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Journal article

The spectrum of mutations causing end-plate acetylcholinesterase deficiency.

Abstract:

The end-plate species of acetylcholinesterase (AChE) is an asymmetric enzyme consisting of a collagenic tail subunit composed of three collagenic strands (ColQ), each attached to a tetramer of the T isoform of the catalytic subunit (AChE(T)) via a proline-rich attachment domain. The principal function of the tail subunit is to anchor asymmetric AChE in the synaptic basal lamina. Human end-plate AChE deficiency was recently shown to be caused by mutations in COLQ. We here report nine novel COL...

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Publication status:
Published

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Authors


Brengman, JM More by this author
Heidenreich, F More by this author
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Journal:
Annals of neurology
Volume:
47
Issue:
2
Pages:
162-170
Publication date:
2000-02-05
DOI:
EISSN:
1531-8249
ISSN:
0364-5134
URN:
uuid:30e5cef4-4385-4605-99af-777a44b24f2a
Source identifiers:
242773
Local pid:
pubs:242773

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