The Experts below are selected from a list of 15504 Experts worldwide ranked by ideXlab platform
Jarl E. S. Wikberg - One of the best experts on this subject based on the ideXlab platform.
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Development of proteo-chemometrics: a novel technology for the analysis of Drug-Receptor Interactions.
Biochimica et biophysica acta, 2001Co-Authors: Maris Lapinsh, Peteris Prusis, Alexandrs Gutcaits, Torbjörn Lundstedt, Jarl E. S. WikbergAbstract:A novel method for the analysis of Drug Receptor Interactions has been developed and used to explore mechanisms involved in the binding of 4-piperidyl oxazole antagonists to alpha1a-, alpha1b- and alpha1d-adrenoceptors. The method exploits affinity data for a series of organic chemical compounds binding to wild-type and artificially mutated Receptors. The Receptor sequences and compounds are assigned predictor variables that are correlated to the measured pharmacological activities using partial least-squares projections to latent structures. The predictor variables consist of one descriptor block derived from the chemical properties of the Receptors' primary amino acid sequences and another descriptor block derived from the chemical properties of the organic compounds. The cross-terms generated from the two descriptor blocks are also derived. Using this approach, very sturdy models were generated describing the Interactions of the chemical compounds with the Receptors. Models are useful to predict binding affinity and Receptor subtype selectivity of compounds prior to their synthesis, and may find use in rational Drug design. Moreover, models also give quantitative information about the Interactions of the amino acids of the Receptors with the ligands, thereby giving an insight into the molecular mechanisms involved in ligand binding.
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Development of proteo-chemometrics: a novel technology for the analysis of Drug-Receptor Interactions
Biochimica et Biophysica Acta, 2001Co-Authors: Maris Lapinsh, Peteris Prusis, Alexandrs Gutcaits, Torbjörn Lundstedt, Jarl E. S. WikbergAbstract:Development of proteo-chemometrics: a novel technology for the analysis of Drug-Receptor Interactions.
Maris Lapinsh - One of the best experts on this subject based on the ideXlab platform.
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Development of proteo-chemometrics: a novel technology for the analysis of Drug-Receptor Interactions.
Biochimica et biophysica acta, 2001Co-Authors: Maris Lapinsh, Peteris Prusis, Alexandrs Gutcaits, Torbjörn Lundstedt, Jarl E. S. WikbergAbstract:A novel method for the analysis of Drug Receptor Interactions has been developed and used to explore mechanisms involved in the binding of 4-piperidyl oxazole antagonists to alpha1a-, alpha1b- and alpha1d-adrenoceptors. The method exploits affinity data for a series of organic chemical compounds binding to wild-type and artificially mutated Receptors. The Receptor sequences and compounds are assigned predictor variables that are correlated to the measured pharmacological activities using partial least-squares projections to latent structures. The predictor variables consist of one descriptor block derived from the chemical properties of the Receptors' primary amino acid sequences and another descriptor block derived from the chemical properties of the organic compounds. The cross-terms generated from the two descriptor blocks are also derived. Using this approach, very sturdy models were generated describing the Interactions of the chemical compounds with the Receptors. Models are useful to predict binding affinity and Receptor subtype selectivity of compounds prior to their synthesis, and may find use in rational Drug design. Moreover, models also give quantitative information about the Interactions of the amino acids of the Receptors with the ligands, thereby giving an insight into the molecular mechanisms involved in ligand binding.
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Development of proteo-chemometrics: a novel technology for the analysis of Drug-Receptor Interactions
Biochimica et Biophysica Acta, 2001Co-Authors: Maris Lapinsh, Peteris Prusis, Alexandrs Gutcaits, Torbjörn Lundstedt, Jarl E. S. WikbergAbstract:Development of proteo-chemometrics: a novel technology for the analysis of Drug-Receptor Interactions.
Serdar Durdagi - One of the best experts on this subject based on the ideXlab platform.
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modeling and protein engineering studies of active and inactive states of human dopamine d2 Receptor d2r and investigation of Drug Receptor Interactions
Molecular Diversity, 2015Co-Authors: Ramin Ekhteiari Salmas, Mine Yurtsever, Matthias Stein, Serdar DurdagiAbstract:Homology model structures of the dopamine D2 Receptor (D2R) were generated starting from the active and inactive states of \(\upbeta \)2-adrenergic crystal structure templates. To the best of our knowledge, the active conformation of D2R was modeled for the first time in this study. The homology models are built and refined using MODELLER and ROSETTA programs. Top-ranked models have been validated with ligand docking simulations and in silico Alanine-scanning mutagenesis studies. The derived extra-cellular loop region of the protein models is directed toward the binding site cavity which is often involved in ligand binding. The binding sites of protein models were refined using induced fit docking to enable the side-chain refinement during ligand docking simulations. The derived models were then tested using molecular modeling techniques on several marketed Drugs for schizophrenia. Alanine-scanning mutagenesis and molecular docking studies gave similar results for marketed Drugs tested. We believe that these new D2 Receptor models will be very useful for a better understanding of the mechanisms of action of Drugs to be targeted to the binding sites of D2Rs and they will contribute significantly to Drug design studies involving G-protein-coupled Receptors in the future.
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modeling and protein engineering studies of active and inactive states of human dopamine d2 Receptor d2r and investigation of Drug Receptor Interactions
Molecular Diversity, 2015Co-Authors: Ramin Ekhteiari Salmas, Mine Yurtsever, Matthias Stein, Serdar DurdagiAbstract:Homology model structures of the dopamine D2 Receptor (D2R) were generated starting from the active and inactive states of \(\upbeta \)2-adrenergic crystal structure templates. To the best of our knowledge, the active conformation of D2R was modeled for the first time in this study. The homology models are built and refined using MODELLER and ROSETTA programs. Top-ranked models have been validated with ligand docking simulations and in silico Alanine-scanning mutagenesis studies. The derived extra-cellular loop region of the protein models is directed toward the binding site cavity which is often involved in ligand binding. The binding sites of protein models were refined using induced fit docking to enable the side-chain refinement during ligand docking simulations. The derived models were then tested using molecular modeling techniques on several marketed Drugs for schizophrenia. Alanine-scanning mutagenesis and molecular docking studies gave similar results for marketed Drugs tested. We believe that these new D2 Receptor models will be very useful for a better understanding of the mechanisms of action of Drugs to be targeted to the binding sites of D2Rs and they will contribute significantly to Drug design studies involving G-protein-coupled Receptors in the future.
Torbjörn Lundstedt - One of the best experts on this subject based on the ideXlab platform.
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Development of proteo-chemometrics: a novel technology for the analysis of Drug-Receptor Interactions.
Biochimica et biophysica acta, 2001Co-Authors: Maris Lapinsh, Peteris Prusis, Alexandrs Gutcaits, Torbjörn Lundstedt, Jarl E. S. WikbergAbstract:A novel method for the analysis of Drug Receptor Interactions has been developed and used to explore mechanisms involved in the binding of 4-piperidyl oxazole antagonists to alpha1a-, alpha1b- and alpha1d-adrenoceptors. The method exploits affinity data for a series of organic chemical compounds binding to wild-type and artificially mutated Receptors. The Receptor sequences and compounds are assigned predictor variables that are correlated to the measured pharmacological activities using partial least-squares projections to latent structures. The predictor variables consist of one descriptor block derived from the chemical properties of the Receptors' primary amino acid sequences and another descriptor block derived from the chemical properties of the organic compounds. The cross-terms generated from the two descriptor blocks are also derived. Using this approach, very sturdy models were generated describing the Interactions of the chemical compounds with the Receptors. Models are useful to predict binding affinity and Receptor subtype selectivity of compounds prior to their synthesis, and may find use in rational Drug design. Moreover, models also give quantitative information about the Interactions of the amino acids of the Receptors with the ligands, thereby giving an insight into the molecular mechanisms involved in ligand binding.
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Development of proteo-chemometrics: a novel technology for the analysis of Drug-Receptor Interactions
Biochimica et Biophysica Acta, 2001Co-Authors: Maris Lapinsh, Peteris Prusis, Alexandrs Gutcaits, Torbjörn Lundstedt, Jarl E. S. WikbergAbstract:Development of proteo-chemometrics: a novel technology for the analysis of Drug-Receptor Interactions.
Alexandrs Gutcaits - One of the best experts on this subject based on the ideXlab platform.
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Development of proteo-chemometrics: a novel technology for the analysis of Drug-Receptor Interactions.
Biochimica et biophysica acta, 2001Co-Authors: Maris Lapinsh, Peteris Prusis, Alexandrs Gutcaits, Torbjörn Lundstedt, Jarl E. S. WikbergAbstract:A novel method for the analysis of Drug Receptor Interactions has been developed and used to explore mechanisms involved in the binding of 4-piperidyl oxazole antagonists to alpha1a-, alpha1b- and alpha1d-adrenoceptors. The method exploits affinity data for a series of organic chemical compounds binding to wild-type and artificially mutated Receptors. The Receptor sequences and compounds are assigned predictor variables that are correlated to the measured pharmacological activities using partial least-squares projections to latent structures. The predictor variables consist of one descriptor block derived from the chemical properties of the Receptors' primary amino acid sequences and another descriptor block derived from the chemical properties of the organic compounds. The cross-terms generated from the two descriptor blocks are also derived. Using this approach, very sturdy models were generated describing the Interactions of the chemical compounds with the Receptors. Models are useful to predict binding affinity and Receptor subtype selectivity of compounds prior to their synthesis, and may find use in rational Drug design. Moreover, models also give quantitative information about the Interactions of the amino acids of the Receptors with the ligands, thereby giving an insight into the molecular mechanisms involved in ligand binding.
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Development of proteo-chemometrics: a novel technology for the analysis of Drug-Receptor Interactions
Biochimica et Biophysica Acta, 2001Co-Authors: Maris Lapinsh, Peteris Prusis, Alexandrs Gutcaits, Torbjörn Lundstedt, Jarl E. S. WikbergAbstract:Development of proteo-chemometrics: a novel technology for the analysis of Drug-Receptor Interactions.
