Evidence map›Paper›PMID 27943341›Full record

ArticleJournal of neurochemistry2017

Pittsburgh Compound-B (PiB) binds amyloid β-protein protofibrils.

Ghiam Yamin, David B Teplow

Open access · bronzeAbstract read
In one paragraph

Article in Journal of neurochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 2 pooled it
1.9field-weighted citation impact, top 14% 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

24 citing papers in PubMed, 2 syntheses or guidelines pooled it, 43 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. β-Amyloid accumulation in the human brain after one night of sleep deprivation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Trial
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. The striatum is an early, accurate indicator of amyloid burden using [Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Article
  11. Article
  12. Article
  13. An autonomic mode of brain activity.Progress in neurobiology · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Postmortem NeocorticalFrontiers in aging neuroscience · 2021
    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

2 authors at 1 institution in 1 country.

Ghiam YaminDepartment of Radiology, University of California San Diego School of Medicine, La Jolla, CA, USA.
David B TeplowDepartment of Neurology, David Geffen School of Medicine at UCLA, and Molecular Biology Institute (MBI) and Brain Research Institute (BRI), University of California, Los Angeles, CA, USA.
University of California, Los Angeles · US

Funding

STRUCTURAL/KINETIC ANALYSIS OF ABETA FIBRILLOGENESISR01NS038328 · NINDS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TEPLOW, DAVID B. · 1999 to 2014
$4.0M
Traning Clinical Scientists in Radiological ImagingT32EB005970 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Eric Y Chang, Rebecca Ann Rakow-Penner · 2007 to 2026
$3.2M
Physical Biochemistry and Biology of Amyloid Beta-ProteinR01AG041295 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TEPLOW, DAVID B. · 2011 to 2015
$1.6M
NIA NIH HHS R01 AG041295NIBIB NIH HHS T32 EB005970NINDS NIH HHS R01 NS038328
6 · The paper itself

Abstract

The neuropathology of Alzheimer's disease (AD) includes amyloid plaque formation by the amyloid β-protein (Aβ) and intracellular paired helical filament formation by tau protein. These neuropathogenetic features correlate with disease progression and have been revealed in brains of AD patients using positron emission tomography (PET). One of the most useful positron emission tomography imaging agents has been Pittsburgh Compound-B (PiB). However, since its introduction in 2002, substantial evidence has accumulated suggesting that Aβ oligomerization and protofibril formation, rather than fibril formation per se, may be the more important pathogenetic event in AD. Detecting protofibrils and oligomeric forms of Aβ thus may be of value. We report here the results of experiments to determine whether PiB binds to oligomers or protofibrils formed by Aβ40 and Aβ42. We observed strong binding to Aβ42 fibrils, significant binding to protofibrils, and weaker binding to Aβ42 oligomers. PiB also binds Aβ40 fibrils, but its binding to Aβ40 protofibrils and oligomers is substantially lower than for that observed for Aβ42.

Indexed as

Alzheimer DiseaseAmyloidAmyloid beta-PeptidesAniline CompoundsBrainDisease ProgressionHumansNeurofibrillary TanglesPositron-Emission TomographyProtein Bindingtau ProteinsThiazoles2-(4'-(methylamino)phenyl)-6-hydroxybenzothiazoleAmyloidAmyloid beta-PeptidesAniline Compoundstau ProteinsThiazolesamyloid β-protein (Aβ)oligomersPittsburgh Compound-B (PiB)positron emission tomography (PET)protofibrils

Identifiers

PMID27943341
PMCPMC5225051
OpenAlexW2547214116

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.