PRiMA: the membrane anchor of acetylcholinesterase in the brain (Q28587630)

31 January 2017

title

PRiMA: the membrane anchor of acetylcholinesterase in the brain (English)

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Proline rich membrane anchor 1

31 January 2017

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GOA release 2020-03-11

author name string

Anselme L. Perrier

series ordinal

1

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31 January 2017

Jean Massoulié

series ordinal

2

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31 January 2017

Eric Krejci

series ordinal

3

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31 January 2017

language of work or name

English

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publication date

17 January 2002

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31 January 2017

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31 January 2017

volume

33

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31 January 2017

issue

2

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31 January 2017

page(s)

275–285

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Tetramerization domain of human butyrylcholinesterase is at the C-terminus

31 January 2017

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Quaternary associations of acetylcholinesterase. II. The polyproline attachment domain of the collagen tail

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The membrane anchor of mammalian brain acetylcholinesterase consists of a single glycosylated protein of 22 kDa.

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A 13 kDa fragment is responsible for the hydrophobic aggregation of brain G4 acetylcholinesterase

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7 January 2021

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7 January 2021

Two distinct proteins are associated with tetrameric acetylcholinesterase on the cell surface

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7 January 2021

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A four-to-one association between peptide motifs: four C-terminal domains from cholinesterase assemble with one proline-rich attachment domain (PRAD) in the secretory pathway

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Common EF-hand motifs in cholinesterases and neuroligins suggest a role for Ca2 binding in cell surface associations

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Identifiers

DOI

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