Evidence map›Paper›PMID 30262834›Full record

ArticleNature communications2018

Structural insights into modulation and selectivity of transsynaptic neurexin-LRRTM interaction.

Atsushi Yamagata, Sakurako Goto-Ito, Yusuke Sato, Tomoko Shiroshima, Asami Maeda, Masahiko Watanabe, Takashi Saitoh, Katsumi Maenaka, Tohru Terada, Tomoyuki Yoshida and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 1 pooled it
2.4field-weighted citation impact, top 11% 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

31 citing papers in PubMed, 1 synthesis or guideline pooled it, 44 citations in OpenAlex.

  1. Pooled it
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  3. Review
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  8. Article
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  14. Review
  15. Cell Adhesion Molecule Signaling at the Synapse: Beyond the Scaffold.Cold Spring Harbor perspectives in biology · 2024
    Review
  16. Article
  17. Structure and evolution of neuronal wiring receptors and ligands.Developmental dynamics : an official publication of the American Association of Anatomists · 2023
    Review
  18. Article
  19. Article
  20. Review
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 5 institutions in 2 countries.

Atsushi YamagataInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Sakurako Goto-ItoInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Yusuke SatoInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Tomoko ShiroshimaInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Asami MaedaInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Masahiko WatanabeDepartment of Anatomy, Hokkaido University Faculty of Medicine, Sapporo, 060-8638, Japan.
Takashi SaitohDepartment of Medicinal Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University of Science, Sapporo, 006-8585, Japan.
Katsumi MaenakaCenter for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, 060-0812, Japan.ORCID http://orcid.org/0000-0002-5459-521X
Tohru TeradaInterfaculty Initiative in Information Studies, The University of Tokyo, Tokyo, 113-0033, Japan.ORCID http://orcid.org/0000-0002-7091-0646
Tomoyuki YoshidaDepartment of Molecular Neuroscience, Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Toyama, 930-0194, Japan.
Takeshi UemuraCREST, JST, Saitama, 332-0012, Japan. tuemura@shinshu-u.ac.jp.
Shuya FukaiInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan. fukai@iam.u-tokyo.ac.jp.ORCID http://orcid.org/0000-0002-1241-1443
Japan Science and Technology Agency · JPHokkaido University · JPHokkaido University of Science · JPShinshu University · JPThe University of Tokyo · JP

Funding

Japan Science and Technology Agency (JST) PRESTOJapan Society for the Promotion of Science (JSPS) JP16H04749Japan Society for the Promotion of Science (JSPS) JP24247014Japan Society for the Promotion of Science (JSPS) JP25290021Japan Society for the Promotion of Science (JSPS) JP25293057JST | Core Research for Evolutional Science and Technology (CREST) JPMJCR12M5
6 · The paper itself

Abstract

Leucine-rich repeat transmembrane neuronal proteins (LRRTMs) function as postsynaptic organizers that induce excitatory synapses. Neurexins (Nrxns) and heparan sulfate proteoglycans have been identified as presynaptic ligands for LRRTMs. Specifically, LRRTM1 and LRRTM2 bind to the Nrxn splice variant lacking an insert at the splice site 4 (S4). Here, we report the crystal structure of the Nrxn1β-LRRTM2 complex at 3.4 Å resolution. The Nrxn1β-LRRTM2 interface involves Ca

Indexed as

Amino Acid SequenceAnimalsCalcium-Binding ProteinsCell Adhesion Molecules, NeuronalHEK293 CellsHumansMembrane ProteinsMiceMutant ProteinsNerve Tissue ProteinsNeural Cell Adhesion MoleculesProtein BindingSynapsesCalcium-Binding ProteinsCell Adhesion Molecules, NeuronalLRRTM2 protein, humanLRRTM2 protein, mouseMembrane ProteinsMutant ProteinsNerve Tissue ProteinsNeural Cell Adhesion MoleculesNRXN1 protein, humanNrxn1 protein, mouse

Identifiers

PMID30262834
PMCPMC6160412
OpenAlexW2890145919

What OpenQuestion 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 OpenQuestion graph.