Evidence map›Paper›PMID 27130233›Full record

ArticleMolecular imaging and biology2016

Non-Invasive Imaging of Amyloid Deposits in a Mouse Model of AGel Using

Adriaan Verhelle, Wouter Van Overbeke, Cindy Peleman, Rebecca De Smet, Olivier Zwaenepoel, Tony Lahoutte, Jo Van Dorpe, Nick Devoogdt, Jan Gettemans

Abstract read
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In one paragraph

Article in Molecular imaging and biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-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

10 citing papers in PubMed, 16 citations in OpenAlex.

  1. A molecular perspective of gelsolin amyloidosis: An old foe with new faces.Cellular and molecular life sciences : CMLS · 2026
    Review
  2. Review
  3. Nanobodies asRSC chemical biology · 2021
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  5. Exploring cellular biochemistry with nanobodies.The Journal of biological chemistry · 2020
    Review
  6. Nanobodies as non-invasive imaging tools.Immuno-oncology technology · 2020
    Review
  7. Review
  8. Article
  9. Article
  10. 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

9 authors at 2 institutions in 1 country.

Adriaan VerhelleDepartment of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Albert Baertsoenkaai 3, B-9000, Ghent, Belgium.
Wouter Van OverbekeDepartment of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Albert Baertsoenkaai 3, B-9000, Ghent, Belgium.
Cindy PelemanIn Vivo Cellular and Molecular Imaging Laboratory, Vrije Universiteit Brussel, Brussels, Belgium.
Rebecca De SmetDepartment of Medical and Forensic Pathology, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium.
Olivier ZwaenepoelDepartment of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Albert Baertsoenkaai 3, B-9000, Ghent, Belgium.
Tony LahoutteIn Vivo Cellular and Molecular Imaging Laboratory, Vrije Universiteit Brussel, Brussels, Belgium.
Jo Van DorpeDepartment of Medical and Forensic Pathology, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium.
Nick DevoogdtIn Vivo Cellular and Molecular Imaging Laboratory, Vrije Universiteit Brussel, Brussels, Belgium.
Jan GettemansDepartment of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Albert Baertsoenkaai 3, B-9000, Ghent, Belgium. jan.gettemans@ugent.be.
Ghent University · BEVrije Universiteit Brussel · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

purposeGelsolin amyloidosis (AGel), also known as familial amyloidosis, Finnish type (FAF), is an autosomal, dominant, incurable disease caused by a point mutation (G654A/T) in the gelsolin (GSN) gene. The mutation results in loss of a Ca PROCEDURES: Three nanobodies (FAF Nb1-3) raised against the 8-kDa fragment were screened as AGel amyloid imaging agents in WT and AGel mice using

resultsAll three nanobodies possess the characteristics desired for a

conclusionThese findings demonstrate the potential of this nanobody as a non-invasive tool to image amyloidogenic gelsolin deposition and assess the therapeutic capacity of AGel therapeutics currently under development. We propose that this approach can be extended to other amyloid diseases, thereby contributing to the development of specific therapies.

Indexed as

Tomography, Emission-Computed, Single-PhotonTomography, X-Ray ComputedAmyloidAmyloidosis, FamilialAnimalsAntibody SpecificityBinding SitesDisease Models, AnimalFluorescent Antibody TechniqueGelsolinMice, Inbred C57BLMuscle, SkeletalMyocardiumSignal-To-Noise RatioSingle-Domain AntibodiesStaining and LabelingAmyloidGelsolinSingle-Domain AntibodiesTechnetiumAGelGelsolinNanobodySPECTVHH

Identifiers

PMID27130233
OpenAlexW2345231723

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.