Evidence map›Paper›PMID 26520118›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2016

Production, Isolation, and Structural Analysis of Ligands and Receptors of the TGF-β Superfamily.

Tao Huang, Andrew P Hinck

Open access · greenAbstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

20 citing papers in PubMed, 41 citations in OpenAlex.

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  9. The BMP Pathway in Blood Vessel and Lymphatic Vessel Biology.International journal of molecular sciences · 2021
    Review
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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

2 authors at 1 institution in 1 country.

Tao HuangProtein Chemistry, Novo Nordisk Research Center China, 20 Life Science Park Rd, Bldg 2, Beijing, 102206, China.
Andrew P HinckProtein Chemistry, Novo Nordisk Research Center China, 20 Life Science Park Rd, Bldg 2, Beijing, 102206, China. ahinck@pitt.edu.
Novogene Bioinformatics Institute · CN

Funding

TISSUE CULTURE---COREP30CA054174 · NCI · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI Lei Zheng · 1991 to 2026
$59.1M
LIGAND/RECEPTOR INTERACTIONS IN THE TGF BETA SUPERFAMILYR01GM058670 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI HINCK, ANDREW P · 1999 to 2017
$3.6M
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
NCI NIH HHS CA172886NCI NIH HHS P30 CA054174NCI NIH HHS R01 CA172886NIGMS NIH HHS GM58670NIGMS NIH HHS R01 GM058670
6 · The paper itself

Abstract

The ability to understand the molecular mechanisms by which secreted signaling proteins of the TGF-β superfamily assemble their cell surface receptors into complexes to initiate downstream signaling is dependent upon the ability to determine atomic-resolution structures of the signaling proteins, the ectodomains of the receptors, and the complexes that they form. The structures determined to date have revealed major differences in the overall architecture of the signaling complexes formed by the TGF-βs and BMPs, which has provided insights as to how they have evolved to fulfill their distinct functions. Such studies, have however, only been applied to a few members of the TGF-β superfamily, which is largely due to the difficulty of obtaining milligram-scale quantities of highly homogenous preparations of the disulfide-rich signaling proteins and receptor ectodomains of the superfamily. Here we describe methods used to produce signaling proteins and receptor ectodomains of the TGF-β superfamily using bacterial and mammalian expression systems and procedures to purify them to homogeneity.

Indexed as

LigandsAnimalsCell LineCrystallography, X-RayGene ExpressionHumansMagnetic Resonance SpectroscopyProtein BindingProtein Interaction Domains and MotifsReceptors, Transforming Growth Factor betaRecombinant Fusion ProteinsSignal TransductionTransforming Growth Factor betaLigandsReceptors, Transforming Growth Factor betaRecombinant Fusion ProteinsTransforming Growth Factor betaligand and receptorprotein expressionprotein purificationstructural analysisTGF-β

Identifiers

PMID26520118
PMCPMC4846357
OpenAlexW1950803773

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.