Halliday_2012_Protein.Pept.Lett_19_165

Reference

Title : From protein to peptides: a spectrum of non-hydrolytic functions of acetylcholinesterase - Halliday_2012_Protein.Pept.Lett_19_165
Author(s) : Halliday AC , Greenfield SA
Ref : Protein Pept Lett , 19 :165 , 2012
Abstract :

Acetylcholinesterase (AChE), a member of the alpha/beta-hydrolase fold superfamily of proteins, is a serine hydrolase responsible for the hydrolysis of the well studied neurotransmitter acetylcholine (ACh). However, it is becoming clear that AChE has a range of actions other than this 'classical' role. Non-classical AChE functions have been identified in apoptosis, stress-responses, neuritogenesis, and neurodegeneration. Furthermore, these non-classical roles are attributable not only to the native protein, which appears to act as a mediary binding protein under a number of circumstances, but also to peptides cleaved from the parent protein. Peptides cleaved from AChE can act as independent signalling molecules. Here we discuss the implications of non-hydrolytic functions of this multi-tasking protein.

PubMedSearch : Halliday_2012_Protein.Pept.Lett_19_165
PubMedID: 21933122

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Citations formats

Halliday AC, Greenfield SA (2012)
From protein to peptides: a spectrum of non-hydrolytic functions of acetylcholinesterase
Protein Pept Lett 19 :165

Halliday AC, Greenfield SA (2012)
Protein Pept Lett 19 :165