A new variant of proline-rich membrane anchor (PRiMA) of acetylcholinesterase in chicken: Expression in different muscle fiber types
Author:
Publisher
Elsevier BV
Subject
General Neuroscience
Reference14 articles.
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2. Determinants of the t peptide involved in folding, degradation, and secretion of acetylcholinesterase;Falasca;J. Biol. Chem.,2005
3. Oligomerization of chicken acetylcholinesterase does not require intersubunit disulfide bonds;Gough;J. Neurochem.,1995
4. Differences in expression of acetylcholinesterase and collagen Q control the distribution and oligomerization of the collagen-tailed forms in fast and slow muscles;Krejci;J. Neurosci.,1999
5. Old and new questions about cholinesterases;Massoulié;Chem. Biol. Interact.,2008
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2. Non-neuronal Role of Acetylcholinesterase in Bone Development and Degeneration;Frontiers in Cell and Developmental Biology;2021-01-28
3. Three N-Glycosylation Sites of Human Acetylcholinesterase Shares Similar Glycan Composition;Journal of Molecular Neuroscience;2015-08-01
4. N-linked glycosylation of proline-rich membrane anchor (PRiMA) is not required for assembly and trafficking of globular tetrameric acetylcholinesterase;Neuroscience Letters;2012-08
5. The Assembly of Proline-rich Membrane Anchor (PRiMA)-linked Acetylcholinesterase Enzyme;Journal of Biological Chemistry;2011-09
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