Evidence map›Paper›PMID 25330023›Full record

ArticleACS chemical biology2014

Super-resolution fluorescence of huntingtin reveals growth of globular species into short fibers and coexistence of distinct aggregates.

Whitney C Duim, Yan Jiang, Koning Shen, Judith Frydman, W E Moerner

Abstract read
In one paragraph

Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

31 citing papers in PubMed, 77 citations in OpenAlex.

  1. Review
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  3. Characterizing heterogeneity in amyloid formation processes.Current opinion in structural biology · 2024
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  17. Abrogation of prenucleation, transient oligomerization of the Huntingtin exon 1 protein by human profilin I.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Review
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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

5 authors at 1 institution in 1 country.

Whitney C DuimDepartment of Chemistry, ‡Department of Applied Physics, and §Department of Biology, Stanford University , Stanford, California 94305, United States.
Yan Jiang
Koning Shen
Judith Frydman
W E Moerner
Stanford University · US

Funding

Center for Protein Folding Machinery (RMI)PN2EY016525 · NEI · BAYLOR COLLEGE OF MEDICINE · PI CHIU, WAH · 2005 to 2015
$33.6M
NEI NIH HHS PN2 EY016525NEI NIH HHS PN2-EY016525
6 · The paper itself

Abstract

Polyglutamine-expanded huntingtin, the protein encoded by HTT mutations associated with Huntington's disease, forms aggregate species in vitro and in vivo. Elucidation of the mechanism of growth of fibrillar aggregates from soluble monomeric protein is critical to understanding the progression of Huntington's disease and to designing therapeutics for the disease, as well as for aggregates implicated in Alzheimer's and Parkinson's diseases. We used the technique of multicolor single-molecule, super-resolution fluorescence imaging to characterize the growth of huntingtin exon 1 aggregates. The huntingtin exon 1 aggregation followed a pathway from exclusively spherical or globular species of ∼80 nm to fibers ∼1 μm in length that increased in width, but not length, over time with the addition of more huntingtin monomers. The fibers further aggregated with one another into aggregate assemblies of increasing size. Seeds created by sonication, which were comparable in shape and size to the globular species in the pathway, were observed to grow through multidirectional elongation into fibers, suggesting a mechanism for growth of globular species into fibers. The single-molecule sensitivity of our approach made it possible to characterize the aggregation pathway across a large range of size scales, from monomers to fiber assemblies, and revealed the coexistence of different aggregate species (globular species, fibers, fiber assemblies) even at late time points.

Indexed as

Protein AggregatesEscherichia coliExonsGene ExpressionHumansHuntingtin ProteinMolecular ImagingNerve Tissue ProteinsProtein ConformationProtein MultimerizationRecombinant Fusion ProteinsSonicationSpectrometry, FluorescenceTime FactorsHTT protein, humanHuntingtin ProteinNerve Tissue ProteinsProtein AggregatesRecombinant Fusion Proteins

Identifiers

PMID25330023
PMCPMC4273975
OpenAlexW1998122246

What OpenQuestion holds

Textmetadata
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.