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@article{707230,
author = {Wiesner, Jiří and Kříž, Zdeněk and Kuča, Kamil and Jun, Daniel and Koča, Jaroslav},
article_location = {UK},
article_number = {4},
keywords = {computational chemistry;computer modeling;acetycholinesterase;AChE;species;alignment},
language = {eng},
issn = {1475-6366},
journal = {Journal of Enzyme Inhibition and Medicinal Chemistry},
title = {Acetylcholinesterases - the similarities and differences},
volume = {22},
year = {2007}
}
TY - JOUR
ID - 707230
AU - Wiesner, Jiří - Kříž, Zdeněk - Kuča, Kamil - Jun, Daniel - Koča, Jaroslav
PY - 2007
TI - Acetylcholinesterases - the similarities and differences
JF - Journal of Enzyme Inhibition and Medicinal Chemistry
VL - 22
IS - 4
SP - 417-424
EP - 417-424
PB - Taylor & Francis
SN - 14756366
KW - computational chemistry;computer modeling;acetycholinesterase;AChE;species;alignment
N2 - Acetylcholinesterase (AChE) is a widely spread enzyme playing a very important role in nerve signal transmission. There are several reasons as to why this enzyme is studied, one of them is the treatment of Alzheimers disease. As AChE controls key processes, its inhibition leads to the very fast death of an organism, including humans. However, when this feature is to be used for killing of unwanted organisms (like mosquitoes), one is faced with the question - how much does AChEs differ between species and what are the differences? In this article, the structural point of view was utilized to answer the above questions. The various primary and tertiary alignments show that AChEs are very evolutionary conserved enzymes and this fact leads to difficulties in the search for inhibitors specific for a particular species.
ER -
WIESNER, Jiří, Zdeněk KŘÍŽ, Kamil KUČA, Daniel JUN and Jaroslav KOČA. Acetylcholinesterases - the similarities and differences. \textit{Journal of Enzyme Inhibition and Medicinal Chemistry}. UK: Taylor \&{} Francis, 2007, vol.~22, No~4, p.~417-424. ISSN~1475-6366.
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