スポンサーリンク
Department of Biological Sciences, Graduate School of Science, osaka university | 論文
- A role of RnlA in the RNase LS activity from Escherichia coli
- 2P154 異核種スピンラベル間の双極子相互作用EPRによる骨格筋アクチン-トロポミオシン間の距離分布計測(筋肉(筋蛋白質・収縮),第48回日本生物物理学会年会)
- 3P001 リン酸化された心筋トロポニンC-トロポニンI複合体のパルスESRを用いた構造解析(蛋白質-構造,第48回日本生物物理学会年会)
- The Apoptosis-Inducing Protein Kinase DRAK2 Is Inhibited in a Calcium-Dependent Manner by the Calcium-Binding Protein CHP
- An Aspartate Aminotransferase from an Extremely Thermophilic Bacterium, Thermus thermophilus HB8^1
- An O^6-methylguanine-DNA Methyltransferase-like Protein from Thermus thermophilus Interacts with a Nucleotide Excision Repair Protein
- Crystal Structure of TTHA0252 from Thermus thermophilus HB8, a RNA Degradation Protein of the Metallo-β-lactamase Superfamily
- Novel Reaction Mechanism of GTP Cyclohydrolase I. High-Resolution X-Ray Crystallography of Thermus thermophilus HB8 Enzyme Complexed with a Transition State Analogue, the 8-Oxoguanine Derivative
- Crystal Structure of Thermus thermophilus HB8 UvrB Protein, a Key Enzyme of Nucleotide Excision Repair
- Saccharomyces cerevisiae Na^+/H^+ Antiporter Nha1p Associates with Lipid Rafts and Requires Sphingolipid for Stable Localization to the Plasma Membrane
- 1P001 心筋収縮制御タンパク質トロポニンのESRを用いた動的構造解析(蛋白質-構造,第48回日本生物物理学会年会)
- 3TA5-04 筋収縮制御タンパク質トロポニンの二量子コヒーレンスESRによる構造解析(蛋白質-構造,第47回日本生物物理学会年会)
- RecA Protein Has Extremely High Cooperativity for substrate in Its ATPase Activity^1
- Synthesis of a New Water Soluble 2,2-Bifunctionalized Spin Label and Its Application to Troponin C
- Calcium Imaging for Detection and Estimation of Spike Activities in Aplysia Neurons(Physiology)
- Oligocene-Early Miocene Molluscs and Diatoms from the Kitami-Tsubetsu area, Eastern Hokkaido, Japan
- Application of Bis(terpyridine)ruthenium(II) to N-terminal amino acid sequencing
- 2P-148 SDSL-ESRを用いた心筋トロポニンの動的構造変化(筋肉(筋蛋白質・収縮),第46回日本生物物理学会年会)
- Biochemical Characterization of TT1383 from Thermus thermophilus Identifies a Novel dNTP Triphosphohydrolase Activity Stimulated by dATP and dTTP
- Thermus thermophilus MutS2, a MutS Paralogue, Possesses an Endonuclease Activity Promoted by MutL
スポンサーリンク