期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 65, 期 15, 页码 2296-2306出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-008-8088-0
关键词
SNARE; botulism; tetanus; synaptotagmin; metalloprotease; endocytosis; synaptic vesicle; neurotransmission
资金
- Howard Hughes Medical Institute Funding Source: Medline
Despite its extreme toxicity, botulinum neurotoxin is widely utilized in low doses as a treatment for several neurological disorders; higher doses cause the neuroparalytic syndrome botulism. The toxin blocks neurotransmitter release by preferentially attaching to pre-synaptic membrane receptors at neuromuscular junctions and subsequently delivering a Zn2+-dependent protease component to presynaptic neuronal cytosol. These highly specialized enzymes exclusively hydrolyze peptide bonds within SNARE (soluble N-ethylmaleiamide sensitive factor attachment protein receptor) proteins. In this review we discuss the structural basis for botulinum toxin's exquisite specificity for its neuronal cell-surface receptors and intracellular SNARE targets.
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