The Experts below are selected from a list of 283374 Experts worldwide ranked by ideXlab platform
Chikashi Terao - One of the best experts on this subject based on the ideXlab platform.
-
descriptive epidemiology of spot urine sodium to potassium ratio clarified Close Relationship with blood pressure level the nagahama study
Journal of Hypertension, 2015Co-Authors: Yasuharu Tabara, Yoshimitsu Takahashi, Kyoko Kumagai, Kazuya Setoh, Takahisa Kawaguchi, Meiko Takahashi, Yuki Muraoka, Akitaka Tsujikawa, Norimoto Gotoh, Chikashi TeraoAbstract:Objectives:We undertook descriptive epidemiology of spot urine sodium-to-potassium ratio (Na/K) in a population sample to clarify the Close Relationship between Na/K and blood pressure level independently of potential confounding factors.Methods:Study participants consisted of 9144 apparently health
Doreen Dobritzsch - One of the best experts on this subject based on the ideXlab platform.
-
Dobritzsch D: The crystal structures of dihydropyrimidinases reaffirm the Close Relationship between cyclic amidohydrolases and explain their substrate specificity
2015Co-Authors: Bernhard Lohkamp, Birgit Andersen, Jure Piskur, Doreen DobritzschAbstract:In eukaryotes, dihydropyrimidinase catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Here we describe the three-dimensional structures of dihydropyrimidinase from two eukaryotes, the yeast Saccharomyces kluyveri and the slime mold Dictyostelium discoideum, determined and refined to 2.4 Å and 2.05 Å, respectively. Both enzymes have a (/)8-barrel structural core embedding the catalytic di-zinc centre, which is accompanied by a smaller -sandwich domain. Despite loop-forming insertions in the sequence of the yeast enzyme, the overall structures and architectures of the active sites of the dihydropyrimidinases are strikingly similar to each other, as well as to those of hydantoinases, dihydroorotase and other members of the amidohydrolase superfamily of enzymes. However, formation of the physiologically relevant tetramer shows subtle but nonetheless significant differences. The extension of one of the sheets of the -sandwich domain across a subunit-subunit interface in yeast dihydropyrimidinase underlines its Closer evolutionary Relationship to hydantoinases, while the slime mold enzyme shows higher similarity to the non-catalytic collapsin-response mediator proteins involved in neuron development. Catalysis is expected to follow a dihydroorotase-like mechanism, but in the opposite direction and with a different substrate
-
the crystal structures of dihydropyrimidinases reaffirm the Close Relationship between cyclic amidohydrolases and explain their substrate specificity
Journal of Biological Chemistry, 2006Co-Authors: Bernhard Lohkamp, Birgit Andersen, Jure Piskur, Doreen DobritzschAbstract:In eukaryotes, dihydropyrimidinase catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Here we describe the three-dimensional structures of dihydropyrimidinase from two eukaryotes, the yeast Saccharomyces kluyveri and the slime mold Dictyostelium discoideum, determined and refined to 2.4 and 2.05 angstroms, respectively. Both enzymes have a (beta/alpha)8-barrel structural core embedding the catalytic di-zinc center, which is accompanied by a smaller beta-sandwich domain. Despite loop-forming insertions in the sequence of the yeast enzyme, the overall structures and architectures of the active sites of the dihydropyrimidinases are strikingly similar to each other, as well as to those of hydantoinases, dihydroorotases, and other members of the amidohydrolase superfamily of enzymes. However, formation of the physiologically relevant tetramer shows subtle but nonetheless significant differences. The extension of one of the sheets of the beta-sandwich domain across a subunit-subunit interface in yeast dihydropyrimidinase underlines its Closer evolutionary Relationship to hydantoinases, whereas the slime mold enzyme shows higher similarity to the noncatalytic collapsin-response mediator proteins involved in neuron development. Catalysis is expected to follow a dihydroorotase-like mechanism but in the opposite direction and with a different substrate. Complexes with dihydrouracil and N-carbamyl-beta-alanine obtained for the yeast dihydropyrimidinase reveal the mode of substrate and product binding and allow conclusions about what determines substrate specificity, stereoselectivity, and the reaction direction among cyclic amidohydrolases.
Yasuharu Tabara - One of the best experts on this subject based on the ideXlab platform.
-
descriptive epidemiology of spot urine sodium to potassium ratio clarified Close Relationship with blood pressure level the nagahama study
Journal of Hypertension, 2015Co-Authors: Yasuharu Tabara, Yoshimitsu Takahashi, Kyoko Kumagai, Kazuya Setoh, Takahisa Kawaguchi, Meiko Takahashi, Yuki Muraoka, Akitaka Tsujikawa, Norimoto Gotoh, Chikashi TeraoAbstract:Objectives:We undertook descriptive epidemiology of spot urine sodium-to-potassium ratio (Na/K) in a population sample to clarify the Close Relationship between Na/K and blood pressure level independently of potential confounding factors.Methods:Study participants consisted of 9144 apparently health
Andres Alberto Rodriguez - One of the best experts on this subject based on the ideXlab platform.
-
Close Relationship between the state of the oxygen evolving complex and rice cold stress tolerance
Plant Science, 2020Co-Authors: Juan Manuel Vilas, Mariana G Corigliano, Marina Clemente, Santiago Javier Maiale, Andres Alberto RodriguezAbstract:Abstract The results of the present work suggested a Relationship between the growth stability and functional/structural parameters associated to the primary photochemistry and oxygen evolving complex (OEC) in tolerant rice plants under suboptimal low temperatures (SLT) stress. This was concluded from the absence of changes in net photosynthetic rate and in fraction of reaction centers to reduce quinone A, and very small changes in P680 efficiency to trap and donate electrons to quinone A and in fraction of active OEC in tolerant plants under cold stress but not in sensitive plants. The SLT stress also induced OEC activity limitations in both genotypes, but in a greater extent in sensitive plants. However, an assay using an artificial electron donor to replace OEC indicated that the P680+ capacity to accept electrons was not altered in both genotypes under SLT stress from the beginning of the stress treatment, suggesting that the OEC structure stability is related to rice SLT tolerance to sustain the photosynthesis. This hypothesis was also supported by the fact that tolerant plants but not sensitive plants did not alter the gene expression and protein content of PsbP under SLT stress, an OEC subunit with a role in stabilizing of OEC structure.
Bernhard Lohkamp - One of the best experts on this subject based on the ideXlab platform.
-
Dobritzsch D: The crystal structures of dihydropyrimidinases reaffirm the Close Relationship between cyclic amidohydrolases and explain their substrate specificity
2015Co-Authors: Bernhard Lohkamp, Birgit Andersen, Jure Piskur, Doreen DobritzschAbstract:In eukaryotes, dihydropyrimidinase catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Here we describe the three-dimensional structures of dihydropyrimidinase from two eukaryotes, the yeast Saccharomyces kluyveri and the slime mold Dictyostelium discoideum, determined and refined to 2.4 Å and 2.05 Å, respectively. Both enzymes have a (/)8-barrel structural core embedding the catalytic di-zinc centre, which is accompanied by a smaller -sandwich domain. Despite loop-forming insertions in the sequence of the yeast enzyme, the overall structures and architectures of the active sites of the dihydropyrimidinases are strikingly similar to each other, as well as to those of hydantoinases, dihydroorotase and other members of the amidohydrolase superfamily of enzymes. However, formation of the physiologically relevant tetramer shows subtle but nonetheless significant differences. The extension of one of the sheets of the -sandwich domain across a subunit-subunit interface in yeast dihydropyrimidinase underlines its Closer evolutionary Relationship to hydantoinases, while the slime mold enzyme shows higher similarity to the non-catalytic collapsin-response mediator proteins involved in neuron development. Catalysis is expected to follow a dihydroorotase-like mechanism, but in the opposite direction and with a different substrate
-
the crystal structures of dihydropyrimidinases reaffirm the Close Relationship between cyclic amidohydrolases and explain their substrate specificity
Journal of Biological Chemistry, 2006Co-Authors: Bernhard Lohkamp, Birgit Andersen, Jure Piskur, Doreen DobritzschAbstract:In eukaryotes, dihydropyrimidinase catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Here we describe the three-dimensional structures of dihydropyrimidinase from two eukaryotes, the yeast Saccharomyces kluyveri and the slime mold Dictyostelium discoideum, determined and refined to 2.4 and 2.05 angstroms, respectively. Both enzymes have a (beta/alpha)8-barrel structural core embedding the catalytic di-zinc center, which is accompanied by a smaller beta-sandwich domain. Despite loop-forming insertions in the sequence of the yeast enzyme, the overall structures and architectures of the active sites of the dihydropyrimidinases are strikingly similar to each other, as well as to those of hydantoinases, dihydroorotases, and other members of the amidohydrolase superfamily of enzymes. However, formation of the physiologically relevant tetramer shows subtle but nonetheless significant differences. The extension of one of the sheets of the beta-sandwich domain across a subunit-subunit interface in yeast dihydropyrimidinase underlines its Closer evolutionary Relationship to hydantoinases, whereas the slime mold enzyme shows higher similarity to the noncatalytic collapsin-response mediator proteins involved in neuron development. Catalysis is expected to follow a dihydroorotase-like mechanism but in the opposite direction and with a different substrate. Complexes with dihydrouracil and N-carbamyl-beta-alanine obtained for the yeast dihydropyrimidinase reveal the mode of substrate and product binding and allow conclusions about what determines substrate specificity, stereoselectivity, and the reaction direction among cyclic amidohydrolases.
