Evidence map›Paper›PMID 37241742›Full record

ArticleMolecules (Basel, Switzerland)2023

The Structural Combination of SIL and MODAG Scaffolds Fails to Enhance Binding to α-Synuclein but Reveals Promising Affinity to Amyloid β.

Adriana Di Nanni, Ran Sing Saw, Gregory D Bowden, Natasha S R Bidesi, Kaare Bjerregaard-Andersen, Špela Korat, Matthias M Herth, Bernd J Pichler, Kristina Herfert, Andreas Maurer

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. 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

10 authors at 4 institutions in 3 countries.

Adriana Di NanniWerner Siemens Imaging Center, Department of Preclinical Imaging and Radiopharmacy, Eberhard Karls University Tübingen, 72076 Tübingen, Germany.ORCID 0009-0003-6675-4331
Ran Sing SawWerner Siemens Imaging Center, Department of Preclinical Imaging and Radiopharmacy, Eberhard Karls University Tübingen, 72076 Tübingen, Germany.
Gregory D BowdenWerner Siemens Imaging Center, Department of Preclinical Imaging and Radiopharmacy, Eberhard Karls University Tübingen, 72076 Tübingen, Germany.ORCID 0000-0003-2274-6738
Natasha S R BidesiDepartment of Drug Design and Pharmacology, Faculty of Health and Medicinal Sciences, University of Copenhagen, Jagtvej 160, 2100 Copenhagen, Denmark.
Kaare Bjerregaard-AndersenDepartment of Antibody Engineering and Biochemistry, H. Lundbeck A/S, Ottiliavej 9, 2500 Copenhagen, Denmark.ORCID 0000-0003-3609-3408
Špela KoratDepartment of Radiology and Nuclear Medicine, Amsterdam UMC, Vrije Universiteit Amsterdam, De Boelelaan, 1117 Amsterdam, The Netherlands.
Matthias M HerthDepartment of Drug Design and Pharmacology, Faculty of Health and Medicinal Sciences, University of Copenhagen, Jagtvej 160, 2100 Copenhagen, Denmark.ORCID 0000-0002-7788-513X
Bernd J PichlerWerner Siemens Imaging Center, Department of Preclinical Imaging and Radiopharmacy, Eberhard Karls University Tübingen, 72076 Tübingen, Germany.ORCID 0000-0001-6784-5524
Kristina HerfertWerner Siemens Imaging Center, Department of Preclinical Imaging and Radiopharmacy, Eberhard Karls University Tübingen, 72076 Tübingen, Germany.ORCID 0000-0003-0231-7717
Andreas MaurerWerner Siemens Imaging Center, Department of Preclinical Imaging and Radiopharmacy, Eberhard Karls University Tübingen, 72076 Tübingen, Germany.ORCID 0000-0003-2412-5361
Siemens (Germany) · DEUniversity of Copenhagen · DKAmsterdam Neuroscience · NLLundbeck (Denmark) · DK

Funding

European Union 813528
6 · The paper itself

Abstract

A technique to image α-synuclein (αSYN) fibrils in vivo is an unmet scientific and clinical need that would represent a transformative tool in the understanding, diagnosis, and treatment of various neurodegenerative diseases. Several classes of compounds have shown promising results as potential PET tracers, but no candidate has yet exhibited the affinity and selectivity required to reach clinical application. We hypothesized that the application of the rational drug design technique of molecular hybridization to two promising lead scaffolds could enhance the binding to αSYN up to the fulfillment of those requirements. By combining the structures of SIL and MODAG tracers, we developed a library of diarylpyrazoles (DAPs). In vitro evaluation through competition assays against [

Indexed as

Alzheimer DiseaseAmyloid beta-Peptidesalpha-SynucleinAmyloidHumansalpha-SynucleinAmyloidAmyloid beta-Peptides3,5-diphenylpyrazoleDLBMSAPDPET tracerphenothiazinepositron emission tomographyα-synuclein

Identifiers

PMID37241742
PMCPMC10224536
OpenAlexW4378515512

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.