Evidence map›Paper›PMID 28652325›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Transmembrane features governing Fc receptor CD16A assembly with CD16A signaling adaptor molecules.

Alfonso Blázquez-Moreno, Soohyung Park, Wonpil Im, Melissa J Call, Matthew E Call, Hugh T Reyburn

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

38 citing papers in PubMed, 55 citations in OpenAlex.

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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

6 authors at 4 institutions in 3 countries.

Alfonso Blázquez-MorenoDepartment of Immunology and Oncology, Centro Nacional de Biotecnología-Consejo Superior de Investigaciones Científicas, Madrid 28049, Spain.
Soohyung ParkDepartment of Biological Sciences, Lehigh University, Bethlehem, PA 18015.
Wonpil ImDepartment of Biological Sciences, Lehigh University, Bethlehem, PA 18015.
Melissa J CallStructural Biology Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia.
Matthew E CallStructural Biology Division, The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia; htreyburn@cnb.csic.es mecall@wehi.edu.au.
Hugh T ReyburnDepartment of Immunology and Oncology, Centro Nacional de Biotecnología-Consejo Superior de Investigaciones Científicas, Madrid 28049, Spain; htreyburn@cnb.csic.es mecall@wehi.edu.au.
Centro Nacional de Biotecnología · ESLehigh University · USUniversity of Melbourne · AUWalter and Eliza Hall Institute of Medical Research · AU

Funding

Mechanisms & Energetics of Transmembrane-induced Signaling of Cytokine ReceptorsR01GM092950 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI IM, WONPIL · 2010 to 2014
$1.4M
NIGMS NIH HHS R01 GM092950
6 · The paper itself

Abstract

Many activating immunoreceptors associate with signaling adaptor molecules like FcεR1γ or CD247. FcεR1γ and CD247 share high sequence homology and form disulphide-linked homodimers that contain a pair of acidic aspartic acid residues in their transmembrane (TM) domains that mediate assembly, via interaction with an arginine residue at a similar register to these aspartic acids, with the activating immunoreceptors. However, this model cannot hold true for receptors like CD16A, whose TM domains do not contain basic residues. We have carried out an extensive site-directed mutagenesis analysis of the CD16A receptor complex and now report that the association of receptor with the signaling adaptor depends on a network of polar and aromatic residues along the length of the TM domain. Molecular modeling indicates that CD16A TM residues F

Indexed as

Amino Acid MotifsAnimalsCD3 ComplexCell LineCell MembraneGlycosylationGPI-Linked ProteinsHEK293 CellsHumansHydrogen BondingMagnetic Resonance SpectroscopyMiceMutagenesis, Site-DirectedProtein DomainsProtein MultimerizationReceptors, IgECD3 antigen, zeta chainCD3 ComplexFCGR3B protein, humanGPI-Linked ProteinsReceptors, IgEReceptors, IgGReceptors, Immunologicactivating immunoreceptorsFc receptorssignaling adaptor moleculestransmembrane interactions

Identifiers

PMID28652325
PMCPMC5514760
OpenAlexW2723461340

What OpenQuestion holds

Textmetadata
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.