Evidence map›Paper›PMID 27629394›Full record

ArticleScientific reports2016

Amyloid structure exhibits polymorphism on multiple length scales in human brain tissue.

Jiliang Liu, Isabel Costantino, Nagarajan Venugopalan, Robert F Fischetti, Bradley T Hyman, Matthew P Frosch, Teresa Gomez-Isla, Lee Makowski

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
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  8. Review
  9. Time-Resolved In Situ AFM Measurement of Growth Rates of Aβ40 Fibrils.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  10. Article
  11. Article
  12. Review
  13. Article
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  15. Review
  16. Article
  17. Article
  18. Article
  19. Older, non-demented apolipoprotein εNeurobiology of aging · 2020
    Article
  20. The Structural Basis of Amyloid Strains in Alzheimer's Disease.ACS biomaterials science & engineering · 2020
    Review
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 at 3 institutions in 1 country.

Jiliang LiuDepartment of Bioengineering, Northeastern University, Boston, MA, USA.
Isabel CostantinoMassachusetts Alzheimer's Disease Research Center, Massachusetts General Hospital, Boston, MA, USA.
Nagarajan VenugopalanGM/CA@APS, Argonne National Laboratory, Illnois 60439, USA.
Robert F FischettiGM/CA@APS, Argonne National Laboratory, Illnois 60439, USA.
Bradley T HymanMassachusetts Alzheimer's Disease Research Center, Massachusetts General Hospital, Boston, MA, USA.
Matthew P FroschMassachusetts Alzheimer's Disease Research Center, Massachusetts General Hospital, Boston, MA, USA.
Teresa Gomez-IslaMassachusetts Alzheimer's Disease Research Center, Massachusetts General Hospital, Boston, MA, USA.
Lee MakowskiDepartment of Bioengineering, Northeastern University, Boston, MA, USA.
Massachusetts General Hospital · USArgonne National Laboratory · USNortheastern University · US

Funding

THE ROLE OF ADVANCED CAA IN ALZHEIMER'S DEMENTIAP50AG005134 · NIA · MASSACHUSETTS GENERAL HOSPITAL · PI HYMAN, BRADLEY T. · 1985 to 2018
$42.1M
NIA NIH HHS P50 AG005134
6 · The paper itself

Abstract

Aggregation of Aβ amyloid fibrils into plaques in the brain is a universal hallmark of Alzheimer's Disease (AD), but whether plaques in different individuals are equivalent is unknown. One possibility is that amyloid fibrils exhibit different structures and different structures may contribute differentially to disease, either within an individual brain or between individuals. However, the occurrence and distribution of structural polymorphisms of amyloid in human brain is poorly documented. Here we use X-ray microdiffraction of histological sections of human tissue to map the abundance, orientation and structural heterogeneities of amyloid. Our observations indicate that (i) tissue derived from subjects with different clinical histories may contain different ensembles of fibrillar structures; (ii) plaques harboring distinct amyloid structures can coexist within a single tissue section and (iii) within individual plaques there is a gradient of fibrillar structure from core to margins. These observations have immediate implications for existing theories on the inception and progression of AD.

Indexed as

Alzheimer DiseaseAmyloidAmyloid beta-PeptidesAmyloidosisBrainHumansPeptide FragmentsPlaque, AmyloidAmyloidAmyloid beta-PeptidesPeptide Fragments

Identifiers

PMID27629394
PMCPMC5024092
OpenAlexW2518672626

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.