Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The spectrum of mutations causing end-plate acetylcholinesterase deficiency.

Annals of neurology - 1 Feb 2000

Ohno K, Engel A G, Brengman J M, Shen X M, Heidenreich F, Vincent A, Milone M, Tan E, Demirci M, Walsh P, Nakano S, Akiguchi I

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acetylcholinesterase
Share to Collagen

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to COS Cells

Share to Gene Expression

Share to Infant

Share to Microscopy, Electron

Share to Muscle Proteins

Share to Mutation, Missense

Source

Identifiers

PMID: 10665486

Genes

COLQ
ACHE

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The spectrum of mutations causing end-plate acetylcholinesterase deficiency.PMID 10665486Read ↗

Human endplate acetylcholinesterase deficiency caused by mutations in the collagen-like tail subunit (ColQ) of the asymmetric enzyme.Semantic proximity Read ↗

Mutations in the C-Terminal Domain of ColQ in Endplate Acetylcholinesterase Deficiency Compromise ColQ-MuSK InteractionSemantic proximity Read ↗

Three novel COLQ mutations and variation of phenotypic expressivity due to G240X.Semantic proximity Read ↗

COOH-terminal collagen Q (COLQ) mutants causing human deficiency of endplate acetylcholinesterase impair the interaction of ColQ with proteins of the basal lamina.Semantic proximity Read ↗

C-terminal and heparin-binding domains of collagenic tail subunit are both essential for anchoring acetylcholinesterase at the synapse.Semantic proximity Read ↗

Structural and functional organization of synaptic acetylcholinesterase.Semantic proximity Read ↗

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?Semantic proximity Read ↗

Synaptic congenital myasthenic syndrome in three patients due to a novel missense mutation (T441A) of the COLQ gene.Semantic proximity Read ↗

Patients with congenital myasthenia associated with end-plate acetylcholinesterase deficiency show normal sequence, mRNA splicing, and assembly of catalytic subunits.Semantic proximity Read ↗

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

Two novel mutations in the COLQ gene cause endplate acetylcholinesterase deficiency.Semantic proximity Read ↗

[Molecular bases and therapeutic strategies in defective neuromuscular transmissions: lessons learned from a prototypical synapse].Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.