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

Homology built model of acetylcholinesterase from Drosophila melanogaster.

Journal of enzyme inhibition - 1 Jan 1999

Stojan J

Abstract excerpt

Acetylcholinesterases from Drosophila melanogaster and Torpedo marmorata possess 35% identical residues. We built a homology model of the Drosophila enzyme on the basis of the known three-dimensional structure of Torpedo acetylcholinesterase, which revealed an oval rim of the active site gorge with an additional hollow which could accept small charged ligands more firmly than the corresponding surface in the...

Read the complete abstract on PubMed

Topics

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

Share to Acetylcholine
Share to Acetylcholinesterase
Share to Choline

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

Share to Computer Simulation

Share to Drosophila melanogaster

Share to Sequence Alignment

Share to Sequence Homology, Amino Acid

Share to Torpedo

Source

Identifiers

PMID: 10445043
DOI: 10.3109/14756369909030316

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

Homology built model of acetylcholinesterase from Drosophila melanogaster.PMID 10445043Read ↗

Acetylcholinesterases – the structural similarities and differencesSemantic proximity Read ↗

In silico studies on the role of mutant Y337A to reactivate tabun inhibited mAChE with K048.Semantic proximity Read ↗

Ligand-induced conformational changes in residues flanking the active site gorge of acetylcholinesterase.Semantic proximity Read ↗

Probing the peripheral site of human butyrylcholinesterase.Semantic proximity Read ↗

Differences in active-site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase.Semantic proximity Read ↗

A tryptophan in the bottleneck of the catalytic gorge of an invertebrate acetylcholinesterase confers relative resistance to carbamate and organophosphate inhibitors.Semantic proximity Read ↗

In silico analyses of acetylcholinesterase (AChE) and its genetic variants in interaction with the anti‐Alzheimer drug RivastigmineSemantic proximity Read ↗

Role of tyrosine 337 in the binding of huperzine A to the active site of human acetylcholinesterase.Semantic proximity Read ↗

Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding.Semantic proximity Read ↗

Structural insights into conformational flexibility at the peripheral site and within the active center gorge of AChE.Semantic proximity Read ↗

Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function.Semantic proximity Read ↗

Determinants of substrate specificity of a second non-neuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis.Semantic proximity Read ↗

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