Ontology highlight
ABSTRACT:
SUBMITTER: Kuang Y
PROVIDER: S-EPMC4200273 | biostudies-literature | 2014 Oct
REPOSITORIES: biostudies-literature
Kuang Yi Y Long Marcus J C MJ Zhou Jie J Shi Junfeng J Gao Yuan Y Xu Chen C Hedstrom Lizbeth L Xu Bing B
The Journal of biological chemistry 20140825 42
Emerging evidence reveals that prion-like structures play important roles to maintain the well-being of cells. Although self-assembly of small molecules also affords prion-like nanofibrils (PriSM), little is known about the functions and mechanisms of PriSM. Previous works demonstrated that PriSM formed by a dipeptide derivative selectively inhibiting the growth of glioblastoma cells over neuronal cells and effectively inhibiting xenograft tumor in animal models. Here we examine the protein targ ...[more]