Evidence map›Paper›PMID 29925589›Full record

ArticleThe Journal of biological chemistry2018

Structural and functional analysis of Dickkopf 4 (Dkk4): New insights into Dkk evolution and regulation of Wnt signaling by Dkk and Kremen proteins.

Saleha Patel, Alice M Barkell, Deepti Gupta, Sarah L Strong, Shaun Bruton, Frederick W Muskett, Philip W Addis, Philip S Renshaw, Patrick M Slocombe, Carl Doyle and 8 more

Abstract 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 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
–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

19 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  3. Crystal structure of human Dickkopf 4 cysteine-rich domain 1 and evaluation of conformational rigidity.Acta crystallographica. Section F, Structural biology communications · 2026
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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

18 authors.

Saleha PatelLeicester Institute of Structural and Chemical Biology, Lancaster Road, Leicester LE1 7HB, United Kingdom; Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 7HB, United Kingdom.
Alice M BarkellLeicester Institute of Structural and Chemical Biology, Lancaster Road, Leicester LE1 7HB, United Kingdom; Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 7HB, United Kingdom.
Deepti GuptaUCB, 208 Bath Road, Slough SL1 3WE, United Kingdom.
Sarah L StrongLeicester Institute of Structural and Chemical Biology, Lancaster Road, Leicester LE1 7HB, United Kingdom; Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 7HB, United Kingdom.
Shaun BrutonLeicester Institute of Structural and Chemical Biology, Lancaster Road, Leicester LE1 7HB, United Kingdom; Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 7HB, United Kingdom.
Frederick W MuskettLeicester Institute of Structural and Chemical Biology, Lancaster Road, Leicester LE1 7HB, United Kingdom; Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 7HB, United Kingdom.
Philip W AddisLeicester Institute of Structural and Chemical Biology, Lancaster Road, Leicester LE1 7HB, United Kingdom; Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 7HB, United Kingdom.
Philip S RenshawLeicester Institute of Structural and Chemical Biology, Lancaster Road, Leicester LE1 7HB, United Kingdom; Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 7HB, United Kingdom.
Patrick M SlocombeUCB, 208 Bath Road, Slough SL1 3WE, United Kingdom.
Carl DoyleUCB, 208 Bath Road, Slough SL1 3WE, United Kingdom.
Alison ClargoUCB, 208 Bath Road, Slough SL1 3WE, United Kingdom.
Richard J TaylorUCB, 208 Bath Road, Slough SL1 3WE, United Kingdom.
Christine E ProsserLeicester Institute of Structural and Chemical Biology, Lancaster Road, Leicester LE1 7HB, United Kingdom; UCB, 208 Bath Road, Slough SL1 3WE, United Kingdom.
Alistair J HenryUCB, 208 Bath Road, Slough SL1 3WE, United Kingdom.
Martyn K RobinsonUCB, 208 Bath Road, Slough SL1 3WE, United Kingdom.
Lorna C WatersLeicester Institute of Structural and Chemical Biology, Lancaster Road, Leicester LE1 7HB, United Kingdom; Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 7HB, United Kingdom. Electronic address: lw83@le.ac.uk.
Gill HoldsworthUCB, 208 Bath Road, Slough SL1 3WE, United Kingdom. Electronic address: gill.holdsworth@UCB.com.
Mark D CarrLeicester Institute of Structural and Chemical Biology, Lancaster Road, Leicester LE1 7HB, United Kingdom; Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 7HB, United Kingdom. Electronic address: mdc12@le.ac.uk.

Funding

Medical Research Council MC_U117533887
6 · The paper itself

Abstract

Dickkopf (Dkk) family proteins are important regulators of Wnt signaling pathways, which play key roles in many essential biological processes. Here, we report the first detailed structural and dynamics study of a full-length mature Dkk protein (Dkk4, residues 19-224), including determination of the first atomic-resolution structure for the N-terminal cysteine-rich domain (CRD1) conserved among Dkk proteins. We discovered that CRD1 has significant structural homology to the Dkk C-terminal cysteine-rich domain (CRD2), pointing to multiple gene duplication events during Dkk family evolution. We also show that Dkk4 consists of two independent folded domains (CRD1 and CRD2) joined by a highly flexible, nonstructured linker. Similarly, the N-terminal region preceding CRD1 and containing a highly conserved N

Indexed as

Amino Acid SequenceHumansIntercellular Signaling Peptides and ProteinsLow Density Lipoprotein Receptor-Related Protein-6Membrane ProteinsProtein BindingProtein DomainsSequence AlignmentWnt Signaling PathwayDKK4 protein, humanIntercellular Signaling Peptides and ProteinsKREMEN1 protein, humanLow Density Lipoprotein Receptor-Related Protein-6LRP6 protein, humanMembrane Proteinscell surface receptorcooperativityDkk4Kremen1LRP6nuclear magnetic resonance (NMR)protein-protein interactionprotein structurestructural biologyWnt signaling

Identifiers

PMID29925589
PMCPMC6078440

What OpenQuestion holds

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LicenceCC BY
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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.