Computer Modeling of Enzyme Catalysis and Inhibition: A Study on ODCase Catalysis and Protein Kinase C Inhibition
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Computer Modeling of Enzyme Catalysis and Inhibition
DE PB NWISBN: 9783639125016 bzw. 3639125010, in Deutsch, Vdm Verlag Dr. Müller, Taschenbuch, neu.
Lieferung aus: Deutschland, Versandkostenfrei.
buecher.de GmbH & Co. KG, [1].
Computer modeling techniques have been extensively used to aid drug design via enzymatic reaction studies. Here we present the investigations of the catalysis by orotidine monophosphate decarboxylase (ODCase) and the inhibition of protein kinase C (PKC) isozymes. Decarboxylation, pseudohydrolysis and covalent inhibition reactions were studied using QM and QM/MM methods to understand the mechanistic details of ODCase catalysis. The catalytic site architecture and binding interactions of PKC isozymes a, ß and were also investigated in the context of PKC-ß inhibitor, ruboxistaurin. Homology modeling and docking techniques were used to model the three-dimensional structures of the kinase domains of PKC isozymes and the PKC-ruboxistaurin complexes. For the first time, specific interactions for ruboxistaurin that favor binding to PKC-ß were uncovered. Our study provides opportunity to design isozyme-specific inhibitors for PKC.2009. 92 S. 220 mmVersandfertig in 3-5 Tagen, Softcover.
buecher.de GmbH & Co. KG, [1].
Computer modeling techniques have been extensively used to aid drug design via enzymatic reaction studies. Here we present the investigations of the catalysis by orotidine monophosphate decarboxylase (ODCase) and the inhibition of protein kinase C (PKC) isozymes. Decarboxylation, pseudohydrolysis and covalent inhibition reactions were studied using QM and QM/MM methods to understand the mechanistic details of ODCase catalysis. The catalytic site architecture and binding interactions of PKC isozymes a, ß and were also investigated in the context of PKC-ß inhibitor, ruboxistaurin. Homology modeling and docking techniques were used to model the three-dimensional structures of the kinase domains of PKC isozymes and the PKC-ruboxistaurin complexes. For the first time, specific interactions for ruboxistaurin that favor binding to PKC-ß were uncovered. Our study provides opportunity to design isozyme-specific inhibitors for PKC.2009. 92 S. 220 mmVersandfertig in 3-5 Tagen, Softcover.
2
Computer Modeling of Enzyme Catalysis and Inhibition
DE PB NWISBN: 9783639125016 bzw. 3639125010, in Deutsch, Vdm Verlag Dr. Müller, Taschenbuch, neu.
Lieferung aus: Deutschland, Versandkostenfrei.
buecher.de GmbH & Co. KG, [1].
Computer modeling techniques have been extensively used to aid drug design via enzymatic reaction studies. Here we present the investigations of the catalysis by orotidine monophosphate decarboxylase (ODCase) and the inhibition of protein kinase C (PKC) isozymes. Decarboxylation, pseudohydrolysis and covalent inhibition reactions were studied using QM and QM/MM methods to understand the mechanistic details of ODCase catalysis. The catalytic site architecture and binding interactions of PKC isozymes a, ß and were also investigated in the context of PKC-ß inhibitor, ruboxistaurin. Homology modeling and docking techniques were used to model the three-dimensional structures of the kinase domains of PKC isozymes and the PKC-ruboxistaurin complexes. For the first time, specific interactions for ruboxistaurin that favor binding to PKC-ß were uncovered. Our study provides opportunity to design isozyme-specific inhibitors for PKC.2009. 92 S. 220 mmVersandfertig in 3-5 Tagen, Softcover.
buecher.de GmbH & Co. KG, [1].
Computer modeling techniques have been extensively used to aid drug design via enzymatic reaction studies. Here we present the investigations of the catalysis by orotidine monophosphate decarboxylase (ODCase) and the inhibition of protein kinase C (PKC) isozymes. Decarboxylation, pseudohydrolysis and covalent inhibition reactions were studied using QM and QM/MM methods to understand the mechanistic details of ODCase catalysis. The catalytic site architecture and binding interactions of PKC isozymes a, ß and were also investigated in the context of PKC-ß inhibitor, ruboxistaurin. Homology modeling and docking techniques were used to model the three-dimensional structures of the kinase domains of PKC isozymes and the PKC-ruboxistaurin complexes. For the first time, specific interactions for ruboxistaurin that favor binding to PKC-ß were uncovered. Our study provides opportunity to design isozyme-specific inhibitors for PKC.2009. 92 S. 220 mmVersandfertig in 3-5 Tagen, Softcover.
3
Symbolbild
Computer Modeling of Enzyme Catalysis and Inhibition (2009)
DE PB NW RPISBN: 9783639125016 bzw. 3639125010, in Deutsch, Vdm Verlag Apr 2009, Taschenbuch, neu, Nachdruck.
Von Händler/Antiquariat, AHA-BUCH GmbH [51283250], Einbeck, NDS, Germany.
This item is printed on demand - Print on Demand Titel. - Computer modeling techniques have been extensively used to aid drug design via enzymatic reaction studies. Here we present the investigations of the catalysis by orotidine monophosphate decarboxylase (ODCase) and the inhibition of protein kinase C (PKC) isozymes. Decarboxylation, pseudohydrolysis and covalent inhibition reactions were studied using QM and QM/MM methods to understand the mechanistic details of ODCase catalysis. The catalytic site architecture and binding interactions of PKC isozymes , and were also investigated in the context of PKC- inhibitor, ruboxistaurin. Homology modeling and docking techniques were used to model the three-dimensional structures of the kinase domains of PKC isozymes and the PKC-ruboxistaurin complexes. For the first time, specific interactions for ruboxistaurin that favor binding to PKC- were uncovered. Our study provides opportunity to design isozyme-specific inhibitors for PKC. 92 pp. Englisch.
This item is printed on demand - Print on Demand Titel. - Computer modeling techniques have been extensively used to aid drug design via enzymatic reaction studies. Here we present the investigations of the catalysis by orotidine monophosphate decarboxylase (ODCase) and the inhibition of protein kinase C (PKC) isozymes. Decarboxylation, pseudohydrolysis and covalent inhibition reactions were studied using QM and QM/MM methods to understand the mechanistic details of ODCase catalysis. The catalytic site architecture and binding interactions of PKC isozymes , and were also investigated in the context of PKC- inhibitor, ruboxistaurin. Homology modeling and docking techniques were used to model the three-dimensional structures of the kinase domains of PKC isozymes and the PKC-ruboxistaurin complexes. For the first time, specific interactions for ruboxistaurin that favor binding to PKC- were uncovered. Our study provides opportunity to design isozyme-specific inhibitors for PKC. 92 pp. Englisch.
4
Computer Modeling of Enzyme Catalysis and Inhibition: A Study on ODCase Catalysis and Protein Kinase C Inhibition (2009)
EN PB NWISBN: 9783639125016 bzw. 3639125010, in Englisch, 92 Seiten, VDM Verlag, Taschenbuch, neu.
Lieferung aus: Vereinigte Staaten von Amerika, Usually ships in 24 hours.
Von Händler/Antiquariat, Amazon.com.
Computer modeling techniques have been extensively used to aid drug design via enzymatic reaction studies. Here we present the investigations of the catalysis by orotidine monophosphate decarboxylase (ODCase) and the inhibition of protein kinase C (PKC) isozymes. Decarboxylation, pseudohydrolysis and covalent inhibition reactions were studied using QM and QM/MM methods to understand the mechanistic details of ODCase catalysis. The catalytic site architecture and binding interactions of PKC isozymes ?, ? and ? were also investigated in the context of PKC-? inhibitor, ruboxistaurin. Homology modeling and docking techniques were used to model the three-dimensional structures of the kinase domains of PKC isozymes and the PKC-ruboxistaurin complexes. For the first time, specific interactions for ruboxistaurin that favor binding to PKC-? were uncovered. Our study provides opportunity to design isozyme-specific inhibitors for PKC. Paperback, Label: VDM Verlag, VDM Verlag, Produktgruppe: Book, Publiziert: 2009-04-03, Studio: VDM Verlag.
Von Händler/Antiquariat, Amazon.com.
Computer modeling techniques have been extensively used to aid drug design via enzymatic reaction studies. Here we present the investigations of the catalysis by orotidine monophosphate decarboxylase (ODCase) and the inhibition of protein kinase C (PKC) isozymes. Decarboxylation, pseudohydrolysis and covalent inhibition reactions were studied using QM and QM/MM methods to understand the mechanistic details of ODCase catalysis. The catalytic site architecture and binding interactions of PKC isozymes ?, ? and ? were also investigated in the context of PKC-? inhibitor, ruboxistaurin. Homology modeling and docking techniques were used to model the three-dimensional structures of the kinase domains of PKC isozymes and the PKC-ruboxistaurin complexes. For the first time, specific interactions for ruboxistaurin that favor binding to PKC-? were uncovered. Our study provides opportunity to design isozyme-specific inhibitors for PKC. Paperback, Label: VDM Verlag, VDM Verlag, Produktgruppe: Book, Publiziert: 2009-04-03, Studio: VDM Verlag.
5
Symbolbild
Computer Modeling of Enzyme Catalysis and Inhibition (2009)
DE PB NW RPISBN: 9783639125016 bzw. 3639125010, in Deutsch, VDM Verlag Dr. Müller, Saarbrücken, Deutschland, Taschenbuch, neu, Nachdruck.
Von Händler/Antiquariat, English-Book-Service - A Fine Choice [1048135], Waldshut-Tiengen, Germany.
This item is printed on demand for shipment within 3 working days.
This item is printed on demand for shipment within 3 working days.
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