@article {68434,
	title = {Proximity labeling: spatially resolved proteomic mapping for neurobiology.},
	journal = {Curr Opin Neurobiol},
	volume = {50},
	year = {2018},
	month = {06/2018},
	pages = {17-23},
	abstract = {<p>Understanding signaling pathways in neuroscience requires high-resolution maps of the underlying protein networks. Proximity-dependent biotinylation with engineered enzymes, in combination with mass spectrometry-based quantitative proteomics, has emerged as a powerful method to dissect molecular interactions and the localizations of endogenous proteins. Recent applications to neuroscience have provided insights into the composition of sub-synaptic structures, including the synaptic cleft and inhibitory post-synaptic density. Here we compare the different enzymes and small-molecule probes for proximity labeling in the context of cultured neurons and tissue, review existing studies, and provide technical suggestions for the in vivo application of proximity labeling.</p>
},
	keywords = {Animals, Biotinylation, Humans, Neurobiology, Neuroimaging, Proteome, Proteomics},
	issn = {1873-6882},
	doi = {10.1016/j.conb.2017.10.015},
	author = {Han, Shuo and Li, Jiefu and Ting, Alice Y}
}
