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

Intramolecular relationships in cholinesterases revealed by oocyte expression of site-directed and natural variants of human BCHE.

The EMBO journal - 1 Apr 1992

Neville L F, Gnatt A, Loewenstein Y, Seidman S, Ehrlich G, Soreq H

Abstract excerpt

Structure-function relationships of cholinesterases (CHEs) were studied by expressing site-directed and naturally occurring mutants of human butyrylcholinesterase (BCHE) in microinjected Xenopus oocytes. Site-directed mutagenesis of the conserved electronegative Glu441,Ile442,Glu443 domain to Gly441,Ile442,Gln443 drastically reduced the rate of butyrylthiocholine (BTCh) hydrolysis and caused pronounced resistance...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Base Sequence

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

Share to Binding Sites

Share to Cloning, Molecular

Share to Electrophoresis, Polyacrylamide Gel

Share to Genetic Variation

Share to Kinetics

Share to Molecular Sequence Data

Source

Open in PubMed Open full text

Identifiers

PMID: 1373381
DOI: 10.1002/j.1460-2075.1992.tb05210.x
PMCID: PMC556614

Genes

BCHE

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

Intramolecular relationships in cholinesterases revealed by oocyte expression of site-directed and natural variants of human BCHE.PMID 1373381Read ↗

Anionic site interactions in human butyrylcholinesterase disrupted by two single point mutations.Semantic proximity Read ↗

Site-directed mutagenesis of active site residues reveals plasticity of human butyrylcholinesterase in substrate and inhibitor interactions.Semantic proximity Read ↗

Mutations and impaired expression in the ACHE and BCHE genes: neurological implications.Semantic proximity Read ↗

Enzyme ChE, cholinergic therapy and molecular docking: Significant considerations and future perspectivesSemantic proximity Read ↗

Expression of three naturally occurring genetic variants (G75R, E90D, I99M) of the BCHE gene of human butyrylcholinesterase.Semantic proximity Read ↗

Naturally Occurring Genetic Variants of Human Acetylcholinesterase and Butyrylcholinesterase and Their Potential Impact on the Risk of Toxicity from Cholinesterase Inhibitors.Semantic proximity Read ↗

Successive organophosphate inhibition and oxime reactivation reveals distinct responses of recombinant human cholinesterase variants.Semantic proximity Read ↗

Characterization of four BCHE mutations associated with prolonged effect of suxamethonium.Semantic proximity Read ↗

Understanding the non-catalytic behavior of human butyrylcholinesterase silent variants: Comparison of wild-type enzyme, catalytically active Ala328Cys mutant, and silent Ala328Asp variant.Semantic proximity Read ↗

Mutagenesis of essential functional residues in acetylcholinesterase.Semantic proximity Read ↗

Characterization of a novel BCHE "silent" allele: point mutation (p.Val204Asp) causes loss of activity and prolonged apnea with suxamethonium.Semantic proximity Read ↗

Molecular dissection of cholinesterase domains responsible for carbamate toxicity.Semantic proximity Read ↗

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