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Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formatio...

Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formatio...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_419e3942d7884c3195337cfa2debe0b8

Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formation

About this item

Full title

Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formation

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2018-01, Vol.9 (1), p.269-9, Article 269

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Synapse formation is triggered by
trans
-synaptic interactions of cell adhesion molecules, termed synaptic organizers. Three members of type-II receptor protein tyrosine phosphatases (classified as type-IIa RPTPs; PTPδ, PTPσ and LAR) are known as presynaptic organizers. Synaptic adhesion-like molecules (SALMs) have recently emerged as a famil...

Alternative Titles

Full title

Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formation

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_419e3942d7884c3195337cfa2debe0b8

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_419e3942d7884c3195337cfa2debe0b8

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-017-02417-z

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