The Experts below are selected from a list of 46542 Experts worldwide ranked by ideXlab platform
Steven J. D. Karlish - One of the best experts on this subject based on the ideXlab platform.
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selective fe2 catalyzed oxidative cleavage of gastric h k atpase implications for the energy transduction mechanism of p type cation pumps
Journal of Biological Chemistry, 2001Co-Authors: Jai Moo Shin, Rivka Goldshleger, George Sachs, Keith Munson, Steven J. D. KarlishAbstract:Abstract In the presence of ascorbate/H2O2, Fe2+ ions or the ATP-Fe2+ complex catalyze selective cleavage of the α subunit of gastric H+,K+-ATPase. The electrophoretic mobilities of the fragments and dependence of the cleavage patterns on E 1 andE 2 conformational states are essentially identical to those described previously for renal Na+,K+-ATPase. The cleavage pattern of H+,K+-ATPase by Fe2+ ions is consistent with the existence of two Fe2+ sites: site 1 within highly conserved sequences in the P and A domains, and site 2 at the cytoplasmic entrance to trans-membrane segments M3 and M1. The change in the pattern of cleavage catalyzed by Fe2+ or the ATP-Fe2+ complex induced by different ligands provides evidence for large conformational movements of the N, P, and A cytoplasmic domains of the enzyme. The results are consistent with the Ca2+-ATPase crystal structure (Protein Data Bank Identification Code 1EUL; Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Nature 405, 647–655), anE 1Ca2+ conformation, and a theoretical model of Ca2+-ATPase in anE 2 conformation (Protein Data Bank Identification Code 1FQU). Thus, it can be presumed that the movements of N, P, and A cytoplasmic domains, associated with theE 1 ↔ E 2 transitions, are similar in all P-type ATPases. Fe2+-catalyzed cleavage patterns also reveal sequences involved in phosphate, Mg2+, and ATP binding, which have not yet been shown in crystal structures, as well as changes which occur in E 1 ↔E 2 transitions, and subconformations induced by H+,K+-ATPase-specific ligands such as SCH28080.
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selective fe2 catalyzed oxidative cleavage of gastric h k atpase implications for the energy transduction mechanism of p type cation pumps
Journal of Biological Chemistry, 2001Co-Authors: Jai Moo Shin, Rivka Goldshleger, George Sachs, Keith Munson, Steven J. D. KarlishAbstract:Abstract In the presence of ascorbate/H2O2, Fe2+ ions or the ATP-Fe2+ complex catalyze selective cleavage of the α subunit of gastric H+,K+-ATPase. The electrophoretic mobilities of the fragments and dependence of the cleavage patterns on E 1 andE 2 conformational states are essentially identical to those described previously for renal Na+,K+-ATPase. The cleavage pattern of H+,K+-ATPase by Fe2+ ions is consistent with the existence of two Fe2+ sites: site 1 within highly conserved sequences in the P and A domains, and site 2 at the cytoplasmic entrance to trans-membrane segments M3 and M1. The change in the pattern of cleavage catalyzed by Fe2+ or the ATP-Fe2+ complex induced by different ligands provides evidence for large conformational movements of the N, P, and A cytoplasmic domains of the enzyme. The results are consistent with the Ca2+-ATPase crystal structure (Protein Data Bank Identification Code 1EUL; Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Nature 405, 647–655), anE 1Ca2+ conformation, and a theoretical model of Ca2+-ATPase in anE 2 conformation (Protein Data Bank Identification Code 1FQU). Thus, it can be presumed that the movements of N, P, and A cytoplasmic domains, associated with theE 1 ↔ E 2 transitions, are similar in all P-type ATPases. Fe2+-catalyzed cleavage patterns also reveal sequences involved in phosphate, Mg2+, and ATP binding, which have not yet been shown in crystal structures, as well as changes which occur in E 1 ↔E 2 transitions, and subconformations induced by H+,K+-ATPase-specific ligands such as SCH28080.
Jai Moo Shin - One of the best experts on this subject based on the ideXlab platform.
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selective fe2 catalyzed oxidative cleavage of gastric h k atpase implications for the energy transduction mechanism of p type cation pumps
Journal of Biological Chemistry, 2001Co-Authors: Jai Moo Shin, Rivka Goldshleger, George Sachs, Keith Munson, Steven J. D. KarlishAbstract:Abstract In the presence of ascorbate/H2O2, Fe2+ ions or the ATP-Fe2+ complex catalyze selective cleavage of the α subunit of gastric H+,K+-ATPase. The electrophoretic mobilities of the fragments and dependence of the cleavage patterns on E 1 andE 2 conformational states are essentially identical to those described previously for renal Na+,K+-ATPase. The cleavage pattern of H+,K+-ATPase by Fe2+ ions is consistent with the existence of two Fe2+ sites: site 1 within highly conserved sequences in the P and A domains, and site 2 at the cytoplasmic entrance to trans-membrane segments M3 and M1. The change in the pattern of cleavage catalyzed by Fe2+ or the ATP-Fe2+ complex induced by different ligands provides evidence for large conformational movements of the N, P, and A cytoplasmic domains of the enzyme. The results are consistent with the Ca2+-ATPase crystal structure (Protein Data Bank Identification Code 1EUL; Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Nature 405, 647–655), anE 1Ca2+ conformation, and a theoretical model of Ca2+-ATPase in anE 2 conformation (Protein Data Bank Identification Code 1FQU). Thus, it can be presumed that the movements of N, P, and A cytoplasmic domains, associated with theE 1 ↔ E 2 transitions, are similar in all P-type ATPases. Fe2+-catalyzed cleavage patterns also reveal sequences involved in phosphate, Mg2+, and ATP binding, which have not yet been shown in crystal structures, as well as changes which occur in E 1 ↔E 2 transitions, and subconformations induced by H+,K+-ATPase-specific ligands such as SCH28080.
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selective fe2 catalyzed oxidative cleavage of gastric h k atpase implications for the energy transduction mechanism of p type cation pumps
Journal of Biological Chemistry, 2001Co-Authors: Jai Moo Shin, Rivka Goldshleger, George Sachs, Keith Munson, Steven J. D. KarlishAbstract:Abstract In the presence of ascorbate/H2O2, Fe2+ ions or the ATP-Fe2+ complex catalyze selective cleavage of the α subunit of gastric H+,K+-ATPase. The electrophoretic mobilities of the fragments and dependence of the cleavage patterns on E 1 andE 2 conformational states are essentially identical to those described previously for renal Na+,K+-ATPase. The cleavage pattern of H+,K+-ATPase by Fe2+ ions is consistent with the existence of two Fe2+ sites: site 1 within highly conserved sequences in the P and A domains, and site 2 at the cytoplasmic entrance to trans-membrane segments M3 and M1. The change in the pattern of cleavage catalyzed by Fe2+ or the ATP-Fe2+ complex induced by different ligands provides evidence for large conformational movements of the N, P, and A cytoplasmic domains of the enzyme. The results are consistent with the Ca2+-ATPase crystal structure (Protein Data Bank Identification Code 1EUL; Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Nature 405, 647–655), anE 1Ca2+ conformation, and a theoretical model of Ca2+-ATPase in anE 2 conformation (Protein Data Bank Identification Code 1FQU). Thus, it can be presumed that the movements of N, P, and A cytoplasmic domains, associated with theE 1 ↔ E 2 transitions, are similar in all P-type ATPases. Fe2+-catalyzed cleavage patterns also reveal sequences involved in phosphate, Mg2+, and ATP binding, which have not yet been shown in crystal structures, as well as changes which occur in E 1 ↔E 2 transitions, and subconformations induced by H+,K+-ATPase-specific ligands such as SCH28080.
Keith Munson - One of the best experts on this subject based on the ideXlab platform.
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selective fe2 catalyzed oxidative cleavage of gastric h k atpase implications for the energy transduction mechanism of p type cation pumps
Journal of Biological Chemistry, 2001Co-Authors: Jai Moo Shin, Rivka Goldshleger, George Sachs, Keith Munson, Steven J. D. KarlishAbstract:Abstract In the presence of ascorbate/H2O2, Fe2+ ions or the ATP-Fe2+ complex catalyze selective cleavage of the α subunit of gastric H+,K+-ATPase. The electrophoretic mobilities of the fragments and dependence of the cleavage patterns on E 1 andE 2 conformational states are essentially identical to those described previously for renal Na+,K+-ATPase. The cleavage pattern of H+,K+-ATPase by Fe2+ ions is consistent with the existence of two Fe2+ sites: site 1 within highly conserved sequences in the P and A domains, and site 2 at the cytoplasmic entrance to trans-membrane segments M3 and M1. The change in the pattern of cleavage catalyzed by Fe2+ or the ATP-Fe2+ complex induced by different ligands provides evidence for large conformational movements of the N, P, and A cytoplasmic domains of the enzyme. The results are consistent with the Ca2+-ATPase crystal structure (Protein Data Bank Identification Code 1EUL; Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Nature 405, 647–655), anE 1Ca2+ conformation, and a theoretical model of Ca2+-ATPase in anE 2 conformation (Protein Data Bank Identification Code 1FQU). Thus, it can be presumed that the movements of N, P, and A cytoplasmic domains, associated with theE 1 ↔ E 2 transitions, are similar in all P-type ATPases. Fe2+-catalyzed cleavage patterns also reveal sequences involved in phosphate, Mg2+, and ATP binding, which have not yet been shown in crystal structures, as well as changes which occur in E 1 ↔E 2 transitions, and subconformations induced by H+,K+-ATPase-specific ligands such as SCH28080.
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selective fe2 catalyzed oxidative cleavage of gastric h k atpase implications for the energy transduction mechanism of p type cation pumps
Journal of Biological Chemistry, 2001Co-Authors: Jai Moo Shin, Rivka Goldshleger, George Sachs, Keith Munson, Steven J. D. KarlishAbstract:Abstract In the presence of ascorbate/H2O2, Fe2+ ions or the ATP-Fe2+ complex catalyze selective cleavage of the α subunit of gastric H+,K+-ATPase. The electrophoretic mobilities of the fragments and dependence of the cleavage patterns on E 1 andE 2 conformational states are essentially identical to those described previously for renal Na+,K+-ATPase. The cleavage pattern of H+,K+-ATPase by Fe2+ ions is consistent with the existence of two Fe2+ sites: site 1 within highly conserved sequences in the P and A domains, and site 2 at the cytoplasmic entrance to trans-membrane segments M3 and M1. The change in the pattern of cleavage catalyzed by Fe2+ or the ATP-Fe2+ complex induced by different ligands provides evidence for large conformational movements of the N, P, and A cytoplasmic domains of the enzyme. The results are consistent with the Ca2+-ATPase crystal structure (Protein Data Bank Identification Code 1EUL; Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Nature 405, 647–655), anE 1Ca2+ conformation, and a theoretical model of Ca2+-ATPase in anE 2 conformation (Protein Data Bank Identification Code 1FQU). Thus, it can be presumed that the movements of N, P, and A cytoplasmic domains, associated with theE 1 ↔ E 2 transitions, are similar in all P-type ATPases. Fe2+-catalyzed cleavage patterns also reveal sequences involved in phosphate, Mg2+, and ATP binding, which have not yet been shown in crystal structures, as well as changes which occur in E 1 ↔E 2 transitions, and subconformations induced by H+,K+-ATPase-specific ligands such as SCH28080.
George Sachs - One of the best experts on this subject based on the ideXlab platform.
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selective fe2 catalyzed oxidative cleavage of gastric h k atpase implications for the energy transduction mechanism of p type cation pumps
Journal of Biological Chemistry, 2001Co-Authors: Jai Moo Shin, Rivka Goldshleger, George Sachs, Keith Munson, Steven J. D. KarlishAbstract:Abstract In the presence of ascorbate/H2O2, Fe2+ ions or the ATP-Fe2+ complex catalyze selective cleavage of the α subunit of gastric H+,K+-ATPase. The electrophoretic mobilities of the fragments and dependence of the cleavage patterns on E 1 andE 2 conformational states are essentially identical to those described previously for renal Na+,K+-ATPase. The cleavage pattern of H+,K+-ATPase by Fe2+ ions is consistent with the existence of two Fe2+ sites: site 1 within highly conserved sequences in the P and A domains, and site 2 at the cytoplasmic entrance to trans-membrane segments M3 and M1. The change in the pattern of cleavage catalyzed by Fe2+ or the ATP-Fe2+ complex induced by different ligands provides evidence for large conformational movements of the N, P, and A cytoplasmic domains of the enzyme. The results are consistent with the Ca2+-ATPase crystal structure (Protein Data Bank Identification Code 1EUL; Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Nature 405, 647–655), anE 1Ca2+ conformation, and a theoretical model of Ca2+-ATPase in anE 2 conformation (Protein Data Bank Identification Code 1FQU). Thus, it can be presumed that the movements of N, P, and A cytoplasmic domains, associated with theE 1 ↔ E 2 transitions, are similar in all P-type ATPases. Fe2+-catalyzed cleavage patterns also reveal sequences involved in phosphate, Mg2+, and ATP binding, which have not yet been shown in crystal structures, as well as changes which occur in E 1 ↔E 2 transitions, and subconformations induced by H+,K+-ATPase-specific ligands such as SCH28080.
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selective fe2 catalyzed oxidative cleavage of gastric h k atpase implications for the energy transduction mechanism of p type cation pumps
Journal of Biological Chemistry, 2001Co-Authors: Jai Moo Shin, Rivka Goldshleger, George Sachs, Keith Munson, Steven J. D. KarlishAbstract:Abstract In the presence of ascorbate/H2O2, Fe2+ ions or the ATP-Fe2+ complex catalyze selective cleavage of the α subunit of gastric H+,K+-ATPase. The electrophoretic mobilities of the fragments and dependence of the cleavage patterns on E 1 andE 2 conformational states are essentially identical to those described previously for renal Na+,K+-ATPase. The cleavage pattern of H+,K+-ATPase by Fe2+ ions is consistent with the existence of two Fe2+ sites: site 1 within highly conserved sequences in the P and A domains, and site 2 at the cytoplasmic entrance to trans-membrane segments M3 and M1. The change in the pattern of cleavage catalyzed by Fe2+ or the ATP-Fe2+ complex induced by different ligands provides evidence for large conformational movements of the N, P, and A cytoplasmic domains of the enzyme. The results are consistent with the Ca2+-ATPase crystal structure (Protein Data Bank Identification Code 1EUL; Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Nature 405, 647–655), anE 1Ca2+ conformation, and a theoretical model of Ca2+-ATPase in anE 2 conformation (Protein Data Bank Identification Code 1FQU). Thus, it can be presumed that the movements of N, P, and A cytoplasmic domains, associated with theE 1 ↔ E 2 transitions, are similar in all P-type ATPases. Fe2+-catalyzed cleavage patterns also reveal sequences involved in phosphate, Mg2+, and ATP binding, which have not yet been shown in crystal structures, as well as changes which occur in E 1 ↔E 2 transitions, and subconformations induced by H+,K+-ATPase-specific ligands such as SCH28080.
Rivka Goldshleger - One of the best experts on this subject based on the ideXlab platform.
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selective fe2 catalyzed oxidative cleavage of gastric h k atpase implications for the energy transduction mechanism of p type cation pumps
Journal of Biological Chemistry, 2001Co-Authors: Jai Moo Shin, Rivka Goldshleger, George Sachs, Keith Munson, Steven J. D. KarlishAbstract:Abstract In the presence of ascorbate/H2O2, Fe2+ ions or the ATP-Fe2+ complex catalyze selective cleavage of the α subunit of gastric H+,K+-ATPase. The electrophoretic mobilities of the fragments and dependence of the cleavage patterns on E 1 andE 2 conformational states are essentially identical to those described previously for renal Na+,K+-ATPase. The cleavage pattern of H+,K+-ATPase by Fe2+ ions is consistent with the existence of two Fe2+ sites: site 1 within highly conserved sequences in the P and A domains, and site 2 at the cytoplasmic entrance to trans-membrane segments M3 and M1. The change in the pattern of cleavage catalyzed by Fe2+ or the ATP-Fe2+ complex induced by different ligands provides evidence for large conformational movements of the N, P, and A cytoplasmic domains of the enzyme. The results are consistent with the Ca2+-ATPase crystal structure (Protein Data Bank Identification Code 1EUL; Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Nature 405, 647–655), anE 1Ca2+ conformation, and a theoretical model of Ca2+-ATPase in anE 2 conformation (Protein Data Bank Identification Code 1FQU). Thus, it can be presumed that the movements of N, P, and A cytoplasmic domains, associated with theE 1 ↔ E 2 transitions, are similar in all P-type ATPases. Fe2+-catalyzed cleavage patterns also reveal sequences involved in phosphate, Mg2+, and ATP binding, which have not yet been shown in crystal structures, as well as changes which occur in E 1 ↔E 2 transitions, and subconformations induced by H+,K+-ATPase-specific ligands such as SCH28080.
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selective fe2 catalyzed oxidative cleavage of gastric h k atpase implications for the energy transduction mechanism of p type cation pumps
Journal of Biological Chemistry, 2001Co-Authors: Jai Moo Shin, Rivka Goldshleger, George Sachs, Keith Munson, Steven J. D. KarlishAbstract:Abstract In the presence of ascorbate/H2O2, Fe2+ ions or the ATP-Fe2+ complex catalyze selective cleavage of the α subunit of gastric H+,K+-ATPase. The electrophoretic mobilities of the fragments and dependence of the cleavage patterns on E 1 andE 2 conformational states are essentially identical to those described previously for renal Na+,K+-ATPase. The cleavage pattern of H+,K+-ATPase by Fe2+ ions is consistent with the existence of two Fe2+ sites: site 1 within highly conserved sequences in the P and A domains, and site 2 at the cytoplasmic entrance to trans-membrane segments M3 and M1. The change in the pattern of cleavage catalyzed by Fe2+ or the ATP-Fe2+ complex induced by different ligands provides evidence for large conformational movements of the N, P, and A cytoplasmic domains of the enzyme. The results are consistent with the Ca2+-ATPase crystal structure (Protein Data Bank Identification Code 1EUL; Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Nature 405, 647–655), anE 1Ca2+ conformation, and a theoretical model of Ca2+-ATPase in anE 2 conformation (Protein Data Bank Identification Code 1FQU). Thus, it can be presumed that the movements of N, P, and A cytoplasmic domains, associated with theE 1 ↔ E 2 transitions, are similar in all P-type ATPases. Fe2+-catalyzed cleavage patterns also reveal sequences involved in phosphate, Mg2+, and ATP binding, which have not yet been shown in crystal structures, as well as changes which occur in E 1 ↔E 2 transitions, and subconformations induced by H+,K+-ATPase-specific ligands such as SCH28080.
