Molecular structure of acetylcholinesterase

Israel Silman

doi:10.1016/S0968-0004(76)80096-5

Molecular structure of acetylcholinesterase

Israel Silman^*

^*Corresponding author for this work

Department of Brain Sciences

Research output: Contribution to journal › Review article › peer-review

18 Citations (Scopus)

Abstract

Electric eel acetylcholinesterase is a complex molecular structure in which a multisubunit head bearing the active sites of the enzyme is attached to an elongated tail. Recent evidence suggests that the tail is of a collagenous nature and that in situ acetylcholinesterase is associated with the collagenous matrix of the basement membrane.

Original language	English
Pages (from-to)	225-227
Number of pages	3
Journal	Trends in Biochemical Sciences
Volume	1
Issue number	4
DOIs	https://doi.org/10.1016/S0968-0004(76)80096-5
Publication status	Published - Dec 1976

All Science Journal Classification (ASJC) codes

Molecular Biology
Biochemistry

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10.1016/S0968-0004(76)80096-5

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title = "Molecular structure of acetylcholinesterase",

abstract = "Electric eel acetylcholinesterase is a complex molecular structure in which a multisubunit head bearing the active sites of the enzyme is attached to an elongated tail. Recent evidence suggests that the tail is of a collagenous nature and that in situ acetylcholinesterase is associated with the collagenous matrix of the basement membrane.",

author = "Israel Silman",

year = "1976",

month = dec,

doi = "10.1016/S0968-0004(76)80096-5",

language = "English",

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AU - Silman, Israel

PY - 1976/12

Y1 - 1976/12

N2 - Electric eel acetylcholinesterase is a complex molecular structure in which a multisubunit head bearing the active sites of the enzyme is attached to an elongated tail. Recent evidence suggests that the tail is of a collagenous nature and that in situ acetylcholinesterase is associated with the collagenous matrix of the basement membrane.

AB - Electric eel acetylcholinesterase is a complex molecular structure in which a multisubunit head bearing the active sites of the enzyme is attached to an elongated tail. Recent evidence suggests that the tail is of a collagenous nature and that in situ acetylcholinesterase is associated with the collagenous matrix of the basement membrane.

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U2 - 10.1016/S0968-0004(76)80096-5

DO - 10.1016/S0968-0004(76)80096-5

M3 - Review article

SN - 0968-0004

VL - 1

SP - 225

EP - 227

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

IS - 4

ER -

Molecular structure of acetylcholinesterase

Abstract

All Science Journal Classification (ASJC) codes

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