docking analyses Search Results


docking analyses of substrate with lip and mutants  (Chemical Computing Group)
90
Chemical Computing Group docking analyses of substrate with lip and mutants
Docking Analyses Of Substrate With Lip And Mutants, supplied by Chemical Computing Group, 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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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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molecular ca 2+ docking analyses - by Bioz Stars, 2026-03
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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
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Average 90 stars, based on 1 article reviews
in silico docking analyses - by Bioz Stars, 2026-03
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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, 2026-03
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dynamics md-based docking analyses  (Molecular Dynamics Inc)
90
Molecular Dynamics Inc dynamics md-based 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
Dynamics Md Based Docking Analyses, supplied by Molecular Dynamics Inc, 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/dynamics md-based docking analyses/product/Molecular Dynamics Inc
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dynamics md-based docking analyses - by Bioz Stars, 2026-03
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docking analyses using glide in extra precision  (Otava Inc)
90
Otava Inc docking analyses using glide in extra precision
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 Using Glide In Extra Precision, supplied by Otava Inc, 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 using glide in extra precision/product/Otava Inc
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docking analyses using glide in extra precision - by Bioz Stars, 2026-03
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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, 2026-03
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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