Zobrazeno 1 - 9 of 9 pro vyhledávání: '"AndrĂŠ Lorenz"'
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Additional file 8: Figure S8. of In vitro analyses of mitochondrial ATP/phosphate carriers from Arabidopsis thaliana revealed unexpected Ca2+-effects
Autor: AndrĂŠ Lorenz, Lorenz, Melanie, Vothknecht, Ute, Niopek-Witz, Sandra, H. Neuhaus, Haferkamp, Ilka
Docking poses of Ca2+ ions within the N-terminal domains of AtAPC1-3, interacting residues and structural superimposition with human SCaMC1 (SLC25A24). Three-dimensional homology models of the N-terminal domains of AtAPC1 (residues 34-189, green), At
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::085ed427565707411b38566dc6daab17
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2
Additional file 6: Figure S6. of In vitro analyses of mitochondrial ATP/phosphate carriers from Arabidopsis thaliana revealed unexpected Ca2+-effects
Autor: AndrĂŠ Lorenz, Lorenz, Melanie, Vothknecht, Ute, Niopek-Witz, Sandra, H. Neuhaus, Haferkamp, Ilka
Effects of rising MgCl2 concentrations on [45Ca] transport via the N- terminally truncated AtAPC2. Transport of 20 ÎźM [45Ca] into Pi loaded (dark gray bars) and non- loaded (light gray bars) proteoliposomes was allowed for 10 min (given as nmol mg
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3
Additional file 1: Figure S1. of In vitro analyses of mitochondrial ATP/phosphate carriers from Arabidopsis thaliana revealed unexpected Ca2+-effects
Autor: AndrĂŠ Lorenz, Lorenz, Melanie, Vothknecht, Ute, Niopek-Witz, Sandra, H. Neuhaus, Haferkamp, Ilka
Heterologously expressed AtAPC1-3 proteins accumulate in the inclusion body fraction of E. coli expression cells. (A) SDS- PAGE of 5 Îźg and (B) Western-blot and immunodetection of 0.5 Îźg of the inclusion bodies fraction from cells expressing At
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4
Additional file 7: Figure S7. of In vitro analyses of mitochondrial ATP/phosphate carriers from Arabidopsis thaliana revealed unexpected Ca2+-effects
Autor: AndrĂŠ Lorenz, Lorenz, Melanie, Vothknecht, Ute, Niopek-Witz, Sandra, H. Neuhaus, Haferkamp, Ilka
Alignment of APC proteins from different organisms. Amino acid sequence alignment of APCs from A. thaliana (AtAPC1-3 [GenBank:At5g61810; At5g51050; At5g07320]), S. cerevisiae (Sal1p [GenBank: YNL083w]) and human (HsSCaMC1-3 [GenBank:SLC25A24; SLC25A2
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5
Additional file 6: Figure S6. of In vitro analyses of mitochondrial ATP/phosphate carriers from Arabidopsis thaliana revealed unexpected Ca2+-effects
Autor: AndrĂŠ Lorenz, Lorenz, Melanie, Vothknecht, Ute, Niopek-Witz, Sandra, H. Neuhaus, Haferkamp, Ilka
Effects of rising MgCl2 concentrations on [45Ca] transport via the N- terminally truncated AtAPC2. Transport of 20 ÎźM [45Ca] into Pi loaded (dark gray bars) and non- loaded (light gray bars) proteoliposomes was allowed for 10 min (given as nmol mg
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6
Additional file 2: Figure S2. of In vitro analyses of mitochondrial ATP/phosphate carriers from Arabidopsis thaliana revealed unexpected Ca2+-effects
Autor: AndrĂŠ Lorenz, Lorenz, Melanie, Vothknecht, Ute, Niopek-Witz, Sandra, H. Neuhaus, Haferkamp, Ilka
Time dependent ADP transport via AtAPC1-3. Transport of 50 ÎźM [Îą32P]-ADP into Pi (A, C, E) and into ADP (B, D, F) loaded proteoliposomes with reconstituted AtAPC1 (A, B), AtAPC2 (C, D) and AtAPC3 (E, F). Non-loaded liposomes (non-filled rhombs;
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7
Additional file 2: Figure S2. of In vitro analyses of mitochondrial ATP/phosphate carriers from Arabidopsis thaliana revealed unexpected Ca2+-effects
Autor: AndrĂŠ Lorenz, Lorenz, Melanie, Vothknecht, Ute, Niopek-Witz, Sandra, H. Neuhaus, Haferkamp, Ilka
Time dependent ADP transport via AtAPC1-3. Transport of 50 ÎźM [Îą32P]-ADP into Pi (A, C, E) and into ADP (B, D, F) loaded proteoliposomes with reconstituted AtAPC1 (A, B), AtAPC2 (C, D) and AtAPC3 (E, F). Non-loaded liposomes (non-filled rhombs;
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8
Additional file 8: Figure S8. of In vitro analyses of mitochondrial ATP/phosphate carriers from Arabidopsis thaliana revealed unexpected Ca2+-effects
Autor: AndrĂŠ Lorenz, Lorenz, Melanie, Vothknecht, Ute, Niopek-Witz, Sandra, H. Neuhaus, Haferkamp, Ilka
Docking poses of Ca2+ ions within the N-terminal domains of AtAPC1-3, interacting residues and structural superimposition with human SCaMC1 (SLC25A24). Three-dimensional homology models of the N-terminal domains of AtAPC1 (residues 34-189, green), At
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1c7a82080fdc8bc189f31559d806db60
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9
Additional file 7: Figure S7. of In vitro analyses of mitochondrial ATP/phosphate carriers from Arabidopsis thaliana revealed unexpected Ca2+-effects
Autor: AndrĂŠ Lorenz, Lorenz, Melanie, Vothknecht, Ute, Niopek-Witz, Sandra, H. Neuhaus, Haferkamp, Ilka
Alignment of APC proteins from different organisms. Amino acid sequence alignment of APCs from A. thaliana (AtAPC1-3 [GenBank:At5g61810; At5g51050; At5g07320]), S. cerevisiae (Sal1p [GenBank: YNL083w]) and human (HsSCaMC1-3 [GenBank:SLC25A24; SLC25A2
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5ccc1af92585cd02bb3187ef049847cd
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