three-dimensional structural model for agps Search Results


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ATCC pseudomonas sp
Sequence alignment of the cloned BDH gene from <t>Pseudomonas</t> sp. ATCC17453 with BDH from Pseudomonas sp. TCU-HL1 (Tsang et al. ) using ClustalW 1.7. Identical amino acids are marked with *. Active site amino acids are in bold
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Sequence alignment of the cloned BDH gene from <t>Pseudomonas</t> sp. ATCC17453 with BDH from Pseudomonas sp. TCU-HL1 (Tsang et al. ) using ClustalW 1.7. Identical amino acids are marked with *. Active site amino acids are in bold
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Sequence alignment of the cloned BDH gene from <t>Pseudomonas</t> sp. ATCC17453 with BDH from Pseudomonas sp. TCU-HL1 (Tsang et al. ) using ClustalW 1.7. Identical amino acids are marked with *. Active site amino acids are in bold
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Sequence alignment of the cloned BDH gene from <t>Pseudomonas</t> sp. ATCC17453 with BDH from Pseudomonas sp. TCU-HL1 (Tsang et al. ) using ClustalW 1.7. Identical amino acids are marked with *. Active site amino acids are in bold
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Sequence alignment of the cloned BDH gene from <t>Pseudomonas</t> sp. ATCC17453 with BDH from Pseudomonas sp. TCU-HL1 (Tsang et al. ) using ClustalW 1.7. Identical amino acids are marked with *. Active site amino acids are in bold
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Federation of European Neuroscience Societies structural model
Sequence alignment of the cloned BDH gene from <t>Pseudomonas</t> sp. ATCC17453 with BDH from Pseudomonas sp. TCU-HL1 (Tsang et al. ) using ClustalW 1.7. Identical amino acids are marked with *. Active site amino acids are in bold
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Tripos Inc sybyl 7.0
Sequence alignment of the cloned BDH gene from <t>Pseudomonas</t> sp. ATCC17453 with BDH from Pseudomonas sp. TCU-HL1 (Tsang et al. ) using ClustalW 1.7. Identical amino acids are marked with *. Active site amino acids are in bold
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Inte Ligand three-dimensional mpo structure models
Sequence alignment of the cloned BDH gene from <t>Pseudomonas</t> sp. ATCC17453 with BDH from Pseudomonas sp. TCU-HL1 (Tsang et al. ) using ClustalW 1.7. Identical amino acids are marked with *. Active site amino acids are in bold
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(a) Schematic diagram indicating the time course of the experimental procedure. (b) Flow chart of the experimental groups. KCl: potassium chloride; CA: cardiac arrest; CPR: cardiopulmonary resuscitation; Echo: <t>echocardiography;</t> TEM: transmission electron microscopy; Vehicle: mice subjected to CA/CPR treated with normal saline; Sal B: salvianolic acid B; n : number of mice; ROSC: return of spontaneous circulation; h: hours; min: minutes; EF: ejection fraction; FS: fractional shortening; DHE: dihydroethidium; H&E: hematoxylin-eosin; TUNEL: terminal dUTP nick-end labeling; NADPH: nicotinamide adenine dinucleotide phosphate.
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ARTEC CO LTD structured-light scanner artec eva
(a) Schematic diagram indicating the time course of the experimental procedure. (b) Flow chart of the experimental groups. KCl: potassium chloride; CA: cardiac arrest; CPR: cardiopulmonary resuscitation; Echo: <t>echocardiography;</t> TEM: transmission electron microscopy; Vehicle: mice subjected to CA/CPR treated with normal saline; Sal B: salvianolic acid B; n : number of mice; ROSC: return of spontaneous circulation; h: hours; min: minutes; EF: ejection fraction; FS: fractional shortening; DHE: dihydroethidium; H&E: hematoxylin-eosin; TUNEL: terminal dUTP nick-end labeling; NADPH: nicotinamide adenine dinucleotide phosphate.
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Hypogen Inc 3d-qsar pharmacophore
(a) Schematic diagram indicating the time course of the experimental procedure. (b) Flow chart of the experimental groups. KCl: potassium chloride; CA: cardiac arrest; CPR: cardiopulmonary resuscitation; Echo: <t>echocardiography;</t> TEM: transmission electron microscopy; Vehicle: mice subjected to CA/CPR treated with normal saline; Sal B: salvianolic acid B; n : number of mice; ROSC: return of spontaneous circulation; h: hours; min: minutes; EF: ejection fraction; FS: fractional shortening; DHE: dihydroethidium; H&E: hematoxylin-eosin; TUNEL: terminal dUTP nick-end labeling; NADPH: nicotinamide adenine dinucleotide phosphate.
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Autodesk Inc 3d structural model
(a) Schematic diagram indicating the time course of the experimental procedure. (b) Flow chart of the experimental groups. KCl: potassium chloride; CA: cardiac arrest; CPR: cardiopulmonary resuscitation; Echo: <t>echocardiography;</t> TEM: transmission electron microscopy; Vehicle: mice subjected to CA/CPR treated with normal saline; Sal B: salvianolic acid B; n : number of mice; ROSC: return of spontaneous circulation; h: hours; min: minutes; EF: ejection fraction; FS: fractional shortening; DHE: dihydroethidium; H&E: hematoxylin-eosin; TUNEL: terminal dUTP nick-end labeling; NADPH: nicotinamide adenine dinucleotide phosphate.
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Image Search Results


Sequence alignment of the cloned BDH gene from Pseudomonas sp. ATCC17453 with BDH from Pseudomonas sp. TCU-HL1 (Tsang et al. ) using ClustalW 1.7. Identical amino acids are marked with *. Active site amino acids are in bold

Journal: Applied Microbiology and Biotechnology

Article Title: Engineering of a borneol dehydrogenase from P. putida for the enzymatic resolution of camphor

doi: 10.1007/s00253-021-11239-5

Figure Lengend Snippet: Sequence alignment of the cloned BDH gene from Pseudomonas sp. ATCC17453 with BDH from Pseudomonas sp. TCU-HL1 (Tsang et al. ) using ClustalW 1.7. Identical amino acids are marked with *. Active site amino acids are in bold

Article Snippet: The three-dimensional structural models of Pseudomonas sp. ATCC 17453 borneol dehydrogenase were generated with the program SWISS-MODEL (Waterhouse et al. ), using the crystal structure of 3-alpha, 20 beta-hydroxysteroid dehydrogenases (PDB: 2HSD) as template (Ghosh et al. ).

Techniques: Sequencing, Clone Assay

Characterization of BDH from Pseudomonas sp. ATCC17453. ( a + b ) Temperature and pH optimum for the oxidation of (±)-borneol. ( c + d ) Temperature and pH optimum for the reduction of camphor

Journal: Applied Microbiology and Biotechnology

Article Title: Engineering of a borneol dehydrogenase from P. putida for the enzymatic resolution of camphor

doi: 10.1007/s00253-021-11239-5

Figure Lengend Snippet: Characterization of BDH from Pseudomonas sp. ATCC17453. ( a + b ) Temperature and pH optimum for the oxidation of (±)-borneol. ( c + d ) Temperature and pH optimum for the reduction of camphor

Article Snippet: The three-dimensional structural models of Pseudomonas sp. ATCC 17453 borneol dehydrogenase were generated with the program SWISS-MODEL (Waterhouse et al. ), using the crystal structure of 3-alpha, 20 beta-hydroxysteroid dehydrogenases (PDB: 2HSD) as template (Ghosh et al. ).

Techniques:

Model of the substrate binding pocket of BDH from Pseudomonas sp. ATCC17453. NADH is shown in red, camphor is shown in cyan, and amino acids chosen for mutagenesis are shown in green

Journal: Applied Microbiology and Biotechnology

Article Title: Engineering of a borneol dehydrogenase from P. putida for the enzymatic resolution of camphor

doi: 10.1007/s00253-021-11239-5

Figure Lengend Snippet: Model of the substrate binding pocket of BDH from Pseudomonas sp. ATCC17453. NADH is shown in red, camphor is shown in cyan, and amino acids chosen for mutagenesis are shown in green

Article Snippet: The three-dimensional structural models of Pseudomonas sp. ATCC 17453 borneol dehydrogenase were generated with the program SWISS-MODEL (Waterhouse et al. ), using the crystal structure of 3-alpha, 20 beta-hydroxysteroid dehydrogenases (PDB: 2HSD) as template (Ghosh et al. ).

Techniques: Binding Assay, Mutagenesis

Kinetic resolution of racemic camphor catalyzed by improved mutants of borneol dehydrogenase from  Pseudomonas sp.  ATCC17453. The enantiomeric ratio E was calculated using Eq. ( <xref ref-type= 2 )" width="100%" height="100%">

Journal: Applied Microbiology and Biotechnology

Article Title: Engineering of a borneol dehydrogenase from P. putida for the enzymatic resolution of camphor

doi: 10.1007/s00253-021-11239-5

Figure Lengend Snippet: Kinetic resolution of racemic camphor catalyzed by improved mutants of borneol dehydrogenase from Pseudomonas sp. ATCC17453. The enantiomeric ratio E was calculated using Eq. ( 2 )

Article Snippet: The three-dimensional structural models of Pseudomonas sp. ATCC 17453 borneol dehydrogenase were generated with the program SWISS-MODEL (Waterhouse et al. ), using the crystal structure of 3-alpha, 20 beta-hydroxysteroid dehydrogenases (PDB: 2HSD) as template (Ghosh et al. ).

Techniques: Variant Assay

Kinetic resolution of camphor catalyzed by improved double mutants of borneol dehydrogenase from  Pseudomonas sp.  ATCC17453

Journal: Applied Microbiology and Biotechnology

Article Title: Engineering of a borneol dehydrogenase from P. putida for the enzymatic resolution of camphor

doi: 10.1007/s00253-021-11239-5

Figure Lengend Snippet: Kinetic resolution of camphor catalyzed by improved double mutants of borneol dehydrogenase from Pseudomonas sp. ATCC17453

Article Snippet: The three-dimensional structural models of Pseudomonas sp. ATCC 17453 borneol dehydrogenase were generated with the program SWISS-MODEL (Waterhouse et al. ), using the crystal structure of 3-alpha, 20 beta-hydroxysteroid dehydrogenases (PDB: 2HSD) as template (Ghosh et al. ).

Techniques: Variant Assay

Kinetic analysis of wild type as well as enantioselective borneol dehydrogenase variants from  Pseudomonas sp.  ATCC17453

Journal: Applied Microbiology and Biotechnology

Article Title: Engineering of a borneol dehydrogenase from P. putida for the enzymatic resolution of camphor

doi: 10.1007/s00253-021-11239-5

Figure Lengend Snippet: Kinetic analysis of wild type as well as enantioselective borneol dehydrogenase variants from Pseudomonas sp. ATCC17453

Article Snippet: The three-dimensional structural models of Pseudomonas sp. ATCC 17453 borneol dehydrogenase were generated with the program SWISS-MODEL (Waterhouse et al. ), using the crystal structure of 3-alpha, 20 beta-hydroxysteroid dehydrogenases (PDB: 2HSD) as template (Ghosh et al. ).

Techniques: Variant Assay

(a) Schematic diagram indicating the time course of the experimental procedure. (b) Flow chart of the experimental groups. KCl: potassium chloride; CA: cardiac arrest; CPR: cardiopulmonary resuscitation; Echo: echocardiography; TEM: transmission electron microscopy; Vehicle: mice subjected to CA/CPR treated with normal saline; Sal B: salvianolic acid B; n : number of mice; ROSC: return of spontaneous circulation; h: hours; min: minutes; EF: ejection fraction; FS: fractional shortening; DHE: dihydroethidium; H&E: hematoxylin-eosin; TUNEL: terminal dUTP nick-end labeling; NADPH: nicotinamide adenine dinucleotide phosphate.

Journal: Oxidative Medicine and Cellular Longevity

Article Title: Salvianolic Acid B Improves Postresuscitation Myocardial and Cerebral Outcomes in a Murine Model of Cardiac Arrest: Involvement of Nrf2 Signaling Pathway

doi: 10.1155/2020/1605456

Figure Lengend Snippet: (a) Schematic diagram indicating the time course of the experimental procedure. (b) Flow chart of the experimental groups. KCl: potassium chloride; CA: cardiac arrest; CPR: cardiopulmonary resuscitation; Echo: echocardiography; TEM: transmission electron microscopy; Vehicle: mice subjected to CA/CPR treated with normal saline; Sal B: salvianolic acid B; n : number of mice; ROSC: return of spontaneous circulation; h: hours; min: minutes; EF: ejection fraction; FS: fractional shortening; DHE: dihydroethidium; H&E: hematoxylin-eosin; TUNEL: terminal dUTP nick-end labeling; NADPH: nicotinamide adenine dinucleotide phosphate.

Article Snippet: Cardiac function and structure were assessed three hours post-ROSC using echocardiography (Vevo 2100, VisualSonics, Toronto, Canada) with a 25 MHz imaging transducer.

Techniques: Transmission Assay, Electron Microscopy, Saline, TUNEL Assay, End Labeling

Salvianolic acid B treatment improved cardiac dysfunction and increased survival following cardiac arrest and cardiopulmonary resuscitation (CA/CPR). (a) Cardiac function was evaluated by echocardiography 3 hours following resuscitation. (b, c) Quantitative analysis of LVEF and LVFS in the indicated groups ( n = 8 per group). Statistical significance was determined using one-way ANOVA followed by post-hoc Bonferroni correction. ## p < 0.01 vs. sham-operated controls; ∗∗ p < 0.01 vs. vehicle group. (d) Kaplan-Meier survival curve of WT and Sal B-treated WT mice after successful CA/CPR within 72 hours ( n = 20 per group). The number of surviving animals is shown to the right in brackets. ∗ p < 0.05 vs. Vehicle by log-rank test. WT: wild type; LVEF: left ventricular ejection fraction; LVFS: left ventricular fractional shortening.

Journal: Oxidative Medicine and Cellular Longevity

Article Title: Salvianolic Acid B Improves Postresuscitation Myocardial and Cerebral Outcomes in a Murine Model of Cardiac Arrest: Involvement of Nrf2 Signaling Pathway

doi: 10.1155/2020/1605456

Figure Lengend Snippet: Salvianolic acid B treatment improved cardiac dysfunction and increased survival following cardiac arrest and cardiopulmonary resuscitation (CA/CPR). (a) Cardiac function was evaluated by echocardiography 3 hours following resuscitation. (b, c) Quantitative analysis of LVEF and LVFS in the indicated groups ( n = 8 per group). Statistical significance was determined using one-way ANOVA followed by post-hoc Bonferroni correction. ## p < 0.01 vs. sham-operated controls; ∗∗ p < 0.01 vs. vehicle group. (d) Kaplan-Meier survival curve of WT and Sal B-treated WT mice after successful CA/CPR within 72 hours ( n = 20 per group). The number of surviving animals is shown to the right in brackets. ∗ p < 0.05 vs. Vehicle by log-rank test. WT: wild type; LVEF: left ventricular ejection fraction; LVFS: left ventricular fractional shortening.

Article Snippet: Cardiac function and structure were assessed three hours post-ROSC using echocardiography (Vevo 2100, VisualSonics, Toronto, Canada) with a 25 MHz imaging transducer.

Techniques: