Entry ID | Original Release date | Data summary | Entry Title | Citation Title(s) | Authors |
---|---|---|---|---|---|
19702 | 2014-04-11 | Chemical Shifts: 1 set |
Structure of the dimerization domain of the human polyoma, JC virus agnoprotein is an amphipathic alpha-helix. |
1: Human polyomavirus JC small regulatory agnoprotein forms highly stable dimers and oligomers: implications for their roles in agnoprotein function. 2: Nuclear magnetic resonance structure revealed that human polyoma JC virus agnoprotein contains an alpha-helix encompassing the Leu/Ile/Phe-rich domain. 3: Nuclear magnetic resonance structure revealed that human polyoma, JC virus agnoprotein contains an alpha-helix encompassing the Leu/Ile/Phe-rich domain |
A Sami Saribas, E R Viola, Magid Abou-Gharbia, Mahmut Safak, Martyn K White, Martyn White, M K White, M Safak, Pascale Coric, Sami A Saribas, Serge Bouaziz, T B Arachea, Wayne Childers |