Takashi Ohtsu

RNA aptamers selected against the receptor activator of NF-κB acquire general affinity to proteins of the tumor necrosis factor receptor family

Mori, Tadashi, Oguro, Akihiro, Ohtsu, Takashi, Nakamura, Yoshikazu

The receptor activator of NF-κB (RANK) is a member of the tumor necrosis factor (TNF) receptor family and acts to cause osteoclastgenesis through the interaction with its ligand, RANKL. We isolated...

NMR structures of double loops of an RNA aptamer against mammalian initiation factor 4A

Sakamoto, Taiichi, Oguro, Akihiro, Kawai, Gota, Ohtsu, Takashi, Nakamura, Yoshikazu

A high affinity RNA aptamer (APT58, 58 nt long) against mammalian initiation factor 4A (eIF4A) requires nearly its entire nucleotide sequence for efficient binding. Since splitting either APT58 or...

RNA aptamers to initiation factor 4A helicase hinder cap-dependent translation by blocking ATP hydrolysis

OGURO, AKIHIRO, OHTSU, TAKASHI, SVITKIN, YURI V., SONENBERG, NAHUM, NAKAMURA, YOSHIKAZU

The mammalian translation initiation factor 4A (eIF4A) is a prototype member of the DEAD-box RNA helicase family that couples ATPase activity to RNA binding and unwinding. In the crystal form, eIF4A...

High affinity RNA for mammalian initiation factor 4E interferes with mRNA-cap binding and inhibits translation

MOCHIZUKI, KIYOTAKA, OGURO, AKIHIRO, OHTSU, TAKASHI, SONENBERG, NAHUM, NAKAMURA, YOSHIKAZU

The eukaryotic translation initiation factor 4F (eIF4F) consists of three polypeptides (eIF4A, eIF4G, and eIF4E) and is responsible for recruiting ribosomes to mRNA. eIF4E recognizes the mRNA...

RNA aptamers selected against the receptor activator of NF-κB acquire general affinity to proteins of the tumor necrosis factor receptor family

Mori, Tadashi, Oguro, Akihiro, Ohtsu, Takashi, Nakamura, Yoshikazu

The receptor activator of NF-κB (RANK) is a member of the tumor necrosis factor (TNF) receptor family and acts to cause osteoclastgenesis through the interaction with its ligand, RANKL. We isolated...

NMR structures of double loops of an RNA aptamer against mammalian initiation factor 4A

Sakamoto, Taiichi, Oguro, Akihiro, Kawai, Gota, Ohtsu, Takashi, Nakamura, Yoshikazu

A high affinity RNA aptamer (APT58, 58 nt long) against mammalian initiation factor 4A (eIF4A) requires nearly its entire nucleotide sequence for efficient binding. Since splitting either APT58 or...

RNA aptamers to initiation factor 4A helicase hinder cap-dependent translation by blocking ATP hydrolysis

OGURO, AKIHIRO, OHTSU, TAKASHI, SVITKIN, YURI V., SONENBERG, NAHUM, NAKAMURA, YOSHIKAZU

The mammalian translation initiation factor 4A (eIF4A) is a prototype member of the DEAD-box RNA helicase family that couples ATPase activity to RNA binding and unwinding. In the crystal form, eIF4A...

High affinity RNA for mammalian initiation factor 4E interferes with mRNA-cap binding and inhibits translation

MOCHIZUKI, KIYOTAKA, OGURO, AKIHIRO, OHTSU, TAKASHI, SONENBERG, NAHUM, NAKAMURA, YOSHIKAZU

The eukaryotic translation initiation factor 4F (eIF4F) consists of three polypeptides (eIF4A, eIF4G, and eIF4E) and is responsible for recruiting ribosomes to mRNA. eIF4E recognizes the mRNA...

RNA aptamers to mammalian initiation factor 4G inhibit cap-dependent translation by blocking the formation of initiation factor complexes

Miyakawa, Shin, Oguro, Akihiro, Ohtsu, Takashi, Imataka, Hiroaki, Sonenberg, Nahum, Nakamura, Yoshikazu

Eukaryotic translation initiation factor 4G (eIF4G) plays a crucial multimodulatory role in mRNA translation and decay by interacting with other translation factors and mRNA-associated proteins. In...