Evidence map›Paper›PMID 22742450›Full record

ArticleThe Biochemical journal2012

Human YKL-39 is a pseudo-chitinase with retained chitooligosaccharide-binding properties.

Marianne Schimpl, Christina L Rush, Marie Betou, Ian M Eggleston, Anneliese D Recklies, Daan M F van Aalten

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

36 citing papers in PubMed, 63 citations in OpenAlex.

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  20. Chitins and chitinase activity in airway diseases.The Journal of allergy and clinical immunology · 2018
    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

6 authors at 1 institution in 1 country.

Marianne SchimplDivision of Molecular Microbiology, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK.
Christina L Rush
Marie Betou
Ian M Eggleston
Anneliese D Recklies
Daan M F van Aalten
McGill University · CA

Funding

Medical Research Council G0900138Medical Research Council G0900138(90614)Wellcome Trust 087590
6 · The paper itself

Abstract

The chitinase-like proteins YKL-39 (chitinase 3-like-2) and YKL-40 (chitinase 3-like-1) are highly expressed in a number of human cells independent of their origin (mesenchymal, epithelial or haemapoietic). Elevated serum levels of YKL-40 have been associated with a negative outcome in a number of diseases ranging from cancer to inflammation and asthma. YKL-39 expression has been associated with osteoarthritis. However, despite the reported association with disease, the physiological or pathological role of these proteins is still very poorly understood. Although YKL-39 is homologous to the two family 18 chitinases in the human genome, it has been reported to lack any chitinase activity. In the present study, we show that human YKL-39 possesses a chitinase-like fold, but lacks key active-site residues required for catalysis. A glycan screen identified oligomers of N-acetylglucosamine as preferred binding partners. YKL-39 binds chitooligosaccharides and a newly synthesized derivative of the bisdionin chitinase-inhibitor class with micromolar affinity, through a number of conserved tryptophan residues. Strikingly, the chitinase activity of YKL-39 was recovered by reverting two non-conservative substitutions in the active site to those found in the active enzymes, suggesting that YKL-39 is a pseudo-chitinase with retention of chitinase-like ligand-binding properties.

Indexed as

AcetylglucosamineAdipokinesAmino Acid SubstitutionCatalytic DomainChitinChitinase-3-Like Protein 1ChitinasesCrystallography, X-RayEnzyme InhibitorsHumansLectinsOligosaccharidesPoint MutationProtein ConformationProtein FoldingTryptophanAcetylglucosamineAdipokinesCHI3L1 protein, humanChitinChitinase-3-Like Protein 1ChitinasesEnzyme InhibitorsLectinsOligosaccharidesTryptophan

Identifiers

PMID22742450
PMCPMC3513709
OpenAlexW2170032191

What OpenQuestion holds

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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.