Ci Ji Lim

This study identifies a RPA-Trt1TERT-Tpz1TPP1 complex in fission yeast that promotes telomere extension and suppresses recombination through specific protein interactions.

This study shows that LEA proteins can reduce orientation bias and improve particle-orientation distributions in cryo-EM by mitigating air-water interface damage.

This study determines the cryo-EM structures of HSV-1 helicase-primase complex with and without inhibitors, revealing how pritelivir and amenamevir block helicase activity.

The paper shows small LEA proteins protect fragile samples from air-water interface damage during cryo-EM plunge freezing, improving structural determination of multisubunit complexes.

This study identifies RPA as a telomerase processivity factor essential for telomere maintenance and shows its role in telomere-related diseases.