Evidence map›Paper›PMID 38953933›Full record

ArticleEuropean journal of nuclear medicine and molecular imaging2024

Efficient characterization of multiple binding sites of small molecule imaging ligands on amyloid-beta, tau and alpha-synuclein.

Jens Sobek, Junhao Li, Benjamin F Combes, Juan A Gerez, Martin T Henrich, Fanni F Geibl, Peter R Nilsson, Kuangyu Shi, Axel Rominger, Wolfgang H Oertel and 4 more

Abstract read
In one paragraph

Article in European journal of nuclear medicine and molecular imaging, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

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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

14 authors.

Jens SobekFunctional Genomics Center, University of Zurich & ETH Zurich, Zürich, Switzerland.
Junhao LiDepartment of Physics and Astronomy, Uppsala University, Uppsala, Sweden.
Benjamin F CombesInstitute for Regenerative Medicine, University of Zurich, Wagistrasse 12, 8952, Zürich, Switzerland.
Juan A GerezLaboratory of Physical Chemistry, Department of Chemistry and Applied Biosciences, ETH Zurich, Zürich, Switzerland.
Martin T HenrichDepartment of Psychiatry and Psychotherapy, Philipps-University Marburg, Marburg, Germany.
Fanni F GeiblDepartment of Psychiatry and Psychotherapy, Philipps-University Marburg, Marburg, Germany.
Peter R NilssonDivison of Chemistry, Department of Physics, Chemistry and Biology, Linköping University, Linköping, Sweden.
Kuangyu ShiDepartment of Nuclear Medicine, Inselspital, Bern University Hospital, University of Bern, Bern, Switzerland.
Axel RomingerDepartment of Nuclear Medicine, Inselspital, Bern University Hospital, University of Bern, Bern, Switzerland.
Wolfgang H OertelDepartment of Psychiatry and Psychotherapy, Philipps-University Marburg, Marburg, Germany.
Roger M NitschInstitute for Regenerative Medicine, University of Zurich, Wagistrasse 12, 8952, Zürich, Switzerland.
Agneta NordbergDivison of Clinical Geriatrics, Center for Alzheimer Research, Department of Neurobiology, Care Sciences and Society, Karolinska Institutet, Stockholm, Sweden.
Hans ÅgrenDepartment of Physics and Astronomy, Uppsala University, Uppsala, Sweden.
Ruiqing NiInstitute for Regenerative Medicine, University of Zurich, Wagistrasse 12, 8952, Zürich, Switzerland. ruiqing.ni@uzh.ch.ORCID 0000-0002-0793-2113

Funding

Swedish National Infrastructure for Computing SNIC 2022-3-34Swiss Centre for Applied Human Toxicology SCAHT-AP_22_02Vetenskapsrådet 2018-05973
6 · The paper itself

Abstract

purposeThere is an unmet need for compounds to detect fibrillar forms of alpha-synuclein (αSyn) and 4-repeat tau, which are critical in many neurodegenerative diseases. Here, we aim to develop an efficient surface plasmon resonance (SPR)-based assay to facilitate the characterization of small molecules that can bind these fibrils.

methodsSPR measurements were conducted to characterize the binding properties of fluorescent ligands/compounds toward recombinant amyloid-beta (Aβ)

resultsWe optimized the protocol for the immobilization of Aβ

conclusionSPR measurements of small molecules binding to Aβ

Indexed as

alpha-SynucleinAmyloid beta-Protein PrecursorComputer Simulationtau ProteinsAgedAnimalsBinding SitesBrainBrain ChemistryFluorescenceForensic ImagingHumansMaleMiceMice, Inbred C57BLMiddle Agedalpha-SynucleinAmyloid beta-Protein PrecursorRecombinant Proteinstau ProteinsAlpha-synucleinAmyloid-betaBinding sitesIn silicoSurface plasmon resonanceTau

Identifiers

PMID38953933
PMCPMC11527973

What OpenQuestion holds

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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.