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Articles by Thomas Cast
Multiple N-linked glycosylation sites critically modulate the synaptic abundance of Neuroligin isoforms
ABSTRACT In recent years, elegant glycomic and glycoproteomic approaches have revealed an intricate glycosylation profile of mammalian brain with enormous spatial and temporal diversities. Nevertheless, at a cellular level, it is unclear how these post-translational modifications (PTMs) affect various proteins to influence crucial neuronal properties.
Induction of synapse formation by de novo neurotransmitter synthesis - Nature Communications
Abstract A vital question in neuroscience is how neurons align their postsynaptic structures with presynaptic release sites. Although synaptic adhesion proteins are known to contribute in this process, the role of neurotransmitters remains unclear. Here we inquire whether de novo biosynthesis and vesicular release of a noncanonical transmitter can facilitate the assembly of its corresponding postsynapses.
An Autism-Associated Mutation Impairs Neuroligin-4 Glycosylation and Enhances Excitatory Synaptic Transmission in Human Neurons
Cover ArticleResearch Articles, Cellular/Molecular Thomas P. Cast, Daniel J. Boesch, Kim Smyth, Alisa E. Shaw, Michael Ghebrial and Soham Chanda Journal of Neuroscience 20 January 2021, 41 (3) 392-407; DOI: https://doi.org/10.1523/JNEUROSCI.0404-20.2020 Abstract Neuroligins (NLGNs) are a class of postsynaptic cell adhesion molecules that interact with presynaptic neurexins (NRXNs) and regulate synapse function.
An Autism-Associated Mutation Impairs Neuroligin-4 Glycosylation and Enhances Excitatory Synaptic Transmission in Human Neurons
Research Articles, Cellular/Molecular Thomas Cast, Daniel Boesch, Kim Smyth, Alisa Shaw, Michael Ghebrial and Soham Chanda Journal of Neuroscience 2 December 2020, JN-RM-0404-20; DOI: https://doi.org/10.1523/JNEUROSCI.0404-20.2020 Abstract Neuroligins (NLGNs) are a class of postsynaptic cell-adhesion molecules that interact with presynaptic Neurexins (NRXNs) and regulate synapse function.
An Unusual Route for p-Aminobenzoate Biosynthesis in Chlamydia trachomatis Involves a Probable Self-Sacrificing Diiron Oxygenase
Research Article | Spotlight Yamilet Macias-Orihuela, Thomas Cast, Ian Crawford, Kevin J. Brandecker, Jennifer J. Thiaville, Alexey G. Murzin, Valérie de Crécy-Lagard, Robert H. White, Kylie D. Allen William W. Metcalf, Editor DOI: 10.1128/JB.00319-20 ABSTRACT Chlamydia trachomatis lacks the canonical genes required for the biosynthesis of p-aminobenzoate (pABA), a component of essential folate cofactors. Previous studies revealed a single gene from C.
An unusual route for p-aminobenzoate biosynthesis in Chlamydia trachomatis involves a probable self-sacrificing diiron oxygenase
Research Article Yamilet Macias-Orihuela, Thomas Cast, Ian Crawford, Kevin J. Brandecker, Jennifer J. Thiaville, Alexey G. Murzin, Valérie de Crécy-Lagard, Robert H. White, Kylie D. Allen DOI: 10.1128/JB.00319-20 ABSTRACT Chlamydia trachomatis lacks the canonical genes required for the biosynthesis of p-aminobenzoate (pABA), a component of essential folate cofactors. Previous studies revealed a single gene from C. trachomatis, CT610, that rescues E.
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