-
Something wrong with this record ?
Acetylcholinesterases - the structural similarities and differences
J Wiesner, Z Kriz, K Kuca, D Jun, J Koca
Language English Country Great Britain
NLK
Taylor & Francis Open Access
from 2002-01-01
Medline Complete (EBSCOhost)
from 2007-02-01
- MeSH
- Acetylcholinesterase chemistry MeSH
- Drosophila melanogaster metabolism MeSH
- Financing, Organized MeSH
- Protein Conformation MeSH
- Conserved Sequence MeSH
- Humans MeSH
- Evolution, Molecular MeSH
- Molecular Conformation MeSH
- Molecular Sequence Data MeSH
- Mice MeSH
- Protein Folding MeSH
- Amino Acid Sequence MeSH
- Sequence Homology, Amino Acid MeSH
- Signal Transduction MeSH
- Binding Sites MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Mice MeSH
- Animals MeSH
Acetylcholinesterase (AChE) is a widely spread enzyme playing a very important role in nerve signal transmission. 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 (i.e. mosquitoes), one is faced with the question - how much do AChEs differ between species and what are the differences? Here, a theoretical point of view was utilized to identify the structural basis for such differences. The various primary and tertiary alignments show that AChEs are very evolutionary conserved enzymes and this fact could lead to difficulties, for example, in the search for inhibitors specific for a particular species.
- 000
- 02324naa 2200433 a 4500
- 001
- bmc10012711
- 003
- CZ-PrNML
- 005
- 20111210163304.0
- 008
- 100526s2007 xxk e eng||
- 009
- AR
- 040 __
- $a ABA008 $b cze $c ABA008 $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a xxk
- 100 1_
- $a Wiesner, Jiří. $7 _AN049376
- 245 10
- $a Acetylcholinesterases - the structural similarities and differences / $c J Wiesner, Z Kriz, K Kuca, D Jun, J Koca
- 314 __
- $a National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5/A4, 625 00 Brno, Czech Republic.
- 520 9_
- $a Acetylcholinesterase (AChE) is a widely spread enzyme playing a very important role in nerve signal transmission. 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 (i.e. mosquitoes), one is faced with the question - how much do AChEs differ between species and what are the differences? Here, a theoretical point of view was utilized to identify the structural basis for such differences. The various primary and tertiary alignments show that AChEs are very evolutionary conserved enzymes and this fact could lead to difficulties, for example, in the search for inhibitors specific for a particular species.
- 650 _2
- $a acetylcholinesterasa $x chemie $7 D000110
- 650 _2
- $a sekvence aminokyselin $7 D000595
- 650 _2
- $a zvířata $7 D000818
- 650 _2
- $a vazebná místa $7 D001665
- 650 _2
- $a konzervovaná sekvence $7 D017124
- 650 _2
- $a Drosophila melanogaster $x metabolismus $7 D004331
- 650 _2
- $a molekulární evoluce $7 D019143
- 650 _2
- $a lidé $7 D006801
- 650 _2
- $a myši $7 D051379
- 650 _2
- $a molekulární konformace $7 D008968
- 650 _2
- $a molekulární sekvence - údaje $7 D008969
- 650 _2
- $a konformace proteinů $7 D011487
- 650 _2
- $a sbalování proteinů $7 D017510
- 650 _2
- $a sekvenční homologie aminokyselin $7 D017386
- 650 _2
- $a signální transdukce $7 D015398
- 650 _2
- $a financování organizované $7 D005381
- 700 1_
- $a Kříž, Zdeněk $7 xx0068636
- 700 1_
- $a Kuča, Kamil, $d 1978- $7 xx0041831
- 700 1_
- $a Jun, Daniel, $d 1976- $7 xx0040498
- 700 1_
- $a Koča, Jaroslav, $d 1955-2021 $7 jn20000710314
- 773 0_
- $t Journal of Enzyme Inhibition & Medicinal Chemistry $w MED00008009 $g Roč. 22, č. 4 Aug (2007), s. 417-424 $x 1475-6366
- 910 __
- $a ABA008 $b x $y 8
- 990 __
- $a 20100531115819 $b ABA008
- 991 __
- $a 20100916082852 $b ABA008
- 999 __
- $a ok $b bmc $g 726566 $s 589723
- BAS __
- $a 3
- BMC __
- $a 2007 $b 22 $c 4 Aug $d 417-424 $i 1475-6366 $m Journal of enzyme inhibition and medicinal chemistry $n J Enzyme Inhib Med Chem $x MED00008009
- LZP __
- $a 2010-B2/vtme