Evidence map›Paper›PMID 27471966›Full record

ArticleCell2016

Amyloid-like Self-Assembly of a Cellular Compartment.

Elvan Boke, Martine Ruer, Martin Wühr, Margaret Coughlin, Regis Lemaitre, Steven P Gygi, Simon Alberti, David Drechsel, Anthony A Hyman, Timothy J Mitchison

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 225 papers.

0numbers the graph read from it
0cells of the map it votes in
225citing papers in PubMed
20.0field-weighted citation impact, top 1% 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

225 citing papers in PubMed, 406 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Chemical reviews · 2026
    Review
  5. Article
  6. Liquid-liquid phase separation in neural development.Cellular and molecular life sciences : CMLS · 2026
    Review
  7. Article
  8. Article
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  10. Review
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  16. Review
  17. Article
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  20. Review

165 more citing papers are in PubMed but not listed here.

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

10 authors at 3 institutions in 2 countries.

Elvan BokeDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: elvan_boke@hms.harvard.edu.
Martine RuerMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Martin WührDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Margaret CoughlinDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.
Regis LemaitreMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Steven P GygiDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Simon AlbertiMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
David DrechselMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Anthony A HymanMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Timothy J MitchisonDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.
Max Planck Institute of Molecular Cell Biology and Genetics · DECenter for Systems Biology · USHarvard University · US

Funding

MICROTUBULE DYNAMICS AND MITOTIC MECHANISMR01GM039565 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1988 to 2018
$6.2M
MICROTUBULE DYNAMICS AND MITOTIC MECHANISMR37GM039565 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1997 to 2006
$3.2M
Proteomics of Cell Signaling in Embryogenesis.R01HD091846 · NICHD · HARVARD MEDICAL SCHOOL · PI GYGI, STEVEN P, KIRSCHNER, MARC WALLACE · 2017 to 2021
$3.1M
Cell Cycle proteomicsin XenopusR01GM103785 · NIGMS · HARVARD MEDICAL SCHOOL · PI KIRSCHNER, MARC WALLACE · 2012 to 2016
$2.2M
NICHD NIH HHS R01 HD091846NIGMS NIH HHS R01 GM039565NIGMS NIH HHS R01 GM103785NIGMS NIH HHS R37 GM039565
6 · The paper itself

Abstract

Most vertebrate oocytes contain a Balbiani body, a large, non-membrane-bound compartment packed with RNA, mitochondria, and other organelles. Little is known about this compartment, though it specifies germline identity in many non-mammalian vertebrates. We show Xvelo, a disordered protein with an N-terminal prion-like domain, is an abundant constituent of Xenopus Balbiani bodies. Disruption of the prion-like domain of Xvelo, or substitution with a prion-like domain from an unrelated protein, interferes with its incorporation into Balbiani bodies in vivo. Recombinant Xvelo forms amyloid-like networks in vitro. Amyloid-like assemblies of Xvelo recruit both RNA and mitochondria in binding assays. We propose that Xenopus Balbiani bodies form by amyloid-like assembly of Xvelo, accompanied by co-recruitment of mitochondria and RNA. Prion-like domains are found in germ plasm organizing proteins in other species, suggesting that Balbiani body formation by amyloid-like assembly could be a conserved mechanism that helps oocytes function as long-lived germ cells.

Indexed as

Organelle BiogenesisAmyloidAnimalsBenzothiazolesFemaleFluorescent DyesMitochondriaOocytesOrganellesPrionsProtein DomainsProtein TransportRecombinant Fusion ProteinsRNA, MessengerSf9 CellsT-Box Domain ProteinsAmyloidBenzothiazolesFluorescent DyesPrionsRecombinant Fusion ProteinsRNA, MessengerT-Box Domain ProteinsThiazolesthioflavin Tvelo1 protein, XenopusXenopus Proteinsvelo1

Identifiers

PMID27471966
PMCPMC5082712
OpenAlexW2501424458

What OpenQuestion holds

Textmetadata
LicenceTDM
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.