Assembly and regulation of acetylcholinesterase at the vertebrate neuromuscular junction.

@article{Rotundo2008AssemblyAR,
  title={Assembly and regulation of acetylcholinesterase at the vertebrate neuromuscular junction.},
  author={Richard L. Rotundo and C. Aquino Ruiz and Emilio Gerardo Mart{\'i}nez Marrero and Lewis M Kimbell and Susana G. Rossi and Terrone L. Rosenberry and Andrew J. Darr and Pantelis Tsoulfas},
  journal={Chemico-biological interactions},
  year={2008},
  volume={175 1-3},
  pages={
          26-9
        }
}
The collagen-tailed form of acetylcholinesterase (ColQ-AChE) is the major if not unique form of the enzyme associated with the neuromuscular junction (NMJ). This enzyme form consists of catalytic and non-catalytic subunits encoded by separate genes, assembled as three enzymatic tetramers attached to the three-stranded collagen-like tail (ColQ). This synaptic form of the enzyme is tightly attached to the basal lamina associated with the glycosaminoglycan perlecan. Fasciculin-2 is a snake toxin… CONTINUE READING
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