Evidence map›Paper›PMID 35798951›Full record

ArticleNature chemistry2022

Structure-specific amyloid precipitation in biofluids.

M Rodrigues, P Bhattacharjee, A Brinkmalm, D T Do, C M Pearson, S De, A Ponjavic, J A Varela, K Kulenkampff, I Baudrexel and 10 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

12 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
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  3. Article
  4. Article
  5. Article
  6. Review
  7. Assembly-enhanced recognition: A biomimetic pathway to achieve ultrahigh affinities.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  12. 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

20 authors at 6 institutions in 4 countries.

M RodriguesYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0001-6364-7125
P BhattacharjeeDepartment of Psychiatry and Neurochemistry, Institute of Neuroscience and Physiology, The Sahlgrenska Academy at the University of Gothenburg, Mölndal, Sweden.ORCID 0000-0002-1116-5877
A BrinkmalmDepartment of Psychiatry and Neurochemistry, Institute of Neuroscience and Physiology, The Sahlgrenska Academy at the University of Gothenburg, Mölndal, Sweden.
D T DoDepartment of Chemistry, Indiana University, Bloomington, IN, USA.ORCID 0000-0002-5717-4285
C M PearsonDepartment of Chemistry, Indiana University, Bloomington, IN, USA.
S DeYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0003-1675-0773
A PonjavicYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0002-7561-1127
J A VarelaYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0003-1901-1378
K KulenkampffYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.
I BaudrexelYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0002-3422-8340
D EminYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.
F S RuggeriYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0002-1232-1907
J E LeeYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.
A R CarrYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.
T P J KnowlesYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0002-7879-0140
H ZetterbergDepartment of Psychiatry and Neurochemistry, Institute of Neuroscience and Physiology, The Sahlgrenska Academy at the University of Gothenburg, Mölndal, Sweden.
T N SnaddonDepartment of Chemistry, Indiana University, Bloomington, IN, USA. tsnaddon@indiana.edu.ORCID 0000-0003-1119-0332
S GandhiDepartment of Clinical and Movement Neurosciences, UCL Queen Square Institute of Neurology, London, UK. sonia.gandhi@crick.ac.uk.ORCID 0000-0003-4395-2661
S F LeeYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK. sl591@cam.ac.uk.ORCID 0000-0003-4492-5139
D KlenermanYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK. dk10012@cam.ac.uk.ORCID 0000-0001-7116-6954
University of Cambridge · GBIndiana University Bloomington · USSahlgrenska University Hospital · SEQueen Mary University of London · GBUniversity of Leeds · GBUniversity of St Andrews · GB

Funding

Asymmetric Chemical Synthesis Methods via Cooperative CatalysisR01GM121573 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI SNADDON, THOMAS NEIL · 2016 to 2020
$1.5M
Department of HealthMedical Research Council MR/T008199/1NIGMS NIH HHS R01 GM121573
6 · The paper itself

Abstract

The composition of soluble toxic protein aggregates formed in vivo is currently unknown in neurodegenerative diseases, due to their ultra-low concentration in human biofluids and their high degree of heterogeneity. Here we report a method to capture amyloid-containing aggregates in human biofluids in an unbiased way, a process we name amyloid precipitation. We use a structure-specific chemical dimer, a Y-shaped, bio-inspired small molecule with two capture groups, for amyloid precipitation to increase affinity. Our capture molecule for amyloid precipitation (CAP-1) consists of a derivative of Pittsburgh Compound B (dimer) to target the cross β-sheets of amyloids and a biotin moiety for surface immobilization. By coupling CAP-1 to magnetic beads, we demonstrate that we can target the amyloid structure of all protein aggregates present in human cerebrospinal fluid, isolate them for analysis and then characterize them using single-molecule fluorescence imaging and mass spectrometry. Amyloid precipitation enables unbiased determination of the molecular composition and structural features of the in vivo aggregates formed in neurodegenerative diseases.

Indexed as

AmyloidBodily SecretionsProtein AggregatesAmyloid beta-PeptidesHumansAmyloidAmyloid beta-PeptidesProtein Aggregates

Identifiers

PMID35798951
OpenAlexW4284702532

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.