C-terminal and heparin-binding domains of collagenic tail subunit are both essential for anchoring acetylcholinesterase at the synapse (Q42454995)

31 October 2017

title

C-terminal and heparin-binding domains of collagenic tail subunit are both essential for anchoring acetylcholinesterase at the synapse (English)

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31 October 2017

2

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31 October 2017

Lewis M Kimbell

1

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31 October 2017

Andrew G Engel

series ordinal

3

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31 October 2017

Richard L Rotundo

series ordinal

4

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31 October 2017

language of work or name

English

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publication date

31 December 2003

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Journal of Biological Chemistry

31 October 2017

published in

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31 October 2017

volume

279

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31 October 2017

issue

12

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31 October 2017

page(s)

10997-11005

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Molecular and cellular biology of cholinesterases

31 October 2017

cites work

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Binding of the asymmetric forms of acetylcholinesterase to heparin

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Anchorage of collagen-tailed acetylcholinesterase to the extracellular matrix is mediated by heparan sulfate proteoglycans

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Distribution and anchoring of molecular forms of acetylcholinesterase

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Mutation in the human acetylcholinesterase-associated collagen gene, COLQ, is responsible for congenital myasthenic syndrome with end-plate acetylcholinesterase deficiency (Type Ic)

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Congenital end-plate acetylcholinesterase deficiency caused by a nonsense mutation and an A-->G splice-donor-site mutation at position +3 of the collagenlike-tail-subunit gene (COLQ): how does G at position +3 result in aberrant splicing?

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Congenital myasthenic syndrome caused by prolonged acetylcholine receptor channel openings due to a mutation in the M2 domain of the epsilon subunit

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Two different heparin-binding domains in the triple-helical domain of ColQ, the collagen tail subunit of synaptic acetylcholinesterase

21 January 2018

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21 January 2018

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21 January 2018

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Trimerization domain of the collagen tail of acetylcholinesterase

21 January 2018

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Two heparin-binding domains are present on the collagenic tail of asymmetric acetylcholinesterase

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M305462200

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31 October 2017

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