Evidence map›Paper›PMID 31327662›Full record

ArticleStructure (London, England : 1993)2019

Structural Adaptation in Its Orphan Domain Engenders Betaglycan with an Alternate Mode of Growth Factor Binding Relative to Endoglin.

Sun Kyung Kim, Matthew J Whitley, Troy C Krzysiak, Cynthia S Hinck, Alexander B Taylor, Christian Zwieb, Chang-Hyeock Byeon, Xiaohong Zhou, Valentín Mendoza, Fernando López-Casillas and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
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  4. Synthesis ofOrganic & biomolecular chemistry · 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

12 authors at 3 institutions in 2 countries.

Sun Kyung KimDepartment of Structural Biology, University of Pittsburgh School of Medicine, Biomedical Science Tower 3, Room 2051, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA; Department of Biochemistry and Structural Biology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229-3900, USA.
Matthew J WhitleyDepartment of Structural Biology, University of Pittsburgh School of Medicine, Biomedical Science Tower 3, Room 2051, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA; Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.
Troy C KrzysiakDepartment of Structural Biology, University of Pittsburgh School of Medicine, Biomedical Science Tower 3, Room 2051, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA.
Cynthia S HinckDepartment of Structural Biology, University of Pittsburgh School of Medicine, Biomedical Science Tower 3, Room 2051, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA.
Alexander B TaylorDepartment of Biochemistry and Structural Biology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229-3900, USA; X-ray Crystallography Core Laboratory, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229-3900, USA.
Christian ZwiebDepartment of Biochemistry and Structural Biology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229-3900, USA.
Chang-Hyeock ByeonDepartment of Structural Biology, University of Pittsburgh School of Medicine, Biomedical Science Tower 3, Room 2051, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA.
Xiaohong ZhouDepartment of Structural Biology, University of Pittsburgh School of Medicine, Biomedical Science Tower 3, Room 2051, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA.
Valentín MendozaInstituto de Fisiología Celular, Universidad Nacional Autónoma de México, Ciudad de México 04510, México.
Fernando López-CasillasInstituto de Fisiología Celular, Universidad Nacional Autónoma de México, Ciudad de México 04510, México.
William FureyDepartment of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.
Andrew P HinckDepartment of Structural Biology, University of Pittsburgh School of Medicine, Biomedical Science Tower 3, Room 2051, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA. Electronic address: ahinck@pitt.edu.
University of Pittsburgh · USThe University of Texas Health Science Center at San Antonio · USUniversidad Nacional Autónoma de México · MX

Funding

TISSUE CULTURE---COREP30CA054174 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Robin Jean Leach · 1991 to 2026
$59.1M
Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
Medical Scientist Training Program Training GrantT32GM145449 · NIGMS · DUKE UNIVERSITY · PI Christopher D Kontos · 2022 to 2026
$6.6M
LIGAND/RECEPTOR INTERACTIONS IN THE TGF BETA SUPERFAMILYR01GM058670 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI HINCK, ANDREW P · 1999 to 2017
$3.6M
Phase II SER-CAT Optimization: Acquisition of a next generation area detectorS10RR028976 · NCRR · UNIVERSITY OF GEORGIA · PI WANG, BI-CHENG · 2010 to 2010
$1.5M
Inhibition of the tumor-promoting effects of TGF-beta in advanced prostate cancerR01CA172886 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI HINCK, ANDREW P, SUN, LUZHE · 2013 to 2016
$1.2M
Acquition of a microdiffractometer for SER-CATS10RR025528 · NCRR · UNIVERSITY OF GEORGIA · PI ROSE, JOHN PATRICK · 2009 to 2009
$414k
NCI NIH HHS P30 CA054174NCI NIH HHS R01 CA172886NCRR NIH HHS S10 RR025528NCRR NIH HHS S10 RR028976NIGMS NIH HHS P41 GM103311NIGMS NIH HHS R01 GM058670NIGMS NIH HHS T32 GM145449
6 · The paper itself

Abstract

Betaglycan (BG) and endoglin (ENG), homologous co-receptors of the TGF-β family, potentiate the signaling activity of TGF-β2 and inhibin A, and BMP-9 and BMP-10, respectively. BG exists as monomer and forms 1:1 growth factor (GF) complexes, while ENG exists as a dimer and forms 2:1 GF complexes. Herein, the structure of the BG orphan domain (BG

Indexed as

AnimalsBone Morphogenetic ProteinsEndoglinGrowth Differentiation Factor 2HEK293 CellsHumansProtein Structure, SecondaryProteoglycansRatsReceptors, Transforming Growth Factor betaScattering, Small AngleTransforming Growth Factor betaX-Ray DiffractionZebrafishbetaglycanBMP10 protein, humanBone Morphogenetic ProteinsEndoglinGDF2 protein, humanGrowth Differentiation Factor 2ProteoglycansReceptors, Transforming Growth Factor betaTransforming Growth Factor betabetaglycancardiac developmentcell signalingcell surface receptorco-receptorendoglinSAXSSPRtransforming growth factor beta (TGF-β)X-ray crystallography

Identifiers

PMID31327662
PMCPMC6726503
OpenAlexW2963840012

What OpenQuestion holds

Textmetadata
LicenceTDM
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.