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pubmed-article:19057331pubmed:abstractTextApoptosis has been shown to play an important role in motor neuron (MN) degeneration in both neurodegenerative disease and peripheral neuropathy. Bcl-xL, an antiapoptotic protein, is down-regulated in these etiologies [corrected] The carboxyl-terminal domain of the tetanus toxin heavy chain (Hc) has high affinity for axon terminal binding and uptake into motor and dorsal root ganglion (DRG) neurons. We report the development of a fusion protein between Hc and Bcl-xL to enhance uptake of Bcl-xL by MNs as a strategy for inhibiting peripheral neuronal apoptosis.lld:pubmed
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pubmed-article:19057331pubmed:volume63lld:pubmed
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pubmed-article:19057331pubmed:pagination1175-82; discussion 1182-4lld:pubmed
pubmed-article:19057331pubmed:dateRevised2009-4-28lld:pubmed
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pubmed-article:19057331pubmed:articleTitleFusion of the tetanus toxin C fragment binding domain and Bcl-xL for protection of peripheral nerve neurons.lld:pubmed
pubmed-article:19057331pubmed:affiliationDepartment of Cell Biology, Cleveland Clinic, Cleveland, Ohio, USA.lld:pubmed
pubmed-article:19057331pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:19057331pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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