Evidence map›Paper›PMID 28429761›Full record

ArticleScientific reports2017

A specific nanobody prevents amyloidogenesis of D76N β

Sara Raimondi, Riccardo Porcari, P Patrizia Mangione, Guglielmo Verona, Julien Marcoux, Sofia Giorgetti, Graham W Taylor, Stephan Ellmerich, Maurizio Ballico, Stefano Zanini and 16 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. 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
0.8field-weighted citation impact, top 29% 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, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Structure of Nanobody Nb23.Molecules (Basel, Switzerland) · 2021
    Article
  8. Article
  9. Exploring cellular biochemistry with nanobodies.The Journal of biological chemistry · 2020
    Review
  10. C. elegans expressing D76N βScientific reports · 2019
    Article
  11. Targeting Amyloid Aggregation: An Overview of Strategies and Mechanisms.International journal of molecular sciences · 2018
    Review
  12. 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

26 authors at 6 institutions in 3 countries.

Sara RaimondiDepartment of Molecular Medicine, Institute of Biochemistry, University of Pavia, Via Taramelli 3b, 27100 Pavia, Italy.
Riccardo PorcariWolfson Drug Discovery Unit, Centre for Amyloidosis and Acute Phase Proteins, Division of Medicine, University College London, London NW3 2PF, UK.
P Patrizia MangioneDepartment of Molecular Medicine, Institute of Biochemistry, University of Pavia, Via Taramelli 3b, 27100 Pavia, Italy.
Guglielmo VeronaWolfson Drug Discovery Unit, Centre for Amyloidosis and Acute Phase Proteins, Division of Medicine, University College London, London NW3 2PF, UK.
Julien MarcouxDepartment of Chemistry, University of Oxford, Oxford OX1 3TA, UK.
Sofia GiorgettiDepartment of Molecular Medicine, Institute of Biochemistry, University of Pavia, Via Taramelli 3b, 27100 Pavia, Italy.
Graham W TaylorWolfson Drug Discovery Unit, Centre for Amyloidosis and Acute Phase Proteins, Division of Medicine, University College London, London NW3 2PF, UK.
Stephan EllmerichWolfson Drug Discovery Unit, Centre for Amyloidosis and Acute Phase Proteins, Division of Medicine, University College London, London NW3 2PF, UK.
Maurizio BallicoScience and Math Division, New York University at Abu Dhabi, Abu Dhabi, UAE.
Stefano ZaniniScience and Math Division, New York University at Abu Dhabi, Abu Dhabi, UAE.
Els PardonStructural Biology Research Centre, VIB, Pleinlaan 2, 1050, Brussel, Belgium.
Raya Al-ShawiCentre for Biomedical Science, Division of Medicine, University College London, London NW3 2PF, UK.
J Paul SimonsWolfson Drug Discovery Unit, Centre for Amyloidosis and Acute Phase Proteins, Division of Medicine, University College London, London NW3 2PF, UK.
Alessandra CorazzaDepartment of Medical and Biological Sciences (DSMB), University of Udine, Piazzale Kolbe 4, 33100 Udine, Italy.
Federico FogolariIstituto Nazionale Biostrutture e Biosistemi, Viale Medaglie d'Oro 305, 00136 Roma, Italy.
Manuela LeriDepartment of Biomedical, Experimental and Clinical Sciences 'Mario Serio', University of Florence, Viale Morgagni 50, 50134 Florence, Italy.
Massimo StefaniDepartment of Biomedical, Experimental and Clinical Sciences 'Mario Serio', University of Florence, Viale Morgagni 50, 50134 Florence, Italy.
Monica BucciantiniDepartment of Biomedical, Experimental and Clinical Sciences 'Mario Serio', University of Florence, Viale Morgagni 50, 50134 Florence, Italy.
Julian D GillmoreNational Amyloidosis Centre, University College London, London NW3 2PF, UK.
Philip N HawkinsNational Amyloidosis Centre, University College London, London NW3 2PF, UK.
Maurizia ValliDepartment of Molecular Medicine, Institute of Biochemistry, University of Pavia, Via Taramelli 3b, 27100 Pavia, Italy.
Monica StoppiniDepartment of Molecular Medicine, Institute of Biochemistry, University of Pavia, Via Taramelli 3b, 27100 Pavia, Italy.
Carol V RobinsonDepartment of Chemistry, University of Oxford, Oxford OX1 3TA, UK.
Jan SteyaertStructural Biology Research Centre, VIB, Pleinlaan 2, 1050, Brussel, Belgium.
Gennaro EspositoScience and Math Division, New York University at Abu Dhabi, Abu Dhabi, UAE.
Vittorio BellottiDepartment of Molecular Medicine, Institute of Biochemistry, University of Pavia, Via Taramelli 3b, 27100 Pavia, Italy.
University College London · GBUniversity of Pavia · ITIstituto Nazionale Biostrutture e Biosistemi · ITUniversity of Florence · ITUniversity of Oxford · GBVrije Universiteit Brussel · BE

Funding

Medical Research Council MR/K000187/1
6 · The paper itself

Abstract

Systemic amyloidosis is caused by misfolding and aggregation of globular proteins in vivo for which effective treatments are urgently needed. Inhibition of protein self-aggregation represents an attractive therapeutic strategy. Studies on the amyloidogenic variant of β

Indexed as

AmyloidAmyloidosisAnimalsbeta 2-MicroglobulinCell Line, TumorDoxycyclineHumansMice, 129 StrainMice, KnockoutMutation, MissenseProtein AggregatesProtein Aggregation, PathologicalSingle-Domain AntibodiesTissue DistributionAmyloidbeta 2-MicroglobulinDoxycyclineProtein AggregatesSingle-Domain Antibodies

Identifiers

PMID28429761
PMCPMC5399440
OpenAlexW2606776442

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.