Evidence map›Paper›PMID 36050373›Full record

ArticleScientific reports2022

Dynamics of the secreted frizzled related protein Sizzled and potential implications for binding to bone morphogenetic protein-1 (BMP-1).

Urvashi Sharma, Sandrine Vadon-Le Goff, Karl Harlos, Yuguang Zhao, Natacha Mariano, Cecile Bijakowski, Jean-Marie Bourhis, Catherine Moali, David J S Hulmes, Nushin Aghajari

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 57% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

10 authors at 4 institutions in 2 countries.

Urvashi SharmaMolecular Microbiology and Structural Biochemistry, UMR 5086 CNRS-University of Lyon, 7 passage du Vercors, 69367, Lyon, France.
Sandrine Vadon-Le GoffTissue Biology and Therapeutic Engineering Laboratory, UMR 5305 CNRS-University of Lyon, 7 passage du Vercors, 69367, Lyon, France.
Karl HarlosDivision of Structural Biology, The Wellcome Centre for Human Genetics, University of Oxford, Oxford, OX3 7BN, UK.
Yuguang ZhaoDivision of Structural Biology, The Wellcome Centre for Human Genetics, University of Oxford, Oxford, OX3 7BN, UK.
Natacha MarianoTissue Biology and Therapeutic Engineering Laboratory, UMR 5305 CNRS-University of Lyon, 7 passage du Vercors, 69367, Lyon, France.
Cecile BijakowskiTissue Biology and Therapeutic Engineering Laboratory, UMR 5305 CNRS-University of Lyon, 7 passage du Vercors, 69367, Lyon, France.
Jean-Marie BourhisTissue Biology and Therapeutic Engineering Laboratory, UMR 5305 CNRS-University of Lyon, 7 passage du Vercors, 69367, Lyon, France.
Catherine MoaliTissue Biology and Therapeutic Engineering Laboratory, UMR 5305 CNRS-University of Lyon, 7 passage du Vercors, 69367, Lyon, France.
David J S HulmesTissue Biology and Therapeutic Engineering Laboratory, UMR 5305 CNRS-University of Lyon, 7 passage du Vercors, 69367, Lyon, France.
Nushin AghajariMolecular Microbiology and Structural Biochemistry, UMR 5086 CNRS-University of Lyon, 7 passage du Vercors, 69367, Lyon, France. nushin.aghajari@ibcp.fr.
Biologie Tissulaire et Ingénierie Thérapeutique · FRCentre National de la Recherche Scientifique · FRCentre for Human Genetics · GBUniversité Claude Bernard Lyon 1 · FR

Funding

Cancer Research UK 17721Cancer Research UK C375/A17721Medical Research Council MR/M000141/1Wellcome TrustWellcome Trust 090532/Z/09/Z
6 · The paper itself

Abstract

Sizzled (Szl) is both a secreted frizzled related protein (sFRP) and a naturally occurring inhibitor of the zinc metalloproteinase bone morphogenetic protein-1 (BMP-1), a key regulator of extracellular matrix assembly and growth factor activation. Here we present a new crystal structure for Szl which differs from that previously reported by a large scale (90°) hinge rotation between its cysteine-rich and netrin-like domains. We also present results of a molecular docking analysis showing interactions likely to be involved in the inhibition of BMP-1 activity by Szl. When compared with known structures of BMP-1 in complex with small molecule inhibitors, this reveals features that may be helpful in the design of new inhibitors to prevent the excessive accumulation of extracellular matrix that is the hallmark of fibrotic diseases.

Indexed as

Intercellular Signaling Peptides and ProteinsXenopus ProteinsBone Morphogenetic Protein 1Bone Morphogenetic Protein 2Bone Morphogenetic Protein 7Molecular Docking SimulationProtein BindingBone Morphogenetic Protein 1Bone Morphogenetic Protein 2Bone Morphogenetic Protein 7Intercellular Signaling Peptides and ProteinsXenopus Proteins

Identifiers

PMID36050373
PMCPMC9437010
OpenAlexW4294031799

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.