging Using Expansion Stimulated Raman Scattering Microscopy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Lipid headgroups alter huntingtin aggregation on membranes.Biochimica et biophysica acta. Biomembranes · 2021
    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

9 authors.

Meng LuCambridge Infinitus Research Center, Department of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, United Kingdom.
Luca BanettaDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, United Kingdom.
Laurence J YoungCambridge Infinitus Research Center, Department of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, United Kingdom.
Edward J SmithSobell Department of Motor Neuroscience and Movement Disorders and Huntington's Disease Center, Institute of Neurology, University College London, London WC1N 3BG, United Kingdom.
Gillian P BatesSobell Department of Motor Neuroscience and Movement Disorders and Huntington's Disease Center, Institute of Neurology, University College London, London WC1N 3BG, United Kingdom.
Alessio ZacconeDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, United Kingdom.
Gabriele S Kaminski SchierleCambridge Infinitus Research Center, Department of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, United Kingdom.
Alan TunnacliffeCambridge Infinitus Research Center, Department of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, United Kingdom.
Clemens F KaminskiCambridge Infinitus Research Center, Department of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, United Kingdom. Electronic address: cfk23@cam.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/H023917/1Medical Research Council G0902243Medical Research Council MR/K015850/1Medical Research Council MR/K02292X/1Wellcome Trust 089703/Z/09/ZWellcome Trust 203249/Z/16/ZWellcome Trust 3-3249/Z/16/Z
6 · The paper itself

Abstract

The mechanisms leading to self-assembly of misfolded proteins into amyloid aggregates have been studied extensively in the test tube under well-controlled conditions. However, to what extent these processes are representative of those in the cellular environment remains unclear. Using super-resolution imaging of live cells, we show here that an amyloidogenic polyglutamine-containing protein first forms small, amorphous aggregate clusters in the cytosol, chiefly by diffusion. Dynamic interactions among these clusters limited their elongation and led to structures with a branched morphology, differing from the predominantly linear fibrils observed

Indexed as

Models, BiologicalAnimalsCell NucleusFemaleMaleMiceMicroscopy, FluorescenceMicrotubule-Organizing CenterPeptidesPeptidespolyglutamineaggresome formationamyloid proteinlive cell SIMmolecular dynamicsmolecular imagingmolecular modelingpassive transportprotein aggregationprotein misfoldingtransport

Identifiers

PMID30401748
PMCPMC6322900

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.