Evidence map›Paper›PMID 31167786›Full record

ArticleThe Journal of biological chemistry2019

A knottin scaffold directs the CXC-chemokine-binding specificity of tick evasins.

Angela W Lee, Maud Deruaz, Christopher Lynch, Graham Davies, Kamayani Singh, Yara Alenazi, James R O Eaton, Akane Kawamura, Jeffrey Shaw, Amanda E I Proudfoot and 2 more

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. The hypusine pathway inFrontiers in cellular and infection microbiology · 2025
    Article
  7. Structural basis of chemokine recognition by the class A3 tick evasin EVA-ACA1001.Protein science : a publication of the Protein Society · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Immunomodulatory Proteins in Tick Saliva From a Structural Perspective.Frontiers in cellular and infection microbiology · 2021
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

12 authors.

Angela W LeeRadcliffe Department of Medicine Division of Cardiovascular Medicine, University of Oxford, Oxford OX3 7BN, United Kingdom.
Maud DeruazSerono Pharmaceutical Research Institute, 1228 Geneva, Switzerland.
Christopher LynchRadcliffe Department of Medicine Division of Cardiovascular Medicine, University of Oxford, Oxford OX3 7BN, United Kingdom.ORCID 0000-0002-4534-4865
Graham DaviesRadcliffe Department of Medicine Division of Cardiovascular Medicine, University of Oxford, Oxford OX3 7BN, United Kingdom.
Kamayani SinghRadcliffe Department of Medicine Division of Cardiovascular Medicine, University of Oxford, Oxford OX3 7BN, United Kingdom.
Yara AlenaziRadcliffe Department of Medicine Division of Cardiovascular Medicine, University of Oxford, Oxford OX3 7BN, United Kingdom.
James R O EatonRadcliffe Department of Medicine Division of Cardiovascular Medicine, University of Oxford, Oxford OX3 7BN, United Kingdom.
Akane KawamuraRadcliffe Department of Medicine Division of Cardiovascular Medicine, University of Oxford, Oxford OX3 7BN, United Kingdom.
Jeffrey ShawSerono Pharmaceutical Research Institute, 1228 Geneva, Switzerland.
Amanda E I ProudfootSerono Pharmaceutical Research Institute, 1228 Geneva, Switzerland.
João M DiasSerono Pharmaceutical Research Institute, 1228 Geneva, Switzerland jmdias@pfizer.com.
Shoumo BhattacharyaRadcliffe Department of Medicine Division of Cardiovascular Medicine, University of Oxford, Oxford OX3 7BN, United Kingdom sbhattac@well.ox.ac.uk.ORCID 0000-0002-5571-0478

Funding

British Heart Foundation CH/09/003British Heart Foundation PG/16/100/32632British Heart Foundation RE/13/1/30181British Heart Foundation RG/10/17/28553British Heart Foundation RG/18/1/33351Medical Research Council MC_PC_16056Wellcome TrustWellcome Trust 203141/Z/16/Z
6 · The paper itself

Abstract

Tick evasins (EVAs) bind either CC- or CXC-chemokines by a poorly understood promiscuous or "one-to-many" mechanism to neutralize inflammation. Because EVAs potently inhibit inflammation in many preclinical models, highlighting their potential as biological therapeutics for inflammatory diseases, we sought to further unravel the CXC-chemokine-EVA interactions. Using yeast surface display, we identified and characterized 27 novel CXC-chemokine-binding evasins homologous to EVA3 and defined two functional classes. The first, which included EVA3, exclusively bound ELR

Indexed as

AnimalsChemokines, CXCCrystallography, X-RayCystine-Knot MiniproteinsProtein BindingProtein ConformationReceptors, ChemokineSpecies SpecificityTicksYeastsChemokines, CXCCystine-Knot MiniproteinsReceptors, Chemokinechemokinechemotaxiscrystal structureevasinhost-pathogen interactionimmune responseinflammationknottinprotein-protein interactiontick

Identifiers

PMID31167786
PMCPMC6643034

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Registered trials

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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.