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Entry ID	Original Release date	Data summary	Entry Title	Citation Title	Authors
27926	2020-03-05	Chemical Shifts: 1 set Spectral_peak_list: 2 sets	RTNLB13_APH_16	Revealing the mechanism of protein-lipid interactions for a putative membrane curvature sensor in plant endoplasmic reticulum	Ann M Dixon, Rhiannon L Brooks
27927	2020-03-05	Chemical Shifts: 1 set Spectral_peak_list: 2 sets	RTNLB13_APH_18	Revealing the mechanism of protein-lipid interactions for a putative membrane curvature sensor in plant endoplasmic reticulum	Ann M Dixon, Rhiannon L Brooks
27928	2020-03-05	Chemical Shifts: 1 set Spectral_peak_list: 2 sets	RTNLB13_APH_22	Revealing the mechanism of protein-lipid interactions for a putative membrane curvature sensor in plant endoplasmic reticulum	Ann M Dixon, Rhiannon L Brooks
19297	2013-06-28	Chemical Shifts: 1 set	Chemical shift assignments of the human C-type lectin DC-SIGNR (Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non-integrin related) carbohydrate recognition domain in the holo (calcium bound) form.	Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR protein reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.	Ann M Dixon, Daniel A Mitchell, Fay Probert, Max Crispin, Sara B-M Whittaker