Evidence map›Paper›PMID 32630615›Full record

ArticleInternational journal of molecular sciences2020

Rationally Designed Antibodies as Research Tools to Study the Structure-Toxicity Relationship of Amyloid-β Oligomers.

Ryan Limbocker, Benedetta Mannini, Rodrigo Cataldi, Shianne Chhangur, Aidan K Wright, Ryan P Kreiser, J Alex Albright, Sean Chia, Johnny Habchi, Pietro Sormanni and 6 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 20% 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

14 citing papers in PubMed, 1 synthesis or guideline pooled it, 19 citations in OpenAlex.

  1. Pooled it
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  7. Review
  8. The Toxicity of Protein Aggregates: New Insights into the Mechanisms.International journal of molecular sciences · 2023
    Article
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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

16 authors at 3 institutions in 3 countries.

Ryan LimbockerCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Benedetta ManniniCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.ORCID 0000-0001-6812-7348
Rodrigo CataldiCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.ORCID 0000-0002-3862-7824
Shianne ChhangurCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Aidan K WrightDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996, USA.
Ryan P KreiserDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996, USA.
J Alex AlbrightDepartment of Chemistry and Life Science, United States Military Academy, West Point, NY 10996, USA.
Sean ChiaCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Johnny HabchiCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Pietro SormanniCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Janet R KumitaCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.ORCID 0000-0002-3887-4964
Francesco S RuggeriCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.ORCID 0000-0002-1232-1907
Christopher M DobsonCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Fabrizio ChitiDepartment of Experimental and Clinical Biomedical Science, University of Florence, 50134 Florence, Italy.
Francesco A AprileCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.ORCID 0000-0002-5040-4420
Michele VendruscoloCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.ORCID 0000-0002-3616-1610
University of Cambridge · GBUnited States Military Academy · USUniversity of Florence · IT

Funding

Medical Research Council MR/S033947/1
6 · The paper itself

Abstract

Alzheimer's disease is associated with the aggregation of the amyloid-β peptide (Aβ), resulting in the deposition of amyloid plaques in brain tissue. Recent scrutiny of the mechanisms by which Aβ aggregates induce neuronal dysfunction has highlighted the importance of the Aβ oligomers of this protein fragment. Because of the transient and heterogeneous nature of these oligomers, however, it has been challenging to investigate the detailed mechanisms by which these species exert cytotoxicity. To address this problem, we demonstrate here the use of rationally designed single-domain antibodies (DesAbs) to characterize the structure-toxicity relationship of Aβ oligomers. For this purpose, we use Zn

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAntibodiesAntibody FormationBrainDrug DesignHumansNeuronsPeptide FragmentsPlaque, AmyloidProtein AggregatesProtein EngineeringStructure-Activity RelationshipAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAntibodiesAPP protein, humanPeptide FragmentsProtein AggregatesAlzheimer’s diseaseamyloid-βbiophysicsprotein misfolded oligomersrationally designed antibodiesresearch toolsstructure–toxicity relationship

Identifiers

PMID32630615
PMCPMC7352524
OpenAlexW3037986664

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.