Evidence map›Paper›PMID 30808748›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Probing initial transient oligomerization events facilitating Huntingtin fibril nucleation at atomic resolution by relaxation-based NMR.

Samuel A Kotler, Vitali Tugarinov, Thomas Schmidt, Alberto Ceccon, David S Libich, Rodolfo Ghirlando, Charles D Schwieters, G Marius Clore

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed.

  1. Article
  2. Fold-Switching Proteins.Annual review of biophysics · 2026
    Review
  3. Review
  4. Prevention of ubiquitination at K6 and K9 in mutant huntingtin exacerbates disease pathology in a knock-in mouse model.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Modeling Protein Aggregation Kinetics from NMR Data.Journal of molecular biology · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Characterizing heterogeneity in amyloid formation processes.Current opinion in structural biology · 2024
    Review
  18. Article
  19. Article
  20. 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

8 authors.

Samuel A KotlerLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.
Vitali TugarinovLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.
Thomas SchmidtLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.
Alberto CecconLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.
David S LibichLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520.
Rodolfo GhirlandoLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0530.
Charles D SchwietersImaging Sciences Laboratory Center for Information Technology, National Institutes of Health, Bethesda, MD 20892-5624.
G Marius CloreLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520; mariusc@mail.nih.gov.

Funding

Structure and Dynamics Of Macromolecules In Solution By NMRZIADK029023 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI CLORE, GIDEON · 2009 to 2025
$41.5M
Biophysics of Macromolecular ComplexesZIADK033007 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2024
$4.9M
Misfolding and aggregation of polyglutamine sequences in neurodegenerative diseasesFI2GM117609 · NIGMS · U.S. NATIONAL INST DIABETES/DIGST/KIDNEY · PI KOTLER, SAMUEL A · 2016 to 2016
–
NIGMS NIH HHS FI2 GM117609
6 · The paper itself

Abstract

The N-terminal region of the huntingtin protein, encoded by exon-1, comprises an amphiphilic domain (htt

Indexed as

AmyloidCrystallography, X-RayCytoskeletonExonsHuntingtin ProteinHuntington DiseaseKineticsModels, MolecularNuclear Magnetic Resonance, BiomolecularPeptidesPolymersProtein DomainsProtein MultimerizationStructure-Activity RelationshipAmyloidHTT protein, humanHuntingtin ProteinPeptidespolyglutaminePolymersEPRkineticsprenucleationrelaxation-based NMRstructure

Identifiers

PMID30808748
PMCPMC6397591

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.