Aqueous solubility of cystic fibrosis drug ivacaftor is ~200-fold lower, whereas the potency of its stimulatory effect on the CFTR channel is >100-fold higher, than reported, and is fully reversible.
A histone modification that alters the nucleosome structure occurs in mitosis and promotes chromosome packaging and the timely removal of condensin I and cohesion, to achieve chromosome segregation.
Genetic susceptibility to an infectious disease is linked to competition for binding a molecule on the bacterial surface by two host proteins with opposing roles in host immunity.
The combination of in vitro investigations, the zebrafish screening model and rodent experiments offered a unique approach to optimizing nanoparticles modified with Hepatitis B virus-derived peptides to specifically target hepatocytes.
The alpha-synuclein fibril structure reported here buries residues 50-57 at the interface between its two protofilaments, suggesting that familial Parkinson's disease associated mutations in these residues lead to a structure not compatible with the one presented here.
Analysis of the mechanism of action of cystic fibrosis corrector drugs reveals signalling pathways potently controlling the proteostasis of the main disease-relevant CFTR mutant.
