Evidence map›Paper›PMID 21183075›Full record

ArticleCell2010

Essential role of coiled coils for aggregation and activity of Q/N-rich prions and PolyQ proteins.

Ferdinando Fiumara, Luana Fioriti, Eric R Kandel, Wayne A Hendrickson

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 147 papers.

0numbers the graph read from it
0cells of the map it votes in
147citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

147 citing papers in PubMed, 263 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Coiled-Coil Structures Mediate the Intercellular Propagation of Huntingtin.International journal of molecular sciences · 2025
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  8. Polyglutamine expansion induced dynamic misfolding of androgen receptor.Protein science : a publication of the Protein Society · 2025
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  11. WWC2 modulates GABACell reports · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Invasive mussels fashion silk-like byssus via mechanical processing of massive horizontally acquired coiled coils.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Article
  19. Article
  20. Article

87 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

4 authors at 2 institutions in 2 countries.

Ferdinando FiumaraDepartment of Neuroscience, Columbia University, New York, NY 10032, USA.
Luana Fioriti
Eric R Kandel
Wayne A Hendrickson
Columbia University · USHoward Hughes Medical Institute · US

Funding

Molecular Engineering Approach to Study Long Term Synaptic PlasticityR01NS060762 · NINDS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI JU, JINGYUE · 2008 to 2011
$2.3M
ANOMALOUS-SCATTERING STUDIES OF PROTEIN STRUCTURER01GM034102 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI HENDRICKSON, WAYNE A. · 1985 to 2008
$1.3M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM034102NINDS NIH HHS R01 NS060762
6 · The paper itself

Abstract

The functional switch of glutamine/asparagine (Q/N)-rich prions and the neurotoxicity of polyQ-expanded proteins involve complex aggregation-prone structural transitions, commonly presumed to be forming β sheets. By analyzing sequences of interaction partners of these proteins, we discovered a recurrent presence of coiled-coil domains both in the partners and in segments that flank or overlap Q/N-rich and polyQ domains. Since coiled coils can mediate protein interactions and multimerization, we studied their possible involvement in Q/N-rich and polyQ aggregations. Using circular dichroism and chemical crosslinking, we found that Q/N-rich and polyQ peptides form α-helical coiled coils in vitro and assemble into multimers. Using structure-guided mutagenesis, we found that coiled-coil domains modulate in vivo properties of two Q/N-rich prions and polyQ-expanded huntingtin. Mutations that disrupt coiled coils impair aggregation and activity, whereas mutations that enhance coiled-coil propensity promote aggregation. These findings support a coiled-coil model for the functional switch of Q/N-rich prions and for the pathogenesis of polyQ-expansion diseases.

Indexed as

Amino Acid SequenceAnimalsAplysiaCircular DichroismGlutathione PeroxidaseHuntingtin ProteinMolecular Sequence DataNerve Tissue ProteinsNuclear ProteinsPeptidesPrionsProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGlutathione PeroxidaseHTT protein, humanHuntingtin ProteinNerve Tissue ProteinsNuclear ProteinsPeptidespolyglutaminePrionsSaccharomyces cerevisiae ProteinsURE2 protein, S cerevisiae

Identifiers

PMID21183075
PMCPMC3472970
OpenAlexW1994947657

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.