A new biology review in British Journal of Cancer argues that dynamic three-dimensional protein conformations—often missed by static structure-based design—may help explain why therapies lose effectiveness. The authors frame “dynamic conformational heterogeneity” as a driver of adaptive phenotypic plasticity and therapeutic resistance, describing proteins as fluctuating ensembles rather than single structures. In a separate preclinical and cell/mouse report, icariin was reported to calm nucleolar stress markers in Alzheimer’s disease models, with effects described in Aβ25–35-treated BV2 cells and APP/PS1 mice. The report positions icariin’s effects on nucleolar stress as a potential mechanistic angle for neurodegeneration interventions. Taken together, the items underscore renewed emphasis on conformational dynamics and cellular stress pathways as therapeutic discovery themes.