Synapse formation: if it looks like a duck and quacks like a duck ... (Q28139097)

Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons

Europe PubMed Central

title

Synapse formation: if it looks like a duck and quacks like a duck ... (English)

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author name string

I Cantallops

series ordinal

1

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H T Cline

series ordinal

2

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language of work or name

English

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publication date

7 September 2000

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published in

Current Biology

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volume

10

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issue

17

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page(s)

R620-3

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cites work

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Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses

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The structure and expression of the human neuroligin-3 gene

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Functional redundancy of acetylcholinesterase and neuroligin in mammalian neuritogenesis

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Acetylcholinesterase-transgenic mice display embryonic modulations in spinal cord choline acetyltransferase and neurexin Iβ gene expression followed by late-onset neuromotor deterioration

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Neurotransmitter secretion along growing nerve processes: comparison with synaptic vesicle exocytosis

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Distribution of neurotransmitter secretion in growing axons.

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Assembly of presynaptic active zones from cytoplasmic transport packets

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A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain

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Binding of neuroligins to PSD-95

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CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins

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A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins

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Deficiency in induction but not expression of LTP in hippocampal slices from young rats

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Maturation of a central glutamatergic synapse

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Rho GTPases and signaling networks

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Developmental regulation of spine motility in the mammalian central nervous system

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Essential roles of Drosophila RhoA in the regulation of neuroblast proliferation and dendritic but not axonal morphogenesis

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ChIPping away at potassium channel regulation

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Identification of proteins in the postsynaptic density fraction by mass spectrometry

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