Kenji Kamata

Structural basis for chemical inhibition of human blood coagulation factor Xa

Kamata, Kenji, Kawamoto, Hiroshi, Honma, Teruki, Iwama, Toshiharu, Kim, Sung-Hou

Factor Xa, the converting enzyme of prothrombin to thrombin, has emerged as an alternative (to thrombin) target for drug discovery for thromboembolic diseases. An inhibitor has been synthesized and...

Structural basis of nonnatural amino acid recognition by an engineered aminoacyl-tRNA synthetase for genetic code expansion

Kobayashi, Takatsugu, Sakamoto, Kensaku, Takimura, Tetsuo, Sekine, Ryo, Vincent, Kelly, Kamata, Kenji, ...

The genetic code in a eukaryotic system has been expanded by the engineering of Escherichia coli tyrosyl-tRNA synthetase (TyrRS) with the Y37V and Q195C mutations (37V195C), which specifically...

Structural basis for chemical inhibition of human blood coagulation factor Xa

Kamata, Kenji, Kawamoto, Hiroshi, Honma, Teruki, Iwama, Toshiharu, Kim, Sung-Hou

Factor Xa, the converting enzyme of prothrombin to thrombin, has emerged as an alternative (to thrombin) target for drug discovery for thromboembolic diseases. An inhibitor has been synthesized and...

Structural basis of nonnatural amino acid recognition by an engineered aminoacyl-tRNA synthetase for genetic code expansion

Kobayashi, Takatsugu, Sakamoto, Kensaku, Takimura, Tetsuo, Sekine, Ryo, Vincent, Kelly, Kamata, Kenji, ...

The genetic code in a eukaryotic system has been expanded by the engineering of Escherichia coli tyrosyl-tRNA synthetase (TyrRS) with the Y37V and Q195C mutations (37V195C), which specifically...