| Entry ID |
Data summary |
Entry Title |
Citation Title |
Authors |
| 5039 |
Chemical Shifts: 1 set
|
Solution Structure of Ptu1, a Toxin from the Assassin bug Peirates turpis that blocks the Voltage-sensitive Calcium Channel N-type |
Solution Structure of Ptu1, a Toxin from the Assassin bug Peirates turpis that blocks the Voltage-sensitive Calcium Channel N-type
|
Amor Mosbah, Cedric Bernard, Gerardo Corzo, Herve Darbon, Terumi Nakajima |
| 4541 |
Chemical Shifts: 1 set
|
Solution Structure of the Potassium Channel Scorpion Toxin HsTX1 |
Structural and functional consequences of the presence of a fourth disulfide bridge in the scorpion short toxins: Solution structure of the potassium channel inhibitor HsTX1
|
Andre Menez, Bernard Gilquin, Bruno Lebrun, Philippe Savarin, Regine Romi-Lebrun, Sophie Zinn-Justin, Terumi Nakajima |
| 4190 |
Chemical Shifts: 1 set
|
BmTX1 Toxin from Scorpion Buthus martensii Karsch |
Solution Structure of two new Toxins from the Venom of the Chinese Scorpion Buthus martensii Karsch Blockers of Potassium Channels
|
E Blanc, H Darbon, O Bornet, R Romi-Lebrun, T Nakajima |
| 4191 |
Chemical Shifts: 1 set
|
BmTX2 Toxin from Scorpion Buthus martensii Karsch |
Solution Structure of two new Toxins from the Venom of the Chinese Scorpion Buthus martensii Karsch Blockers of Potassium Channels
|
E Blanc, H Darbon, O Bornet, R Romi-Lebrun, T Nakajima |
| 1728 |
Chemical Shifts: 1 set
|
Solution conformation of endothelin determined by means of 1H-NMR spectroscopy and distance geometry calculations |
Solution conformation of endothelin determined by means of 1H-NMR spectroscopy and distance geometry calculations
|
Haruhiko Tamaoki, Kiichiro Nakajima, Shigenori Nishimura, Shin-ichiro Kumagaye, Shumpei Sakakibara, Tadayasu Ohkubo, Terutoshi Kimura, Yoshimasa Kyogoku, Yuji Kobayashi |
| 779 |
Chemical Shifts: 1 set
|
A 1H-NMR Study of the Solution Conformation of Icaria chemotactic peptide and its [Lys7] analog: Effects on the physiological activity of a substitution of proline to lysine at position 7 |
A 1H-NMR Study of the Solution Conformation of Icaria chemotactic peptide and its [Lys7] analog: Effects on the physiological activity of a substitution of proline to lysine at position 7
|
Chieko Kitada, Ichio Shimada, Kazuki Saito, Koichi Kato, Masahiko Fujino, Terumi Nakajima, Yoji Arata |
