Evidence map›Paper›PMID 31819058›Full record

ArticleNature communications2019

Solution structure of human myeloid-derived growth factor suggests a conserved function in the endoplasmic reticulum.

Valeriu Bortnov, Marco Tonelli, Woonghee Lee, Ziqing Lin, Douglas S Annis, Omar N Demerdash, Alex Bateman, Julie C Mitchell, Ying Ge, John L Markley and 1 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 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Evidence for ~12-h ultradian gene programs in humans.Npj biological timing and sleep · 2024
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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

11 authors at 3 institutions in 2 countries.

Valeriu BortnovDepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.ORCID http://orcid.org/0000-0002-1159-7338
Marco TonelliDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Woonghee LeeDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.ORCID http://orcid.org/0000-0002-0964-203X
Ziqing LinDepartments of Cell and Regenerative Biology and Chemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.ORCID http://orcid.org/0000-0003-0464-5263
Douglas S AnnisDepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.ORCID http://orcid.org/0000-0002-4897-8759
Omar N DemerdashBiosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN, 37831, USA.
Alex BatemanEuropean Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Wellcome Genome Campus, Hinxton, CB10 1SD, UK.
Julie C MitchellBiosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN, 37831, USA.ORCID http://orcid.org/0000-0002-5031-7343
Ying GeDepartments of Cell and Regenerative Biology and Chemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.ORCID http://orcid.org/0000-0001-5211-6812
John L MarkleyDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA.
Deane F MosherDepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI, 53706, USA. dfmosher@wisc.edu.
University of Wisconsin–Madison · USOak Ridge National Laboratory · USEuropean Bioinformatics Institute · GB

Funding

Thr Role of Pin1 in AirwayP01HL088594 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI JARJOUR, NIZAR N · 2008 to 2017
$21.0M
WATER DISTRIB:PHYSICAL PROPERT:PIZZA &LMPS MOZZARELLA CHEESES:EARLY STAGE MATURP41RR002301 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 1985 to 2011
$13.0M
TR&D 3: TECHNOLOGY DEVELOPMENT FOR NMR STUDIES OF SMALL MOLECULES (METABOLOMICS, NATURAL PRODUCTS, METABOLITE-PROTEIN INTERACTIONS) pp.537-585 P41GM103399 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2012 to 2019
$9.4M
Ultra High Resolution Mass Spectrometer for Biomedical ResearchS10OD018475 · OD · UNIVERSITY OF WISCONSIN-MADISON · PI GE, YING · 2015 to 2015
$2.0M
Integrated state-of-the-art LC-MS/NMR system for the University of WisconsinS10RR025062 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2008 to 2008
$1.7M
Proteomics of eosinophil activationR01AI125390 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI COON, JOSHUA J, MOSHER, DEANE FREMONT · 2016 to 2019
$1.5M
MASH Explorer, a Comprehensive Software Environment for Top-Down ProteomicsR01GM125085 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI GE, YING · 2018 to 2021
$1.2M
Upgrade of the NMRFAM 750 MHz NMR SpectrometerS10RR029220 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2010 to 2010
$766k
NMR Spectrometer System Optimized for Direct 13C or 15N DetectionS10RR023438 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2008 to 2008
$500k
CONSOLE UPGRADES FOR NMR FACILITYS10RR008438 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI MARKLEY, JOHN L · 1993 to 1993
–
WIDE-BORE 9.4 TESLA NMR SPECTROMETER FOR UW-MADISONS10RR002781 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI MARKLEY, JOHN L · 1986 to 1986
–
NCRR NIH HHS P41 RR002301NCRR NIH HHS S10 RR002781NCRR NIH HHS S10 RR008438NCRR NIH HHS S10 RR023438NCRR NIH HHS S10 RR025062NCRR NIH HHS S10 RR029220NHLBI NIH HHS P01 HL088594NIAID NIH HHS R01 AI125390NIGMS NIH HHS P41 GM103399NIGMS NIH HHS R01 GM125085NIH HHS S10 OD018475ODCDC CDC HHS S10 OD018475
6 · The paper itself

Abstract

Human myeloid-derived growth factor (hMYDGF) is a 142-residue protein with a C-terminal endoplasmic reticulum (ER) retention sequence (ERS). Extracellular MYDGF mediates cardiac repair in mice after anoxic injury. Although homologs of hMYDGF are found in eukaryotes as distant as protozoans, its structure and function are unknown. Here we present the NMR solution structure of hMYDGF, which consists of a short α-helix and ten β-strands distributed in three β-sheets. Conserved residues map to the unstructured ERS, loops on the face opposite the ERS, and the surface of a cavity underneath the conserved loops. The only protein or portion of a protein known to have a similar fold is the base domain of VNN1. We suggest, in analogy to the tethering of the VNN1 nitrilase domain to the plasma membrane via its base domain, that MYDGF complexed to the KDEL receptor binds cargo via its conserved residues for transport to the ER.

Indexed as

Amino Acid SequenceCalciumEndoplasmic ReticulumHumansHydrogen-Ion ConcentrationInterleukinsMagnetic Resonance SpectroscopyModels, MolecularPhylogenyProtein DomainsRecombinant ProteinsStructural Homology, ProteinCalciumInterleukinsRecombinant Proteins

Identifiers

PMID31819058
PMCPMC6901522
OpenAlexW2984295782

What OpenQuestion holds

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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.