The Experts below are selected from a list of 21 Experts worldwide ranked by ideXlab platform
Raymond Hui - One of the best experts on this subject based on the ideXlab platform.
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T. brucei Hsp83 nucleotide binding pocket.
2013Co-Authors: Juan Carlos Pizarro, Tanya Hills, Guillermo Senisterra, Amy K. Wernimont, Claire Mackenzie, Neil R. Norcross, Michael A. J. Ferguson, Paul G. Wyatt, Ian H. Gilbert, Raymond HuiAbstract:Surface representation in the NTD binding site for the Trypanosoma complex structures (compound 1 complex – cyan; thienopyrimidine Derivative compound 3 – green; Benzamidine Derivative compound 4 – brown). The nucleotide binding pocket of L. major (PDB code 3H80 – Magenta) is shown for comparison purposes.
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T. brucei Hsp83 NTD structural changes.
2013Co-Authors: Juan Carlos Pizarro, Tanya Hills, Guillermo Senisterra, Amy K. Wernimont, Claire Mackenzie, Neil R. Norcross, Michael A. J. Ferguson, Paul G. Wyatt, Ian H. Gilbert, Raymond HuiAbstract:Cartoon representation of α-helices 1, 3 and 4, and the lid region from the Hsp83 in complex with different compounds (compound 1 complex – cyan; thienopyrimidine Derivative compound 3 – green; Benzamidine Derivative compound 4 – brown; and L. major with AMPPNP – magenta). Side chains of residues Asn90 and Asn91 are indicated in sticks, also the nucleotide is indicated as yellow dots to illustrate the location of binding site.
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Crystal structure of T. brucei Hsp83 NTD.
2013Co-Authors: Juan Carlos Pizarro, Tanya Hills, Guillermo Senisterra, Amy K. Wernimont, Claire Mackenzie, Neil R. Norcross, Michael A. J. Ferguson, Paul G. Wyatt, Ian H. Gilbert, Raymond HuiAbstract:(A) A cartoon representation of the parasitic protein, the nucleotide lid region is highlighted in magenta, α-helices 3 and 4 are shown in light green. The ATP mimetic shown to indicate the position of the nucleotide binding site was derived from the L. major complex structure (PBD entry 3H80). (B) NTDs structural overlay between TbHsp83 (cyan) and human αHsp90 (yellow – PDB entry 3QDD). (C) Structural overlay of TbHsp83 NTD inhibitor complexes. Two orthogonal views of ribbon representations of the three complexes and the compounds are indicated as sticks. The structures are colored as follows, compound 1 complex – cyan; thienopyrimidine Derivative compound 3 – green; Benzamidine Derivative compound 4 – brown.
Carsten Werner - One of the best experts on this subject based on the ideXlab platform.
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Immobilization of an anticoagulant Benzamidine Derivative: effect of spacer arms and carrier hydrophobicity on thrombin binding.
Acta biomaterialia, 2005Co-Authors: Katrin Salchert, Marie-françoise Gouzy, Maja Glorius, Anett Kühn, Mirko Nitschke, Carsten WernerAbstract:Prevention of blood coagulation is very often a prerequisite for successful medical devices. For that purpose, passivation of the key coagulation enzyme thrombin through the derivatization of the material's surface with an amidine-based molecule has been found to be promising. To further enhance the efficiency of this approach, thin layers of maleic anhydride copolymers offering different physico-chemical characteristics were tethered with carboxyl terminated polyethylene glycol to covalently immobilize a Benzamidine-type Derivative. The free carboxyl surface groups produced by the attachment of polyethylene glycol (PEG) were quantified by Ag(+) labeling and subsequent XPS detection. The film thickness as well as the carboxyl group content were found to be clearly dependent on the copolymer hydrophobicity and the nature of the PEG molecule. For the assessment of the anchorage of the thrombin to the Benzamidine-Derivative functionalized surfaces, the substrates were immersed in a buffered thrombin solution and the enzyme adsorption was studied using immunostaining/confocal laser scanning microscopy. Higher degrees of thrombin binding were observed for substrates configured with the hydrophilic compared to the more hydrophobic copolymer. Moreover, surface-bound spacers based on alpha,omega-heterobifunctional PEG amino acids (alphaAm,omegaAc-PEG) also enhanced the Benzamidine surface density in comparison to homofunctional PEG diacids (alphaAc,omegaAc-PEG) because of a lower degree of carboxyl inactivation due to PEG 'bridging'. Altogether, the choice of copolymer coatings and the type of PEG spacers were demonstrated to enhance the efficiency of the thrombin scavenging by the covalently immobilized coagulation inhibitor.
Juan Carlos Pizarro - One of the best experts on this subject based on the ideXlab platform.
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T. brucei Hsp83 nucleotide binding pocket.
2013Co-Authors: Juan Carlos Pizarro, Tanya Hills, Guillermo Senisterra, Amy K. Wernimont, Claire Mackenzie, Neil R. Norcross, Michael A. J. Ferguson, Paul G. Wyatt, Ian H. Gilbert, Raymond HuiAbstract:Surface representation in the NTD binding site for the Trypanosoma complex structures (compound 1 complex – cyan; thienopyrimidine Derivative compound 3 – green; Benzamidine Derivative compound 4 – brown). The nucleotide binding pocket of L. major (PDB code 3H80 – Magenta) is shown for comparison purposes.
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T. brucei Hsp83 NTD structural changes.
2013Co-Authors: Juan Carlos Pizarro, Tanya Hills, Guillermo Senisterra, Amy K. Wernimont, Claire Mackenzie, Neil R. Norcross, Michael A. J. Ferguson, Paul G. Wyatt, Ian H. Gilbert, Raymond HuiAbstract:Cartoon representation of α-helices 1, 3 and 4, and the lid region from the Hsp83 in complex with different compounds (compound 1 complex – cyan; thienopyrimidine Derivative compound 3 – green; Benzamidine Derivative compound 4 – brown; and L. major with AMPPNP – magenta). Side chains of residues Asn90 and Asn91 are indicated in sticks, also the nucleotide is indicated as yellow dots to illustrate the location of binding site.
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Crystal structure of T. brucei Hsp83 NTD.
2013Co-Authors: Juan Carlos Pizarro, Tanya Hills, Guillermo Senisterra, Amy K. Wernimont, Claire Mackenzie, Neil R. Norcross, Michael A. J. Ferguson, Paul G. Wyatt, Ian H. Gilbert, Raymond HuiAbstract:(A) A cartoon representation of the parasitic protein, the nucleotide lid region is highlighted in magenta, α-helices 3 and 4 are shown in light green. The ATP mimetic shown to indicate the position of the nucleotide binding site was derived from the L. major complex structure (PBD entry 3H80). (B) NTDs structural overlay between TbHsp83 (cyan) and human αHsp90 (yellow – PDB entry 3QDD). (C) Structural overlay of TbHsp83 NTD inhibitor complexes. Two orthogonal views of ribbon representations of the three complexes and the compounds are indicated as sticks. The structures are colored as follows, compound 1 complex – cyan; thienopyrimidine Derivative compound 3 – green; Benzamidine Derivative compound 4 – brown.
Amy K. Wernimont - One of the best experts on this subject based on the ideXlab platform.
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T. brucei Hsp83 nucleotide binding pocket.
2013Co-Authors: Juan Carlos Pizarro, Tanya Hills, Guillermo Senisterra, Amy K. Wernimont, Claire Mackenzie, Neil R. Norcross, Michael A. J. Ferguson, Paul G. Wyatt, Ian H. Gilbert, Raymond HuiAbstract:Surface representation in the NTD binding site for the Trypanosoma complex structures (compound 1 complex – cyan; thienopyrimidine Derivative compound 3 – green; Benzamidine Derivative compound 4 – brown). The nucleotide binding pocket of L. major (PDB code 3H80 – Magenta) is shown for comparison purposes.
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T. brucei Hsp83 NTD structural changes.
2013Co-Authors: Juan Carlos Pizarro, Tanya Hills, Guillermo Senisterra, Amy K. Wernimont, Claire Mackenzie, Neil R. Norcross, Michael A. J. Ferguson, Paul G. Wyatt, Ian H. Gilbert, Raymond HuiAbstract:Cartoon representation of α-helices 1, 3 and 4, and the lid region from the Hsp83 in complex with different compounds (compound 1 complex – cyan; thienopyrimidine Derivative compound 3 – green; Benzamidine Derivative compound 4 – brown; and L. major with AMPPNP – magenta). Side chains of residues Asn90 and Asn91 are indicated in sticks, also the nucleotide is indicated as yellow dots to illustrate the location of binding site.
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Crystal structure of T. brucei Hsp83 NTD.
2013Co-Authors: Juan Carlos Pizarro, Tanya Hills, Guillermo Senisterra, Amy K. Wernimont, Claire Mackenzie, Neil R. Norcross, Michael A. J. Ferguson, Paul G. Wyatt, Ian H. Gilbert, Raymond HuiAbstract:(A) A cartoon representation of the parasitic protein, the nucleotide lid region is highlighted in magenta, α-helices 3 and 4 are shown in light green. The ATP mimetic shown to indicate the position of the nucleotide binding site was derived from the L. major complex structure (PBD entry 3H80). (B) NTDs structural overlay between TbHsp83 (cyan) and human αHsp90 (yellow – PDB entry 3QDD). (C) Structural overlay of TbHsp83 NTD inhibitor complexes. Two orthogonal views of ribbon representations of the three complexes and the compounds are indicated as sticks. The structures are colored as follows, compound 1 complex – cyan; thienopyrimidine Derivative compound 3 – green; Benzamidine Derivative compound 4 – brown.
Guillermo Senisterra - One of the best experts on this subject based on the ideXlab platform.
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T. brucei Hsp83 nucleotide binding pocket.
2013Co-Authors: Juan Carlos Pizarro, Tanya Hills, Guillermo Senisterra, Amy K. Wernimont, Claire Mackenzie, Neil R. Norcross, Michael A. J. Ferguson, Paul G. Wyatt, Ian H. Gilbert, Raymond HuiAbstract:Surface representation in the NTD binding site for the Trypanosoma complex structures (compound 1 complex – cyan; thienopyrimidine Derivative compound 3 – green; Benzamidine Derivative compound 4 – brown). The nucleotide binding pocket of L. major (PDB code 3H80 – Magenta) is shown for comparison purposes.
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T. brucei Hsp83 NTD structural changes.
2013Co-Authors: Juan Carlos Pizarro, Tanya Hills, Guillermo Senisterra, Amy K. Wernimont, Claire Mackenzie, Neil R. Norcross, Michael A. J. Ferguson, Paul G. Wyatt, Ian H. Gilbert, Raymond HuiAbstract:Cartoon representation of α-helices 1, 3 and 4, and the lid region from the Hsp83 in complex with different compounds (compound 1 complex – cyan; thienopyrimidine Derivative compound 3 – green; Benzamidine Derivative compound 4 – brown; and L. major with AMPPNP – magenta). Side chains of residues Asn90 and Asn91 are indicated in sticks, also the nucleotide is indicated as yellow dots to illustrate the location of binding site.
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Crystal structure of T. brucei Hsp83 NTD.
2013Co-Authors: Juan Carlos Pizarro, Tanya Hills, Guillermo Senisterra, Amy K. Wernimont, Claire Mackenzie, Neil R. Norcross, Michael A. J. Ferguson, Paul G. Wyatt, Ian H. Gilbert, Raymond HuiAbstract:(A) A cartoon representation of the parasitic protein, the nucleotide lid region is highlighted in magenta, α-helices 3 and 4 are shown in light green. The ATP mimetic shown to indicate the position of the nucleotide binding site was derived from the L. major complex structure (PBD entry 3H80). (B) NTDs structural overlay between TbHsp83 (cyan) and human αHsp90 (yellow – PDB entry 3QDD). (C) Structural overlay of TbHsp83 NTD inhibitor complexes. Two orthogonal views of ribbon representations of the three complexes and the compounds are indicated as sticks. The structures are colored as follows, compound 1 complex – cyan; thienopyrimidine Derivative compound 3 – green; Benzamidine Derivative compound 4 – brown.