Evidence map›Paper›PMID 38198950›Full record

ArticleStructure (London, England : 1993)2024

Engineering the ADDobody protein scaffold for generation of high-avidity ADDomer super-binders.

Dora Buzas, Huan Sun, Christine Toelzer, Sathish K N Yadav, Ufuk Borucu, Gunjan Gautam, Kapil Gupta, Joshua C Bufton, Julien Capin, Richard B Sessions and 3 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Structure (London, England : 1993), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

13 authors at 1 institution in 1 country.

Dora BuzasSchool of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, UK; Max Planck Bristol Centre for Minimal Biology, Cantock's Close, Bristol BS8 1TS, UK.
Huan SunSchool of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, UK; Max Planck Bristol Centre for Minimal Biology, Cantock's Close, Bristol BS8 1TS, UK.
Christine ToelzerSchool of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, UK.
Sathish K N YadavSchool of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, UK.
Ufuk BorucuSchool of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, UK.
Gunjan GautamSchool of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, UK.
Kapil GuptaSchool of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, UK; Imophoron Ltd, Science Creates Old Market, Midland Road, Bristol BS2 0JZ, UK.
Joshua C BuftonSchool of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, UK.
Julien CapinSchool of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, UK.
Richard B SessionsSchool of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, UK.
Frederic GarzoniImophoron Ltd, Science Creates Old Market, Midland Road, Bristol BS2 0JZ, UK.
Imre BergerSchool of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, UK; Max Planck Bristol Centre for Minimal Biology, Cantock's Close, Bristol BS8 1TS, UK; School of Chemistry, University of Bristol, Cantock's Close, Bristol BS8 1TS, UK. Electronic address: imre.berger@bristol.ac.uk.
Christiane SchaffitzelSchool of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, UK. Electronic address: cb14941@bristol.ac.uk.
University of Bristol · GB

Funding

Wellcome Trust 221708
6 · The paper itself

Abstract

Adenovirus-derived nanoparticles (ADDomer) comprise 60 copies of adenovirus penton base protein (PBP). ADDomer is thermostable, rendering the storage, transport, and deployment of ADDomer-based therapeutics independent of a cold chain. To expand the scope of ADDomers for new applications, we engineered ADDobodies, representing PBP crown domain, genetically separated from PBP multimerization domain. We inserted heterologous sequences into hyper-variable loops, resulting in monomeric, thermostable ADDobodies expressed at high yields in Escherichia coli. The X-ray structure of an ADDobody prototype validated our design. ADDobodies can be used in ribosome display experiments to select a specific binder against a target, with an enrichment factor of ∼10

Indexed as

Protein EngineeringBinding SitesADDobodyADDomer nanoparticle super-binderalternative scaffoldProtein engineeringribosome display selection

Identifiers

PMID38198950
PMCPMC7616808
OpenAlexW4390743468

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.