Evidence map›Paper›PMID 31772377›Full record

ArticleNature communications2019

Crystal structure and receptor-interacting residues of MYDGF - a protein mediating ischemic tissue repair.

Rebecca Ebenhoch, Abbas Akhdar, Marc R Reboll, Mortimer Korf-Klingebiel, Priyanka Gupta, Julie Armstrong, Yining Huang, Lee Frego, Irina Rybina, John Miglietta and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 30 citations in OpenAlex.

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  10. A Self-Sustaining Antioxidant Strategy for Effective Treatment of Myocardial Infarction.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
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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

13 authors at 3 institutions in 2 countries.

Rebecca EbenhochBoehringer Ingelheim Pharma GmbH & Co. KG, Birkendorfer Str. 65, 88397, Biberach an der Riss, Germany.ORCID http://orcid.org/0000-0003-4304-7434
Abbas AkhdarDivision of Molecular and Translational Cardiology, Department of Cardiology and Angiology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625, Hannover, Germany.
Marc R RebollDivision of Molecular and Translational Cardiology, Department of Cardiology and Angiology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625, Hannover, Germany.
Mortimer Korf-KlingebielDivision of Molecular and Translational Cardiology, Department of Cardiology and Angiology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625, Hannover, Germany.
Priyanka GuptaBoehringer Ingelheim Pharmaceuticals, Inc., 900 Ridgebury Road, Ridgefield, CT, 06877, USA.ORCID http://orcid.org/0000-0001-6483-3069
Julie ArmstrongBoehringer Ingelheim Pharmaceuticals, Inc., 900 Ridgebury Road, Ridgefield, CT, 06877, USA.
Yining HuangBoehringer Ingelheim Pharmaceuticals, Inc., 900 Ridgebury Road, Ridgefield, CT, 06877, USA.
Lee FregoBoehringer Ingelheim Pharmaceuticals, Inc., 900 Ridgebury Road, Ridgefield, CT, 06877, USA.
Irina RybinaBoehringer Ingelheim Pharmaceuticals, Inc., 900 Ridgebury Road, Ridgefield, CT, 06877, USA.
John MigliettaBoehringer Ingelheim Pharmaceuticals, Inc., 900 Ridgebury Road, Ridgefield, CT, 06877, USA.
Anton PekcecBoehringer Ingelheim Pharma GmbH & Co. KG, Birkendorfer Str. 65, 88397, Biberach an der Riss, Germany.
Kai C WollertDivision of Molecular and Translational Cardiology, Department of Cardiology and Angiology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625, Hannover, Germany.
Herbert NarBoehringer Ingelheim Pharma GmbH & Co. KG, Birkendorfer Str. 65, 88397, Biberach an der Riss, Germany. herbert.nar@boehringer-ingelheim.com.
Boehringer Ingelheim (United States) · USMedizinische Hochschule Hannover · DEBoehringer Ingelheim (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myeloid-derived growth factor (MYDGF) is a paracrine-acting protein that is produced by bone marrow-derived monocytes and macrophages to protect and repair the heart after myocardial infarction (MI). This effect can be used for the development of protein-based therapies for ischemic tissue repair, also beyond the sole application in heart tissue. Here, we report the X-ray structure of MYDGF and identify its functionally relevant receptor binding epitope. MYDGF consists of a 10-stranded β-sandwich with a folding topology showing no similarities to other cytokines or growth factors. By characterizing the epitope of a neutralizing antibody and utilizing functional assays to study the activity of surface patch-mutations, we were able to localize the receptor interaction interface to a region around two surface tyrosine residues 71 and 73 and an adjacent prominent loop structure of residues 97-101. These findings enable structure-guided protein engineering to develop modified MYDGF variants with potentially improved properties for clinical use.

Indexed as

Antibodies, NeutralizingCells, CulturedCoronary VesselsCrystallography, X-RayEpitopesHumansInterleukinsModels, MolecularMutationMyocardial InfarctionProtein ConformationProtein FoldingSequence Homology, Amino AcidTyrosineAntibodies, NeutralizingEpitopesInterleukinsMYDGF protein, humanTyrosine

Identifiers

PMID31772377
PMCPMC6879528
OpenAlexW2990024865

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.