Topological Mutation of Escherichia coli Dihydrofolate Reductase
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概要
- 論文の詳細を見る
- Japanese Biochemical Societyの論文
- 1998-10-01
著者
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TAKENAWA Tatsuyuki
National Institute of Bioscience and Human Technology
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Iwakura Masahiro
National Institute Of Bioscience And Human-technology
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Iwakura Masahiro
National Institute For Advanced Interdisciplinary Research
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Nakamura Tsutomu
National Inst. Advanced Industrial Sci. And Technol. Osaka Jpn
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Takenawa Tatsuyuki
National Institute Of Bioscience And Human-technology
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TAKENAKA Tatsuyuki
National Institute of Bioscience and Human-Technology
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Nakamura Tsutomu
National Institute Of Bioscience And Human-technology
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- Cyanocysteine-Mediated Molecular Dissection of Dihydrofolate Reductase: Occurrence of Intra- and Inter-Molecular Reactions Forming a Peptide Bond
- Nano-Scale Monitoring of the Thermally-Induced Unfolding of Proteins Using Capillary Electrophoresis with In-Column Incubation
- Acceleration of The Dissection Reaction at Cyanocysteine Residue by Neighboring Lysine
- Identification of the Region Responsible for Fibril Formation in the CAD Domain of Caspase-Activated DNase
- Enzyme-inhibition system for identifying potential antimalarials that target highly drug-resistant mutants of Plasmodium falciparum dihydrofolate reductase
- Effects of Mutation at Methionine-42 of Escherichia coli Dihydrofolate Reductase on Stability and Function : Implication of Hydrophobic Interactions
- Introduction of Cysteine Residue to Engineered Cys-Free Dihydrofolate Reductase and Its Application for the Specific Molecular Dissection
- Effects of Point Mutations at the Flexible Loop Alanine-145 of Escherichia coli Dihydrofolate Reductase on Its Stability and Function^1
- Availability of Dihydrofolate Reductase Affinity Handle in Expressing Human Prolactin as a Soluble Fusion Protein
- In Search of Circular Permuted Variants of Escherichia coli Dihydrofolate Reductase
- Mass Spectrometric Analysis Using Ruthenium (II)-Labeling for Identification of Glycosyl Hydrolase Product
- Crystal structure of peroxiredoxin from Aeropyrum pernix K1 complexed with its substrate, hydrogen peroxide
- Stability and Reversibility of Thermal Denaturation Are Greatly Improved by Limiting Terminal Flexibility of Escherichia coli Dihydrofolate Reductase
- Topological Mutation of Escherichia coli Dihydrofolate Reductase
- Characterization and crystal structure of the thermophilic ROK hexokinase from Thermus thermophilus(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Characterization and crystal structure of the thermophilic ROK hexokinase from Thermus thermophilus
- Stability and Reversibility of Thermal Denaturation Are Greatly Improved by Limiting Terminal Flexibility of Escherichia coli Dihydrofolate Reductase.