docking analyses Search Results


molecular ca 2+ docking analyses  (AUTODOCK GmbH)
90
AUTODOCK GmbH molecular ca 2+ docking analyses
Ca 2+ -impact on ATP transport via At APC1-3. Effect of rising Ca 2+ -concentrations (0–500 μM) on transport mediated by recombinant At APC1 ( a , b ), At APC2 ( c , d ) and At APC3 ( e , f ). Transport of 50 μM [α 32 P]-ATP was conducted in absence (black rhombs) and presence of supplemental MgCl 2 (gray rhombs). Transport was allowed for 5 min and is given in nmol mg protein −1 h −1 . Ca 2+ -dependent stimulation of ATP/P i hetero-exchanges ( a , c , e ) and ATP/ATP homo-exchanges ( b , d , f ). Non-loaded liposomes (non-filled rhombs; negative control) showed only marginal accumulation of ATP and the corresponding rates were unaffected by MgCl 2 addition. Data represent mean values of three independent replicates, standard errors are given
Molecular Ca 2+ Docking Analyses, supplied by AUTODOCK GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
molecular ca 2+ docking analyses - by Bioz Stars, 2026-06
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docking analyses  (Accelrys)
86
Accelrys docking analyses
Ca 2+ -impact on ATP transport via At APC1-3. Effect of rising Ca 2+ -concentrations (0–500 μM) on transport mediated by recombinant At APC1 ( a , b ), At APC2 ( c , d ) and At APC3 ( e , f ). Transport of 50 μM [α 32 P]-ATP was conducted in absence (black rhombs) and presence of supplemental MgCl 2 (gray rhombs). Transport was allowed for 5 min and is given in nmol mg protein −1 h −1 . Ca 2+ -dependent stimulation of ATP/P i hetero-exchanges ( a , c , e ) and ATP/ATP homo-exchanges ( b , d , f ). Non-loaded liposomes (non-filled rhombs; negative control) showed only marginal accumulation of ATP and the corresponding rates were unaffected by MgCl 2 addition. Data represent mean values of three independent replicates, standard errors are given
Docking Analyses, supplied by Accelrys, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 86 stars, based on 1 article reviews
docking analyses - by Bioz Stars, 2026-06
86/100 stars
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docking analyses  (Molecular Dynamics Inc)
86
Molecular Dynamics Inc docking analyses
Ca 2+ -impact on ATP transport via At APC1-3. Effect of rising Ca 2+ -concentrations (0–500 μM) on transport mediated by recombinant At APC1 ( a , b ), At APC2 ( c , d ) and At APC3 ( e , f ). Transport of 50 μM [α 32 P]-ATP was conducted in absence (black rhombs) and presence of supplemental MgCl 2 (gray rhombs). Transport was allowed for 5 min and is given in nmol mg protein −1 h −1 . Ca 2+ -dependent stimulation of ATP/P i hetero-exchanges ( a , c , e ) and ATP/ATP homo-exchanges ( b , d , f ). Non-loaded liposomes (non-filled rhombs; negative control) showed only marginal accumulation of ATP and the corresponding rates were unaffected by MgCl 2 addition. Data represent mean values of three independent replicates, standard errors are given
Docking Analyses, supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/docking analyses/product/Molecular Dynamics Inc
Average 86 stars, based on 1 article reviews
docking analyses - by Bioz Stars, 2026-06
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in silico docking analyses  (MBL Life science)
90
MBL Life science in silico docking analyses
Ca 2+ -impact on ATP transport via At APC1-3. Effect of rising Ca 2+ -concentrations (0–500 μM) on transport mediated by recombinant At APC1 ( a , b ), At APC2 ( c , d ) and At APC3 ( e , f ). Transport of 50 μM [α 32 P]-ATP was conducted in absence (black rhombs) and presence of supplemental MgCl 2 (gray rhombs). Transport was allowed for 5 min and is given in nmol mg protein −1 h −1 . Ca 2+ -dependent stimulation of ATP/P i hetero-exchanges ( a , c , e ) and ATP/ATP homo-exchanges ( b , d , f ). Non-loaded liposomes (non-filled rhombs; negative control) showed only marginal accumulation of ATP and the corresponding rates were unaffected by MgCl 2 addition. Data represent mean values of three independent replicates, standard errors are given
In Silico Docking Analyses, supplied by MBL Life science, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/in silico docking analyses/product/MBL Life science
Average 90 stars, based on 1 article reviews
in silico docking analyses - by Bioz Stars, 2026-06
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molecular docking analyses  (Schrodinger LLC)
90
Schrodinger LLC molecular docking analyses
Ca 2+ -impact on ATP transport via At APC1-3. Effect of rising Ca 2+ -concentrations (0–500 μM) on transport mediated by recombinant At APC1 ( a , b ), At APC2 ( c , d ) and At APC3 ( e , f ). Transport of 50 μM [α 32 P]-ATP was conducted in absence (black rhombs) and presence of supplemental MgCl 2 (gray rhombs). Transport was allowed for 5 min and is given in nmol mg protein −1 h −1 . Ca 2+ -dependent stimulation of ATP/P i hetero-exchanges ( a , c , e ) and ATP/ATP homo-exchanges ( b , d , f ). Non-loaded liposomes (non-filled rhombs; negative control) showed only marginal accumulation of ATP and the corresponding rates were unaffected by MgCl 2 addition. Data represent mean values of three independent replicates, standard errors are given
Molecular Docking Analyses, supplied by Schrodinger LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/molecular docking analyses/product/Schrodinger LLC
Average 90 stars, based on 1 article reviews
molecular docking analyses - by Bioz Stars, 2026-06
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docking analyses  (Verlag GmbH)
90
Verlag GmbH docking analyses
Ca 2+ -impact on ATP transport via At APC1-3. Effect of rising Ca 2+ -concentrations (0–500 μM) on transport mediated by recombinant At APC1 ( a , b ), At APC2 ( c , d ) and At APC3 ( e , f ). Transport of 50 μM [α 32 P]-ATP was conducted in absence (black rhombs) and presence of supplemental MgCl 2 (gray rhombs). Transport was allowed for 5 min and is given in nmol mg protein −1 h −1 . Ca 2+ -dependent stimulation of ATP/P i hetero-exchanges ( a , c , e ) and ATP/ATP homo-exchanges ( b , d , f ). Non-loaded liposomes (non-filled rhombs; negative control) showed only marginal accumulation of ATP and the corresponding rates were unaffected by MgCl 2 addition. Data represent mean values of three independent replicates, standard errors are given
Docking Analyses, supplied by Verlag GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/docking analyses/product/Verlag GmbH
Average 90 stars, based on 1 article reviews
docking analyses - by Bioz Stars, 2026-06
90/100 stars
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Image Search Results


Ca 2+ -impact on ATP transport via At APC1-3. Effect of rising Ca 2+ -concentrations (0–500 μM) on transport mediated by recombinant At APC1 ( a , b ), At APC2 ( c , d ) and At APC3 ( e , f ). Transport of 50 μM [α 32 P]-ATP was conducted in absence (black rhombs) and presence of supplemental MgCl 2 (gray rhombs). Transport was allowed for 5 min and is given in nmol mg protein −1 h −1 . Ca 2+ -dependent stimulation of ATP/P i hetero-exchanges ( a , c , e ) and ATP/ATP homo-exchanges ( b , d , f ). Non-loaded liposomes (non-filled rhombs; negative control) showed only marginal accumulation of ATP and the corresponding rates were unaffected by MgCl 2 addition. Data represent mean values of three independent replicates, standard errors are given

Journal: BMC Plant Biology

Article Title: In vitro analyses of mitochondrial ATP/phosphate carriers from Arabidopsis thaliana revealed unexpected Ca 2+ -effects

doi: 10.1186/s12870-015-0616-0

Figure Lengend Snippet: Ca 2+ -impact on ATP transport via At APC1-3. Effect of rising Ca 2+ -concentrations (0–500 μM) on transport mediated by recombinant At APC1 ( a , b ), At APC2 ( c , d ) and At APC3 ( e , f ). Transport of 50 μM [α 32 P]-ATP was conducted in absence (black rhombs) and presence of supplemental MgCl 2 (gray rhombs). Transport was allowed for 5 min and is given in nmol mg protein −1 h −1 . Ca 2+ -dependent stimulation of ATP/P i hetero-exchanges ( a , c , e ) and ATP/ATP homo-exchanges ( b , d , f ). Non-loaded liposomes (non-filled rhombs; negative control) showed only marginal accumulation of ATP and the corresponding rates were unaffected by MgCl 2 addition. Data represent mean values of three independent replicates, standard errors are given

Article Snippet: Residues predicted by Scanprosite ( http://prosite.expasy.org/scanprosite ) are marked in green and by molecular Ca 2+ docking analyses with AutoDock vina (see also Additional file : Figure S8) are marked in orange.

Techniques: Recombinant, Liposomes, Negative Control

Ca 2+ -impact on ATP and ADP transport of full-length and N-terminally truncated At APC2. Transport via recombinant At APC2 ( a ) and via the mutated version lacking its N-terminal domain ( b ). Import of [α 32 P]-ATP into P i loaded proteoliposomes (black squares) and of [α 32 P]-ADP into ATP loaded vesicles (gray circles) was allowed for 5 min. Transport without CaCl 2 was set to 100 % and transport in presence of rising concentrations of externally added CaCl 2 (0 - 500 μM) was calculated accordingly. Data represent net values of ATP/P i and ADP/ATP uptake minus the respective control (non-loaded vesicles) of three independent replicates. Standard errors are given

Journal: BMC Plant Biology

Article Title: In vitro analyses of mitochondrial ATP/phosphate carriers from Arabidopsis thaliana revealed unexpected Ca 2+ -effects

doi: 10.1186/s12870-015-0616-0

Figure Lengend Snippet: Ca 2+ -impact on ATP and ADP transport of full-length and N-terminally truncated At APC2. Transport via recombinant At APC2 ( a ) and via the mutated version lacking its N-terminal domain ( b ). Import of [α 32 P]-ATP into P i loaded proteoliposomes (black squares) and of [α 32 P]-ADP into ATP loaded vesicles (gray circles) was allowed for 5 min. Transport without CaCl 2 was set to 100 % and transport in presence of rising concentrations of externally added CaCl 2 (0 - 500 μM) was calculated accordingly. Data represent net values of ATP/P i and ADP/ATP uptake minus the respective control (non-loaded vesicles) of three independent replicates. Standard errors are given

Article Snippet: Residues predicted by Scanprosite ( http://prosite.expasy.org/scanprosite ) are marked in green and by molecular Ca 2+ docking analyses with AutoDock vina (see also Additional file : Figure S8) are marked in orange.

Techniques: Recombinant, Control

Determination of Ca 2+ transport via At APC2. Time dependent uptake of [ 45 Ca] via full-length At APC2 ( a ) and via N-terminally truncated At APC2 ( b ) reconstituted into P i (black rhombs) and non-loaded liposomes (gray squares). ( c ) Effects of rising MgCl 2 concentrations on [ 45 Ca] transport into P i loaded (dark gray bars) and non-loaded (light gray bars) At APC2 proteoliposomes. Transport media contained 20 μM [ 45 Ca] and were additionally supplemented with 100 μM non-labeled ATP and the indicated concentrations of MgCl 2 . For determination of the Mg 2+ -effects on Ca 2+ transport via At APC2 uptake was allowed for 10 min (given as nmol mg protein −1 h −1 ). Data represent mean values of three independent replicates. Standard errors are indicated

Journal: BMC Plant Biology

Article Title: In vitro analyses of mitochondrial ATP/phosphate carriers from Arabidopsis thaliana revealed unexpected Ca 2+ -effects

doi: 10.1186/s12870-015-0616-0

Figure Lengend Snippet: Determination of Ca 2+ transport via At APC2. Time dependent uptake of [ 45 Ca] via full-length At APC2 ( a ) and via N-terminally truncated At APC2 ( b ) reconstituted into P i (black rhombs) and non-loaded liposomes (gray squares). ( c ) Effects of rising MgCl 2 concentrations on [ 45 Ca] transport into P i loaded (dark gray bars) and non-loaded (light gray bars) At APC2 proteoliposomes. Transport media contained 20 μM [ 45 Ca] and were additionally supplemented with 100 μM non-labeled ATP and the indicated concentrations of MgCl 2 . For determination of the Mg 2+ -effects on Ca 2+ transport via At APC2 uptake was allowed for 10 min (given as nmol mg protein −1 h −1 ). Data represent mean values of three independent replicates. Standard errors are indicated

Article Snippet: Residues predicted by Scanprosite ( http://prosite.expasy.org/scanprosite ) are marked in green and by molecular Ca 2+ docking analyses with AutoDock vina (see also Additional file : Figure S8) are marked in orange.

Techniques: Liposomes, Labeling

Structural alignment of the N-terminal domains of At APC1-3 and human SCaMC1. Three-dimensional homology models of At APC1 (residues 34–189, green), At APC2 (residues 38–194, yellow) and At APC3 (residues 35–189, orange). N-terminal domains were built using HHPred server and Modeller based on the crystal structure of the Ca 2+ -binding N-terminal domain of human SCaMC1 (blue; PDB ID: 4N5X) in complex with four calcium ions (gray spheres). The sequence alignment followed by a structural superimposition of the models was carried out using PyMOL (version 1.3)

Journal: BMC Plant Biology

Article Title: In vitro analyses of mitochondrial ATP/phosphate carriers from Arabidopsis thaliana revealed unexpected Ca 2+ -effects

doi: 10.1186/s12870-015-0616-0

Figure Lengend Snippet: Structural alignment of the N-terminal domains of At APC1-3 and human SCaMC1. Three-dimensional homology models of At APC1 (residues 34–189, green), At APC2 (residues 38–194, yellow) and At APC3 (residues 35–189, orange). N-terminal domains were built using HHPred server and Modeller based on the crystal structure of the Ca 2+ -binding N-terminal domain of human SCaMC1 (blue; PDB ID: 4N5X) in complex with four calcium ions (gray spheres). The sequence alignment followed by a structural superimposition of the models was carried out using PyMOL (version 1.3)

Article Snippet: Residues predicted by Scanprosite ( http://prosite.expasy.org/scanprosite ) are marked in green and by molecular Ca 2+ docking analyses with AutoDock vina (see also Additional file : Figure S8) are marked in orange.

Techniques: Binding Assay, Sequencing