Evidence map›Paper›PMID 27258772›Full record

ArticlePloS one2016

Structure of the Plexin Ectodomain Bound by Semaphorin-Mimicking Antibodies.

Kei Suzuki, Hiroyuki Tsunoda, Ryusuke Omiya, Kyoko Matoba, Takeshi Baba, Sachiyo Suzuki, Hiroaki Segawa, Atsushi Kumanogoh, Kenji Iwasaki, Kunihiro Hattori and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

11 citing papers in PubMed, 24 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

11 authors at 2 institutions in 1 country.

Kei SuzukiLaboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita, Osaka, Japan.
Hiroyuki TsunodaResearch Division, Chugai Pharmaceutical Co. Ltd, Gotemba, Shizuoka, Japan.
Ryusuke OmiyaResearch Division, Chugai Pharmaceutical Co. Ltd, Gotemba, Shizuoka, Japan.
Kyoko MatobaLaboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita, Osaka, Japan.
Takeshi BabaResearch Division, Chugai Pharmaceutical Co. Ltd, Gotemba, Shizuoka, Japan.
Sachiyo SuzukiResearch Division, Chugai Pharmaceutical Co. Ltd, Gotemba, Shizuoka, Japan.
Hiroaki SegawaResearch Division, Chugai Pharmaceutical Co. Ltd, Gotemba, Shizuoka, Japan.
Atsushi KumanogohDepartment of Respiratory Medicine, Allergy, and Rheumatic Disease, Graduate School of Medicine, Osaka University, Suita, Osaka, Japan.
Kenji IwasakiLaboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita, Osaka, Japan.
Kunihiro HattoriResearch Division, Chugai Pharmaceutical Co. Ltd, Gotemba, Shizuoka, Japan.
Junichi TakagiLaboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita, Osaka, Japan.
Protein Research Foundation · JPOsaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Semaphorin family proteins act on cells to mediate both repulsive and attractive guidance via binding to plexin family receptors, thereby playing fundamental roles in the morphogenesis and homeostasis of various tissues. Although semaphorin-plexin signaling is implicated in various diseases and is thus a target of intensive research, our mechanistic understanding of how semaphorins activate plexins on the cell surface is limited. Here, we describe unique anti-plexin-A1 antibodies that can induce a collapsed morphology in mouse dendritic cells as efficiently as the semaphorin 3A (Sema3A) ligand. Precise epitope analysis indicates that these "semaphorin-mimicking" antibodies dimerize cell-surface plexin-A1 by binding to the N-terminal sema domain of the plexin at sites away from the interface used by the Sema3A ligand. Structural analysis of plexin-A1 fragments using negative stain electron microscopy further revealed that this agonistic capacity is closely linked to the location and orientation of antibody binding. In addition, the full-length plexin-A1 ectodomain exhibited a highly curved "C" shape, reinforcing the very unusual dimeric receptor conformation of this protein at the cell surface when engaged with Sema3A or agonistic antibodies.

Indexed as

AnimalsAntibodies, MonoclonalCell MembraneDendritic CellsEpitope MappingEpitopesHumansMiceNerve Tissue ProteinsProtein DomainsProtein MultimerizationReceptors, Cell SurfaceSemaphorin-3ASemaphorinsSignal TransductionAntibodies, MonoclonalEpitopesNerve Tissue ProteinsPLXNA1 protein, humanPlxna1 protein, mouseReceptors, Cell SurfaceSema3a protein, mouseSemaphorin-3ASemaphorins

Identifiers

PMID27258772
PMCPMC4892512
OpenAlexW2410864000

What Socratic 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 Socratic graph.