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

doi:10.1073/pnas.95.16.9654

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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 4 Aug 1998

Ohno K, Brengman J, Tsujino A, Engel A G

Abstract excerpt

In skeletal muscle, acetylcholinesterase (AChE) exists in homomeric globular forms of type T catalytic subunits (ACHET) and heteromeric asymmetric forms composed of 1, 2, or 3 tetrameric ACHET attached to a collagenic tail (ColQ). Asymmetric AChE is concentrated at the endplate (EP), where its co...

Topics

Acetylcholinesterase
Adolescent
Adult
Alternative Splicing
Amino Acid Sequence
Animals
Base Sequence
COS Cells
Child
Child, Preschool
Cloning, Molecular
Collagen

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

DNA, Complementary

Female

Heterozygote

Homozygote

Humans

Male

Source

Open in PubMed Open full text

Identifiers

PMID: 9689136
DOI: 10.1073/pnas.95.16.9654
PMCID: PMC21394

Genes

COLQ

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9689136-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Human endplate acetylcholinesterase deficiency caused by mutations in the collagen-like tail subunit (ColQ) of the asymmetric enzyme.PMID 9689136Read ↗

The spectrum of mutations causing end-plate acetylcholinesterase deficiency.Semantic proximity Read ↗

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

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

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

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

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

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 ↗

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

The First Case of Congenital Myasthenic Syndrome Caused by a Large Homozygous Deletion in the C-Terminal Region of COLQ (Collagen Like Tail Subunit of Asymmetric Acetylcholinesterase) Protein.Semantic proximity Read ↗

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