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 .

TY  - CONF
AU  - Popović, Marija
AU  - Nikolić, Katarina
AU  - Purg, Miha
AU  - Repič, Matej
AU  - Mavri, Janez
PY  - 2013
UR  - https://farfar.pharmacy.bg.ac.rs/handle/123456789/5197
AB  - Monoamineoxidase is mitochondrial flavoenzyme which plays essential role in a regulation of levels of biogenic monoamines in human body. MAO enzyme exists in two forms, MAO A and MAO B, as products of separate genes. Differences between two enzymes caused different therapy indications for MAO inhibitors as modern drugs. ...
PB  - Chemistry and Molecular Sciences and Technologies CM1103
C3  - COST CM1103 Training School, Structure-based drug design for diagnosis and treatment of neurological diseases, 9-13 September 2013 in Istanbul, Turkey
T1  - Determination of pKa values of Tyr residues in the active site of MAO A by performing computational simulations
SP  - 2
UR  - https://hdl.handle.net/21.15107/rcub_farfar_5197
ER  - 

@conference{
author = "Popović, Marija and Nikolić, Katarina and Purg, Miha and Repič, Matej and Mavri, Janez",
year = "2013",
abstract = "Monoamineoxidase is mitochondrial flavoenzyme which plays essential role in a regulation of levels of biogenic monoamines in human body. MAO enzyme exists in two forms, MAO A and MAO B, as products of separate genes. Differences between two enzymes caused different therapy indications for MAO inhibitors as modern drugs. ...",
publisher = "Chemistry and Molecular Sciences and Technologies CM1103",
journal = "COST CM1103 Training School, Structure-based drug design for diagnosis and treatment of neurological diseases, 9-13 September 2013 in Istanbul, Turkey",
title = "Determination of pKa values of Tyr residues in the active site of MAO A by performing computational simulations",
pages = "2",
url = "https://hdl.handle.net/21.15107/rcub_farfar_5197"
}

Popović, M., Nikolić, K., Purg, M., Repič, M.,& Mavri, J.. (2013). Determination of pKa values of Tyr residues in the active site of MAO A by performing computational simulations. in COST CM1103 Training School, Structure-based drug design for diagnosis and treatment of neurological diseases, 9-13 September 2013 in Istanbul, Turkey
Chemistry and Molecular Sciences and Technologies CM1103., 2.
https://hdl.handle.net/21.15107/rcub_farfar_5197

Popović M, Nikolić K, Purg M, Repič M, Mavri J. Determination of pKa values of Tyr residues in the active site of MAO A by performing computational simulations. in COST CM1103 Training School, Structure-based drug design for diagnosis and treatment of neurological diseases, 9-13 September 2013 in Istanbul, Turkey. 2013;:2.
https://hdl.handle.net/21.15107/rcub_farfar_5197 .

Popović, Marija, Nikolić, Katarina, Purg, Miha, Repič, Matej, Mavri, Janez, "Determination of pKa values of Tyr residues in the active site of MAO A by performing computational simulations" in COST CM1103 Training School, Structure-based drug design for diagnosis and treatment of neurological diseases, 9-13 September 2013 in Istanbul, Turkey (2013):2,
https://hdl.handle.net/21.15107/rcub_farfar_5197 .