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Theoretical investigation of the differences in the ionization and hydrophobicity of the MAO A active site with and without serotonin

Authorized Users Only
2015
Authors
Popović, Marija
Purg, Miha
Repič, Matej
Nikolić, Katarina
Mavri, Janez
Conference object (Published version)
Metadata
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Abstract
Monoamine oxidase (MAO) is a mitochondrial flavoenzyme which plays an essential role in the regulation of levels of biogenic monoamines in the human body and exists in two forms, MAO A and MAO B. Differences of two enzymes led to different therapy indications for MAO A and MAO B inhibitors [1]. ...
Source:
COST CM1103 ESR Conference in Belgrade 6th-8th May 2015, Belgrade, Serbia “Computational Chemistry for Neurological Targets”, 2015, 16-
Publisher:
  • COST (European Cooperation in Science and Technology)
Note:
  • Structure-based drug design for diagnosis and treatment of neurological diseases COST CM1103
[ Google Scholar ]
Handle
https://hdl.handle.net/21.15107/rcub_farfar_5019
URI
https://farfar.pharmacy.bg.ac.rs/handle/123456789/5019
Collections
  • Radovi istraživača / Researchers’ publications
Institution/Community
Pharmacy
TY  - CONF
AU  - Popović, Marija
AU  - Purg, Miha
AU  - Repič, Matej
AU  - Nikolić, Katarina
AU  - Mavri, Janez
PY  - 2015
UR  - https://farfar.pharmacy.bg.ac.rs/handle/123456789/5019
AB  - Monoamine oxidase (MAO) is a mitochondrial flavoenzyme which plays an essential role in
the regulation of levels of biogenic monoamines in the human body and exists in two forms,
MAO A and MAO B. Differences of two enzymes led to different therapy indications for
MAO A and MAO B inhibitors [1]. ...
PB  - COST (European Cooperation in Science and Technology)
C3  - COST CM1103 ESR Conference in Belgrade 6th-8th May 2015, Belgrade, Serbia “Computational Chemistry for Neurological Targets”
T1  - Theoretical investigation of the differences in the ionization and hydrophobicity of the MAO A active site with and without serotonin
SP  - 16
UR  - https://hdl.handle.net/21.15107/rcub_farfar_5019
ER  - 
@conference{
author = "Popović, Marija and Purg, Miha and Repič, Matej and Nikolić, Katarina and Mavri, Janez",
year = "2015",
abstract = "Monoamine oxidase (MAO) is a mitochondrial flavoenzyme which plays an essential role in
the regulation of levels of biogenic monoamines in the human body and exists in two forms,
MAO A and MAO B. Differences of two enzymes led to different therapy indications for
MAO A and MAO B inhibitors [1]. ...",
publisher = "COST (European Cooperation in Science and Technology)",
journal = "COST CM1103 ESR Conference in Belgrade 6th-8th May 2015, Belgrade, Serbia “Computational Chemistry for Neurological Targets”",
title = "Theoretical investigation of the differences in the ionization and hydrophobicity of the MAO A active site with and without serotonin",
pages = "16",
url = "https://hdl.handle.net/21.15107/rcub_farfar_5019"
}
Popović, M., Purg, M., Repič, M., Nikolić, K.,& Mavri, J.. (2015). Theoretical investigation of the differences in the ionization and hydrophobicity of the MAO A active site with and without serotonin. in COST CM1103 ESR Conference in Belgrade 6th-8th May 2015, Belgrade, Serbia “Computational Chemistry for Neurological Targets”
COST (European Cooperation in Science and Technology)., 16.
https://hdl.handle.net/21.15107/rcub_farfar_5019
Popović M, Purg M, Repič M, Nikolić K, Mavri J. Theoretical investigation of the differences in the ionization and hydrophobicity of the MAO A active site with and without serotonin. in COST CM1103 ESR Conference in Belgrade 6th-8th May 2015, Belgrade, Serbia “Computational Chemistry for Neurological Targets”. 2015;:16.
https://hdl.handle.net/21.15107/rcub_farfar_5019 .
Popović, Marija, Purg, Miha, Repič, Matej, Nikolić, Katarina, Mavri, Janez, "Theoretical investigation of the differences in the ionization and hydrophobicity of the MAO A active site with and without serotonin" in COST CM1103 ESR Conference in Belgrade 6th-8th May 2015, Belgrade, Serbia “Computational Chemistry for Neurological Targets” (2015):16,
https://hdl.handle.net/21.15107/rcub_farfar_5019 .

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