Evidence map›Paper›PMID 33983722›Full record

ArticleJournal of the American Chemical Society2021

Inclusion of the C-Terminal Domain in the β-Sheet Core of Heparin-Fibrillized Three-Repeat Tau Protein Revealed by Solid-State Nuclear Magnetic Resonance Spectroscopy.

Aurelio J Dregni, Harrison K Wang, Haifan Wu, Pu Duan, Jia Jin, William F DeGrado, Mei Hong

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Water-Mediated Phosphoryl Wires Stabilize Pathological Tau Fibrils.Angewandte Chemie (International ed. in English) · 2026
    Article
  3. Article
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  6. Article
  7. Review
  8. Article
  9. Structures of ΔD421 Truncated Tau Fibrils.Journal of molecular biology · 2025
    Article
  10. Chemical Synthesis Reveals Pathogenic Role ofJournal of the American Chemical Society · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Structures of AT8 and PHF1 phosphomimetic tau: Insights into the posttranslational modification code of tau aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Article
  20. Structure of the nonhelical filament of the Alzheimer's disease tau core.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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 at 2 institutions in 1 country.

Aurelio J DregniDepartment of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, Massachusetts 02139, United States.
Harrison K WangDepartment of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, Massachusetts 02139, United States.
Haifan WuDepartment of Pharmaceutical Chemistry, University of California, 555 Mission Bay Blvd. South, CVRB, Room 452 V, San Francisco, California 94158-9001, United States.
Pu DuanDepartment of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, Massachusetts 02139, United States.ORCID 0000-0002-7395-4353
Jia JinDepartment of Pharmaceutical Chemistry, University of California, 555 Mission Bay Blvd. South, CVRB, Room 452 V, San Francisco, California 94158-9001, United States.
William F DeGradoDepartment of Pharmaceutical Chemistry, University of California, 555 Mission Bay Blvd. South, CVRB, Room 452 V, San Francisco, California 94158-9001, United States.
Mei HongDepartment of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, Massachusetts 02139, United States.ORCID 0000-0001-5255-5858
Massachusetts Institute of Technology · USUniversity of California, San Francisco · US

Funding

VIRAL DEGENERATIVE DEMENTING DISEASE IN AGING (SUPP)P01AG002132 · NIA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI PRUSINER, STANLEY B · 1985 to 2024
$51.7M
TR&D 4 -- Advanced Magic Angle Spinning NMR methodsP41GM132079 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2019 to 2021
$3.6M
Molecular structures of tau aggregates studied by solid-state NMRRF1AG059661 · NIA · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HONG, MEI · 2018 to 2021
$2.1M
Tau structure and dynamics in Alzheimer's diseaseR01AG059661 · NIA · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI Mei Hong · 2023 to 2026
$1.8M
New RF Electronics Console and Probes for 900 Mhz NMR SpectrometerS10OD023513 · OD · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2018 to 2018
$1.0M
A 600 MHz NMR console and cryoprobe for studies of macromolecules, drug discovery and cancer biomarkersS10OD023455 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GROSS, JOHN D · 2018 to 2018
$820k
Investigation of Seeded Alzheimer's Disease Tau Fibrils with Solid-State NMRF31AG069418 · NIA · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI DREGNI, AURELIO JAMES · 2020 to 2021
$85k
NIA NIH HHS F31 AG069418NIA NIH HHS P01 AG002132NIA NIH HHS R01 AG059661NIA NIH HHS RF1 AG059661NIGMS NIH HHS P41 GM132079NIH HHS S10 OD023455NIH HHS S10 OD023513
6 · The paper itself

Abstract

Many neurodegenerative diseases such as Alzheimer's disease are characterized by pathological β-sheet filaments of the tau protein, which spread in a prion-like manner in patient brains. To date, high-resolution structures of tau filaments obtained from patient brains show that the β-sheet core only includes portions of the microtubule-binding repeat domains and excludes the C-terminal residues, indicating that the C-terminus is dynamically disordered. Here, we use solid-state NMR spectroscopy to identify the β-sheet core of full-length 0N3R tau fibrillized using heparin. Assignment of

Indexed as

Nuclear Magnetic Resonance, BiomolecularHumansProtein Conformation, beta-Strandtau Proteinstau Proteins

Identifiers

PMID33983722
PMCPMC8283780
OpenAlexW3161071856

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.