The Experts below are selected from a list of 171 Experts worldwide ranked by ideXlab platform
Julie A. Krueger - One of the best experts on this subject based on the ideXlab platform.
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Development of an Oxazolopyridine series of dual thrombin/factor Xa inhibitors via structure-guided lead optimization.
Bioorganic & medicinal chemistry letters, 2005Co-Authors: James Z. Deng, Daniel R. Mcmasters, Philippe M.a. Rabbat, Peter D. Williams, Craig A. Coburn, Youwei Yan, Lawrence C. Kuo, S. Dale Lewis, Bobby J. Lucas, Julie A. KruegerAbstract:Thrombin-inhibitor X-ray crystal structures, in combination with the installation of binding elements optimized within the pyrazinone series of thrombin inhibitors, were utilized to transform a weak triazolopyrimidine lead into a series of potent Oxazolopyridines. A modification intended to attenuate plasma protein binding (i.e., conversion of the P3 pyridine to a piperidine) conferred significant factor Xa activity to this series. Ultimately, these dual thrombin/factor Xa inhibitors demonstrated excellent in vitro and in vivo anticoagulant efficacy.
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development of an Oxazolopyridine series of dual thrombin factor xa inhibitors via structure guided lead optimization
Bioorganic & Medicinal Chemistry Letters, 2005Co-Authors: James Z. Deng, Daniel R. Mcmasters, Philippe M.a. Rabbat, Peter D. Williams, Craig A. Coburn, Youwei Yan, Lawrence C. Kuo, Bobby J. Lucas, Dale S Lewis, Julie A. KruegerAbstract:Thrombin-inhibitor X-ray crystal structures, in combination with the installation of binding elements optimized within the pyrazinone series of thrombin inhibitors, were utilized to transform a weak triazolopyrimidine lead into a series of potent Oxazolopyridines. A modification intended to attenuate plasma protein binding (i.e., conversion of the P3 pyridine to a piperidine) conferred significant factor Xa activity to this series. Ultimately, these dual thrombin/factor Xa inhibitors demonstrated excellent in vitro and in vivo anticoagulant efficacy.
James Z. Deng - One of the best experts on this subject based on the ideXlab platform.
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Development of an Oxazolopyridine series of dual thrombin/factor Xa inhibitors via structure-guided lead optimization.
Bioorganic & medicinal chemistry letters, 2005Co-Authors: James Z. Deng, Daniel R. Mcmasters, Philippe M.a. Rabbat, Peter D. Williams, Craig A. Coburn, Youwei Yan, Lawrence C. Kuo, S. Dale Lewis, Bobby J. Lucas, Julie A. KruegerAbstract:Thrombin-inhibitor X-ray crystal structures, in combination with the installation of binding elements optimized within the pyrazinone series of thrombin inhibitors, were utilized to transform a weak triazolopyrimidine lead into a series of potent Oxazolopyridines. A modification intended to attenuate plasma protein binding (i.e., conversion of the P3 pyridine to a piperidine) conferred significant factor Xa activity to this series. Ultimately, these dual thrombin/factor Xa inhibitors demonstrated excellent in vitro and in vivo anticoagulant efficacy.
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development of an Oxazolopyridine series of dual thrombin factor xa inhibitors via structure guided lead optimization
Bioorganic & Medicinal Chemistry Letters, 2005Co-Authors: James Z. Deng, Daniel R. Mcmasters, Philippe M.a. Rabbat, Peter D. Williams, Craig A. Coburn, Youwei Yan, Lawrence C. Kuo, Bobby J. Lucas, Dale S Lewis, Julie A. KruegerAbstract:Thrombin-inhibitor X-ray crystal structures, in combination with the installation of binding elements optimized within the pyrazinone series of thrombin inhibitors, were utilized to transform a weak triazolopyrimidine lead into a series of potent Oxazolopyridines. A modification intended to attenuate plasma protein binding (i.e., conversion of the P3 pyridine to a piperidine) conferred significant factor Xa activity to this series. Ultimately, these dual thrombin/factor Xa inhibitors demonstrated excellent in vitro and in vivo anticoagulant efficacy.
Peter D. Williams - One of the best experts on this subject based on the ideXlab platform.
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Development of an Oxazolopyridine series of dual thrombin/factor Xa inhibitors via structure-guided lead optimization.
Bioorganic & medicinal chemistry letters, 2005Co-Authors: James Z. Deng, Daniel R. Mcmasters, Philippe M.a. Rabbat, Peter D. Williams, Craig A. Coburn, Youwei Yan, Lawrence C. Kuo, S. Dale Lewis, Bobby J. Lucas, Julie A. KruegerAbstract:Thrombin-inhibitor X-ray crystal structures, in combination with the installation of binding elements optimized within the pyrazinone series of thrombin inhibitors, were utilized to transform a weak triazolopyrimidine lead into a series of potent Oxazolopyridines. A modification intended to attenuate plasma protein binding (i.e., conversion of the P3 pyridine to a piperidine) conferred significant factor Xa activity to this series. Ultimately, these dual thrombin/factor Xa inhibitors demonstrated excellent in vitro and in vivo anticoagulant efficacy.
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development of an Oxazolopyridine series of dual thrombin factor xa inhibitors via structure guided lead optimization
Bioorganic & Medicinal Chemistry Letters, 2005Co-Authors: James Z. Deng, Daniel R. Mcmasters, Philippe M.a. Rabbat, Peter D. Williams, Craig A. Coburn, Youwei Yan, Lawrence C. Kuo, Bobby J. Lucas, Dale S Lewis, Julie A. KruegerAbstract:Thrombin-inhibitor X-ray crystal structures, in combination with the installation of binding elements optimized within the pyrazinone series of thrombin inhibitors, were utilized to transform a weak triazolopyrimidine lead into a series of potent Oxazolopyridines. A modification intended to attenuate plasma protein binding (i.e., conversion of the P3 pyridine to a piperidine) conferred significant factor Xa activity to this series. Ultimately, these dual thrombin/factor Xa inhibitors demonstrated excellent in vitro and in vivo anticoagulant efficacy.
Daniel R. Mcmasters - One of the best experts on this subject based on the ideXlab platform.
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Development of an Oxazolopyridine series of dual thrombin/factor Xa inhibitors via structure-guided lead optimization.
Bioorganic & medicinal chemistry letters, 2005Co-Authors: James Z. Deng, Daniel R. Mcmasters, Philippe M.a. Rabbat, Peter D. Williams, Craig A. Coburn, Youwei Yan, Lawrence C. Kuo, S. Dale Lewis, Bobby J. Lucas, Julie A. KruegerAbstract:Thrombin-inhibitor X-ray crystal structures, in combination with the installation of binding elements optimized within the pyrazinone series of thrombin inhibitors, were utilized to transform a weak triazolopyrimidine lead into a series of potent Oxazolopyridines. A modification intended to attenuate plasma protein binding (i.e., conversion of the P3 pyridine to a piperidine) conferred significant factor Xa activity to this series. Ultimately, these dual thrombin/factor Xa inhibitors demonstrated excellent in vitro and in vivo anticoagulant efficacy.
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development of an Oxazolopyridine series of dual thrombin factor xa inhibitors via structure guided lead optimization
Bioorganic & Medicinal Chemistry Letters, 2005Co-Authors: James Z. Deng, Daniel R. Mcmasters, Philippe M.a. Rabbat, Peter D. Williams, Craig A. Coburn, Youwei Yan, Lawrence C. Kuo, Bobby J. Lucas, Dale S Lewis, Julie A. KruegerAbstract:Thrombin-inhibitor X-ray crystal structures, in combination with the installation of binding elements optimized within the pyrazinone series of thrombin inhibitors, were utilized to transform a weak triazolopyrimidine lead into a series of potent Oxazolopyridines. A modification intended to attenuate plasma protein binding (i.e., conversion of the P3 pyridine to a piperidine) conferred significant factor Xa activity to this series. Ultimately, these dual thrombin/factor Xa inhibitors demonstrated excellent in vitro and in vivo anticoagulant efficacy.
Craig A. Coburn - One of the best experts on this subject based on the ideXlab platform.
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Development of an Oxazolopyridine series of dual thrombin/factor Xa inhibitors via structure-guided lead optimization.
Bioorganic & medicinal chemistry letters, 2005Co-Authors: James Z. Deng, Daniel R. Mcmasters, Philippe M.a. Rabbat, Peter D. Williams, Craig A. Coburn, Youwei Yan, Lawrence C. Kuo, S. Dale Lewis, Bobby J. Lucas, Julie A. KruegerAbstract:Thrombin-inhibitor X-ray crystal structures, in combination with the installation of binding elements optimized within the pyrazinone series of thrombin inhibitors, were utilized to transform a weak triazolopyrimidine lead into a series of potent Oxazolopyridines. A modification intended to attenuate plasma protein binding (i.e., conversion of the P3 pyridine to a piperidine) conferred significant factor Xa activity to this series. Ultimately, these dual thrombin/factor Xa inhibitors demonstrated excellent in vitro and in vivo anticoagulant efficacy.
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development of an Oxazolopyridine series of dual thrombin factor xa inhibitors via structure guided lead optimization
Bioorganic & Medicinal Chemistry Letters, 2005Co-Authors: James Z. Deng, Daniel R. Mcmasters, Philippe M.a. Rabbat, Peter D. Williams, Craig A. Coburn, Youwei Yan, Lawrence C. Kuo, Bobby J. Lucas, Dale S Lewis, Julie A. KruegerAbstract:Thrombin-inhibitor X-ray crystal structures, in combination with the installation of binding elements optimized within the pyrazinone series of thrombin inhibitors, were utilized to transform a weak triazolopyrimidine lead into a series of potent Oxazolopyridines. A modification intended to attenuate plasma protein binding (i.e., conversion of the P3 pyridine to a piperidine) conferred significant factor Xa activity to this series. Ultimately, these dual thrombin/factor Xa inhibitors demonstrated excellent in vitro and in vivo anticoagulant efficacy.
