ReviewProtein science : a publication of the Protein Society2025
Acetylcholinesterase: Structure, dynamics, and interactions with organophosphorus compounds.
Review in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed.
- An Integrated in Silico, in Vitro, and in Vivo Assessment of the Antioxidant and Neuroprotective Profile of Selenocyanate Compounds.Biological trace element research · 2026Article
- Probing novel azole-sulfonamide urea/thiourea conjugates as multitarget inhibitors of AChE and hCAs (I and II): synthesis, in vitro, and in silico studies.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2026Article
- Computational identification of novel acetylcholinesterase inhibitors as potential treatments for Alzheimer's disease.Journal of Alzheimer's disease : JAD · 2026Article
- Design, synthesis, and evaluation of pyrano[3,2-RSC advances · 2026Article
- QSAR-ML- and Metadynamics-Guided Design of Symmetrical Bis-Indanones to Overcome Mutational Anchor Loss in Acetylcholinesterase.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Xeniaphyllane-Type Diterpenoids from the Soft CoralJournal of natural products · 2026Article
- Recent Advances in Pyrazole-Based Cholinesterase Inhibitors: Medicinal Chemistry Perspectives from 2020 to 2025.Pharmaceuticals (Basel, Switzerland) · 2026Review
- The Pharmacokinetic Properties of Veterinary Antiparasitic Drugs in the Context of Human Pregnancy-An In Silico Study.International journal of molecular sciences · 2026Article
- Isolation and identification of hasubanan alkaloids having anti-cholinesterase and antioxidant activity from the stem Stephania japonica.BMC complementary medicine and therapies · 2026Article
- A copper-mediated Fenton-like dual-mode optical sensor for sensitive determination of acetylcholinesterase activity in biological fluids.RSC advances · 2026Article
- Structure-Reactivity Relationships inInternational journal of molecular sciences · 2026Article
- Putative acetylcholinesterase genes from a one-host tick species, the winter tick (Dermacentor albipictus).Parasites & vectors · 2026Article
- Acetylcholinesterase: Structure, dynamics, and interactions with organophosphorus compounds.Protein science : a publication of the Protein Society · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Acetylcholinesterase (AChE) is an enzyme that hydrolyzes the neurotransmitter acetylcholine (ACh), removing it from the synaptic cleft after the transmission of an electrical signal, making it an essential component of chemical neurotransmission. AChE is a serine hydrolase, containing a catalytic triad of Ser/His/Glu. AChE is a prime target for pharmaceuticals treating a variety of neurological disorders. It is also the target of synthetic organophosphorus (OP) compounds that have been used as pesticides and chemical warfare agents. OP compounds contain a potent leaving group, such as fluorine, and act by forming a covalent adduct with the catalytic serine of the AChE active site. A wealth of structural information is available for AChE, including over 300 structures, including a subset of structures in complex with drugs as well as OP compounds. This review will highlight the interactions between OP compounds and AChE from a structural and computational perspective, with a discussion of access to the active site, as well as side reactions that lead to dealkylation of the OP-catalytic serine adduct, a process known as aging. We conclude that while the majority of the conformational changes needed to accommodate the OP compounds are localized to the acyl loop in the crystal structures, molecular dynamics simulations highlight the potential for a far more dynamic enzyme.
Indexed as
Identifiers
What Socratic holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.