Evidence map›Paper›PMID 29487134›Full record

ArticleThe Journal of biological chemistry2018

The N-terminal domain of a tick evasin is critical for chemokine binding and neutralization and confers specific binding activity to other evasins.

James R O Eaton, Yara Alenazi, Kamayani Singh, Graham Davies, Lucia Geis-Asteggiante, Benedikt Kessler, Carol V Robinson, Akane Kawamura, Shoumo Bhattacharya

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

20 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
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  5. Structural basis of chemokine recognition by the class A3 tick evasin EVA-ACA1001.Protein science : a publication of the Protein Society · 2024
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  12. Semisynthesis of an evasin from tick saliva reveals a critical role of tyrosine sulfation for chemokine binding and inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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  14. Review
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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

9 authors at 1 institution in 1 country.

James R O EatonFrom the Division of Cardiovascular Medicine, Radcliffe Department of Medicine.
Yara AlenaziFrom the Division of Cardiovascular Medicine, Radcliffe Department of Medicine.
Kamayani SinghFrom the Division of Cardiovascular Medicine, Radcliffe Department of Medicine.
Graham DaviesFrom the Division of Cardiovascular Medicine, Radcliffe Department of Medicine.
Lucia Geis-Asteggiantethe Department of Chemistry, and.
Benedikt Kesslerthe Nuffield Department of Medicine, University of Oxford, Oxford OX3 7BN, United Kingdom.
Carol V Robinsonthe Department of Chemistry, and.
Akane KawamuraFrom the Division of Cardiovascular Medicine, Radcliffe Department of Medicine.
Shoumo BhattacharyaFrom the Division of Cardiovascular Medicine, Radcliffe Department of Medicine, sbhattac@well.ox.ac.uk.
University of Oxford · GB

Funding

British Heart Foundation CH/09/003British Heart Foundation PG/16/100/32632British Heart Foundation RE/13/1/30181British Heart Foundation RG/10/17/28553Medical Research Council MR/N020413/1Wellcome TrustWellcome Trust 203141/Z/16/Z
6 · The paper itself

Abstract

Tick chemokine-binding proteins (evasins) are an emerging class of biologicals that target multiple chemokines and show anti-inflammatory activities in preclinical disease models. Using yeast surface display, we identified a CCL8-binding evasin, P672, from the tick

Indexed as

AnimalsArthropod ProteinsChemokinesGlycosylationHumansModels, MolecularProtein BindingProtein ConformationReceptors, ChemokineSaccharomyces cerevisiaeTandem Mass SpectrometryTicksArthropod ProteinsChemokinesReceptors, Chemokineanti-inflammatory therapychemokinechemotaxisdomain swappingevasinhomology modelinginflammationmass spectrometry (MS)protein–protein interactiontick

Identifiers

PMID29487134
PMCPMC5912465
OpenAlexW2790051262

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.