Entry ID | Original Release date | Data summary | Entry Title | Citation Title(s) | Authors | Additional Matches |
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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 | |
4461 | 2000-03-23 | Chemical Shifts: 1 set |
1H NMR Solution Structure of Cycloviolacin O1 - A Macro-cyclic Polypeptide Isolated from Viola odorat |
Plant Cyclotides - a unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural moti
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Clement Waine, David J Craik, Norelle L Daly, Trudy Bond | Common name: Viola |