Cis-activation of L1-mediated ankyrin recruitment by TAG-1 homophilic cell adhesion (Q28290362)

ORCID Public Data File 2021

author name string

J D Malhotra

series ordinal

1

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P Tsiotra

series ordinal

2

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M Hortsch

series ordinal

4

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language of work or name

English

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publication date

11 December 1998

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published in

Journal of Biological Chemistry

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volume

273

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issue

50

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page(s)

33354-9

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cites work

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An L1-like molecule, the 8D9 antigen, is a potent substrate for neurite extension

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Structural requirements for outside-in and inside-out signaling by Drosophila neuroglian, a member of the L1 family of cell adhesion molecules

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The axonal glycoprotein TAG-1 is an immunoglobulin superfamily member with neurite outgrowth-promoting activity

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The axonally secreted cell adhesion molecule, axonin-1. Primary structure, immunoglobulin-like and fibronectin-type-III-like domains and glycosyl-phosphatidylinositol anchorage

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The axonally secreted protein axonin-1 is a potent substratum for neurite growth

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Cell-cell adhesion by homophilic interaction of the neuronal recognition molecule axonin-1

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Cell adhesion molecules NgCAM and axonin-1 form heterodimers in the neuronal membrane and cooperate in neurite outgrowth promotion

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The fibronectin domains of the neural adhesion molecule TAX-1 are necessary and sufficient for homophilic binding

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8 Immunoprecipitation of proteins from cell-free translations

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Neurite outgrowth on immobilized axonin-1 is mediated by a heterophilic interaction with L1(G4)

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