Evidence map›Paper›PMID 28654419›Full record

ArticleeLife2017

Affimer proteins are versatile and renewable affinity reagents.

Christian Tiede, Robert Bedford, Sophie J Heseltine, Gina Smith, Imeshi Wijetunga, Rebecca Ross, Danah AlQallaf, Ashley Pe Roberts, Alexander Balls, Alistair Curd and 36 more

Abstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing 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

87 citing papers in PubMed.

  1. Article
  2. Review
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  7. The Molecular Toolbox for Linkage Type-Specific Analysis of Ubiquitin Signaling.Chembiochem : a European journal of chemical biology · 2025
    Review
  8. Article
  9. Review
  10. Review
  11. Self-assembled proteomimetic (SAP) with antibody-like binding from short PNA-peptide conjugates.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

27 more citing papers are in PubMed but not listed here.

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

46 authors.

Christian TiedeSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
Robert BedfordSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
Sophie J HeseltineSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
Gina SmithSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
Imeshi WijetungaLeeds Institute of Cancer Studies and Pathology, University of Leeds, Leeds, United Kingdom.
Rebecca RossLeeds Institute of Cancer Studies and Pathology, University of Leeds, Leeds, United Kingdom.
Danah AlQallafSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
Ashley Pe RobertsThe Pirbright Institute, Woking, United Kingdom.
Alexander BallsSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
Alistair CurdSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
Ruth E HughesSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
Heather MartinSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
Sarah R NeedhamCentral Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Didcot, United Kingdom.
Laura C Zanetti-DominguesCentral Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Didcot, United Kingdom.
Yashar SadighThe Pirbright Institute, Woking, United Kingdom.
Thomas P PeacockThe Pirbright Institute, Woking, United Kingdom.
Anna A TangSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.ORCID http://orcid.org/0000-0002-5216-5080
Naomi GibsonSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
Hannah KyleAvacta Life Sciences, Wetherby, United Kingdom.
Geoffrey W PlattAvacta Life Sciences, Wetherby, United Kingdom.
Nicola IngramLeeds Institute of Cancer Studies and Pathology, University of Leeds, Leeds, United Kingdom.ORCID http://orcid.org/0000-0001-5274-8502
Thomas TaylorSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
Louise P ColettaLeeds Institute of Cancer Studies and Pathology, University of Leeds, Leeds, United Kingdom.
Iain ManfieldSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
Margaret KnowlesLeeds Institute of Cancer Studies and Pathology, University of Leeds, Leeds, United Kingdom.
Sandra BellLeeds Institute of Biomedical and Clinical Sciences, University of Leeds, Leeds, United Kingdom.
Filomena EstevesLeeds Institute of Cancer Studies and Pathology, University of Leeds, Leeds, United Kingdom.
Azhar MaqboolLeeds Institute of Cardiovascular and Metabolic Medicine, University of Leeds, Leeds, United Kingdom.
Raj K PrasadLeeds Institute of Cardiovascular and Metabolic Medicine, University of Leeds, Leeds, United Kingdom.
Mark DrinkhillLeeds Institute of Cardiovascular and Metabolic Medicine, University of Leeds, Leeds, United Kingdom.
Robin S BonLeeds Institute of Cardiovascular and Metabolic Medicine, University of Leeds, Leeds, United Kingdom.
Vikesh PatelDSTL Porton Down, Salisbury, United Kingdom.
Sarah A GoodchildDSTL Porton Down, Salisbury, United Kingdom.
Marisa Martin-FernandezCentral Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Didcot, United Kingdom.
Ray J OwensOxford Protein Production Facility UK, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Didcot, United Kingdom.
Joanne E NettleshipOxford Protein Production Facility UK, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Didcot, United Kingdom.
Michael E WebbSchool of Chemistry, University of Leeds, Leeds, United Kingdom.
Michael HarrisonSchool of Biomedical Sciences, University of Leeds, Leeds, United Kingdom.
Jonathan D LippiatSchool of Biomedical Sciences, University of Leeds, Leeds, United Kingdom.
Sreenivasan PonnambalamSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.ORCID http://orcid.org/0000-0002-4452-7619
Michelle PeckhamSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.ORCID http://orcid.org/0000-0002-3754-2028
Alastair SmithAvacta Life Sciences, Wetherby, United Kingdom.
Paul Ko FerrignoAvacta Life Sciences, Wetherby, United Kingdom.
Matt JohnsonAvacta Life Sciences, Wetherby, United Kingdom.
Michael J McPhersonSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.ORCID http://orcid.org/0000-0002-0719-6427
Darren Charles TomlinsonSchool of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.ORCID http://orcid.org/0000-0003-4134-7484

Funding

British Heart Foundation FS/12/20/29462British Heart Foundation FS/16/24/32133British Heart Foundation FS/17/30/32832British Heart Foundation NH/12/1/29382Medical Research Council MC_EX_MR/K015591/1Medical Research Council MR/K015613/1Medical Research Council MR/K018779/1Wellcome Trust
6 · The paper itself

Abstract

Molecular recognition reagents are key tools for understanding biological processes and are used universally by scientists to study protein expression, localisation and interactions. Antibodies remain the most widely used of such reagents and many show excellent performance, although some are poorly characterised or have stability or batch variability issues, supporting the use of alternative binding proteins as complementary reagents for many applications. Here we report on the use of Affimer proteins as research reagents. We selected 12 diverse molecular targets for Affimer selection to exemplify their use in common molecular and cellular applications including the (a) selection against various target molecules; (b) modulation of protein function in vitro and in vivo; (c) labelling of tumour antigens in mouse models; and (d) use in affinity fluorescence and super-resolution microscopy. This work shows that Affimer proteins, as is the case for other alternative binding scaffolds, represent complementary affinity reagents to antibodies for various molecular and cell biology applications.

Indexed as

AnimalsCarrier ProteinsMiceMolecular BiologyStaining and LabelingCarrier ProteinsAffimerantibodyassaybiochemistrycell biologyE. colihumanmouse

Identifiers

PMID28654419
PMCPMC5487212

What OpenQuestion holds

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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.