ReviewJournal of neurochemistry2021
Cryo-electron microscopy of cholinesterases, present and future.
Review in Journal of neurochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
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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.
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Who cites it
8 citing papers in PubMed.
- GLP-1 receptor agonists in neurological diseases: mechanisms and therapeutic prospects from metabolism to neuroprotection.Frontiers in immunology · 2026Review
- Histone H4K16 acetylation modification regulated autophagy and apoptosis in neuron after spinal cord injury.Scientific reports · 2025Article
- Acetylcholinesterase as a Multifunctional Target in Amyloid-Driven Neurodegeneration: From Dual-Site Inhibitors to Anti-Agregation Strategies.International journal of molecular sciences · 2025Review
- Advances in Cellular and Molecular Biology Assays: A Review of Gold Standard Methods.International journal of innovative science and research technology · 2025Article
- A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization.Biomolecules · 2023Review
- Activation/Inhibition of Cholinesterases by Excess Substrate: Interpretation of the PhenomenologicalInternational journal of molecular sciences · 2023Article
- Identification and molecular characterization of propionylcholinesterase, a novel pseudocholinesterase in rice.Plant signaling & behavior · 2021Article
- Cryo-electron microscopy of cholinesterases, present and future.Journal of neurochemistry · 2021Review
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) exist in a variety of oligomeric forms, each with defined cellular and subcellular distributions. Although crystal structures of AChE and BChE have been available for many years, structures of the physiologically relevant ChE tetramer were only recently solved by cryo-electron microscopy (cryo-EM) single-particle analysis. Here, we briefly review how these structures contribute to our understanding of cholinesterase oligomerization, highlighting the advantages of using cryo-EM to resolve structures of protein assemblies that cannot be expressed recombinantly. We argue that the next frontier in cholinesterase structural biology is to image membrane-anchored ChE oligomers directly in their native environment-the cell.
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Registered trials
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