_id,doi,title
8927,10.1111/liv.14730,Pathophysiological mechanisms of liver injury in COVID-19
9262,10.1126/sciadv.abd9153,Optimal anchoring of a foldamer inhibitor of ASF1 histone chaperone through backbone plasticity
9016,10.1002/cbic.201800633,"Recognition of ASF1 by using hydrocarbon‐constrained peptides"
9018,10.1016/j.chembiol.2019.09.002,Design on a rational basis of high-affinity peptides inhibiting the histone chaperone ASF1
9019,10.1016/j.crci.2015.12.004,"Targeting protein–protein interactions, a wide open field for drug design"
9017,10.1093/nar/gkv021,Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork