Identification and characterization of two novel brain-derived immunoglobulin superfamily members with a unique structural organization (Q24316343)

MAM domain containing glycosylphosphatidylinositol anchor 1

GOA release 2020-03-11

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GOA release 2020-03-11

author name string

E David Litwack

1

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Regis Babey

2

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Reto Buser

3

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Matthias Gesemann

4

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Dennis D M O'Leary

Molecular and Cellular Neuroscience

5

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language of work or name

English

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publication date

February 2004

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published in

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volume

25

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issue

2

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page(s)

263-74

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cites work

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Collateral branch formation related to cellular structures in the axon tract during corticopontine target recognition

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Lbx1 specifies somatosensory association interneurons in the dorsal spinal cord

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IgCAMs: bidirectional signals underlying neurite growth.

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Immunoglobulin superfamily receptors: cis-interactions, intracellular adapters and alternative splicing regulate adhesion.

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Axon guidance: receptor complexes and signaling mechanisms

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Cysteine mutations in the MAM domain result in monomeric meprin and alter stability and activity of the proteinase

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A homologue of the axonally secreted protein axonin-1 is an integral membrane protein of nerve fiber tracts involved in neurite fasciculation.

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

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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 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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Fatcat ID

release_be6m43frrvhv7axsxhdvytq5ua

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https://api.fatcat.wiki/v0/release/be6m43frrvhv7axsxhdvytq5ua

24 November 2022