Evidence map›Paper›PMID 29063723›Full record

ArticleAngewandte Chemie (International ed. in English)2017

Revealing Conformational Variants of Solution-Phase Intrinsically Disordered Tau Protein at the Single-Molecule Level.

Lydia H Manger, Alexander K Foote, Sharla L Wood, Michael R Holden, Kevin D Heylman, Martin Margittai, Randall H Goldsmith

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Evidence of a Three-State Mechanism in DNA Hairpin Folding.Journal of the American Chemical Society · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. The structure and phase of tau: from monomer to amyloid filament.Cellular and molecular life sciences : CMLS · 2021
    Review
  12. Article
  13. Article
  14. 14-3-3/Tau Interaction and Tau Amyloidogenesis.Journal of molecular neuroscience : MN · 2019
    Review
  15. Article
  16. 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.

Lydia H MangerDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Ave., Madison, WI, 53706, USA.ORCID 0000-0001-6018-804X
Alexander K FooteDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Ave., Madison, WI, 53706, USA.
Sharla L WoodDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Ave., Madison, WI, 53706, USA.
Michael R HoldenDepartment of Chemistry & Biochemistry, University of Denver, 2190 East Iliff Ave., Denver, CO, 80208, USA.
Kevin D HeylmanDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Ave., Madison, WI, 53706, USA.
Martin MargittaiDepartment of Chemistry & Biochemistry, University of Denver, 2190 East Iliff Ave., Denver, CO, 80208, USA.ORCID 0000-0003-1903-5927
Randall H GoldsmithDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Ave., Madison, WI, 53706, USA.ORCID 0000-0001-9083-8592

Funding

ESTABLISHING AN ASSAY FOR DETECTING SINGLE TAU FIBRILSR21AG051833 · NIA · UNIVERSITY OF DENVER (COLORADO SEMINARY) · PI MARGITTAI, MARTIN · 2016 to 2017
$401k
NIA NIH HHS R21 AG051833
6 · The paper itself

Abstract

Intrinsically disordered proteins, such as tau protein, adopt a variety of conformations in solution, complicating solution-phase structural studies. We employed an anti-Brownian electrokinetic (ABEL) trap to prolong measurements of single tau proteins in solution. Once trapped, we recorded the fluorescence anisotropy to investigate the diversity of conformations sampled by the single molecules. A distribution of anisotropy values obtained from trapped tau protein is conspicuously bimodal while those obtained by trapping a globular protein or individual fluorophores are not. Time-resolved fluorescence anisotropy measurements were used to provide an explanation of the bimodal distribution as originating from a shift in the compaction of the two different families of conformations.

Indexed as

Fluorescence PolarizationIntrinsically Disordered ProteinsProtein ConformationSolutionstau ProteinsIntrinsically Disordered ProteinsSolutionstau Proteinsbiophysicsfluorescence spectroscopymicrofluidicsprotein structuressingle-molecule studies

Identifiers

PMID29063723
PMCPMC5831721

What OpenQuestion holds

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Registered trials

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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.