Acetylcholinesterase associates differently with its anchoring proteins ColQ and PRiMA - Wikidata - wikimedia - TriplyDB

Acetylcholinesterase associates differently with its anchoring proteins ColQ and PRiMA

Acetylcholinesterase associates differently with its anchoring proteins ColQ and PRiMA

http://www.wikidata.org/entity/Q40423255

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Targeting acetylcholinesterase to membrane rafts: a function mediated by the proline-rich membrane anchor (PRiMA) in neurons The PRiMA-linked cholinesterase tetramers are assembled from homodimers: hybrid molecules composed of acetylcholinesterase and butyrylcholinesterase dimers are up-regulated during development of chicken brain The assembly of proline-rich membrane anchor (PRiMA)-linked acetylcholinesterase enzyme: glycosylation is required for enzymatic activity but not for oligomerization.Fine mapping study reveals novel candidate genes for carotid intima-media thickness in Dominican Republican families Respective roles of the catalytic domains and C-terminal tail peptides in the oligomerization and secretory trafficking of human acetylcholinesterase and butyrylcholinesterase.Three N-Glycosylation Sites of Human Acetylcholinesterase Shares Similar Glycan Composition.Proline-Rich Chaperones Are Compared Computationally and Experimentally for Their Abilities to Facilitate Recombinant Butyrylcholinesterase Tetramerization in CHO Cells.

P2860

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P2860

Acetylcholinesterase associates differently with its anchoring proteins ColQ and PRiMA

http://www.wikidata.org/entity/Q40423255

description

2008 nî lūn-bûn

@nan

2008年の論文

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2008年学术文章

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2008年学术文章

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2008年学术文章

@zh-hans

2008年学术文章

@zh-my

2008年学术文章

@zh-sg

2008年學術文章

@yue

2008年學術文章

@zh

2008年學術文章

@zh-hant

name

Acetylcholinesterase associates differently with its anchoring proteins ColQ and PRiMA

@en

type

label

Acetylcholinesterase associates differently with its anchoring proteins ColQ and PRiMA

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prefLabel

Acetylcholinesterase associates differently with its anchoring proteins ColQ and PRiMA

@en

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P1433

Journal of Biological Chemistry

P1476

Acetylcholinesterase associates differently with its anchoring proteins ColQ and PRiMA

@en

P2093

Claudine Schmitt

http://www.w3.org/2001/XMLSchema#string

Hiba Noureddine

http://www.w3.org/2001/XMLSchema#string

Jean Massoulié

http://www.w3.org/2001/XMLSchema#string

Stéphanie Carvalho

http://www.w3.org/2001/XMLSchema#string

Suzanne Bon

http://www.w3.org/2001/XMLSchema#string

P2860

The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix

A new and rapid colorimetric determination of acetylcholinesterase activity

Rapid and efficient site-specific mutagenesis without phenotypic selection

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

Cloning and expression of a rat acetylcholinesterase subunit: generation of multiple molecular forms and complementarity with a Torpedo collagenic subunit

PRiMA: the membrane anchor of acetylcholinesterase in the brain

pEF-BOS, a powerful mammalian expression vector

Molecular architecture of acetylcholinesterase collagen-tailed forms; construction of a glycolipid-tailed tetramer

Amphiphilic and nonamphiphilic forms of bovine and human dopamine beta-hydroxylase.

Asymmetric and globular forms of acetylcholinesterase in mammals and birds.

P304

20722-20732

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scholarly article

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10.1074/JBC.M801364200

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30

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283

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2008-05-29T00:00:00Z

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18511416

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3258952

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