Normal view

Received — 13 April 2026 ⏭ Journals

Cell Death Discovery nature.com science feeds
NAT10 promotes cisplatin resistance and immune escape by increasing the expression of DUSP1 and PD-L1 in gastric cancer Lilin Qian · Wenrong Gao · Xinyi Wang · Shuqi Cui · Xiaoqi Han · Xia Xu · Jihui Jia · Zhifang Liu
Cell Death Discovery, Published online: 10 April 2026; doi:10.1038/s41420-026-03107-wNAT10 promotes cisplatin resistance and immune escape by increasing the expression of DUSP1 and PD-L1 in gastric cancer
10 April 2026 at 08:00

NAT10 promotes cisplatin resistance and immune escape by increasing the expression of DUSP1 and PD-L1 in gastric cancer

Cell Death Discovery nature.com science feeds

By: Lilin Qian · Wenrong Gao · Xinyi Wang · Shuqi Cui · Xiaoqi Han · Xia Xu · Jihui Jia · Zhifang Liu

10 April 2026 at 08:00

Cell Death Discovery, Published online: 10 April 2026; doi:10.1038/s41420-026-03107-w

NAT10 promotes cisplatin resistance and immune escape by increasing the expression of DUSP1 and PD-L1 in gastric cancer

Received — 14 March 2026 ⏭ Journals

Nature - Issue - nature.com science feeds
Structures of Marburgvirus glycoprotein and its complex with NPC1 receptor Gang Ye · Fan Bu · Hailey Turner-Hubbard · Morgan Herbst · Lanying Du · Ge Yang · Bin Liu · Fang Li
Nature, Published online: 11 March 2026; doi:10.1038/s41586-026-10240-0Marburgvirus glycoprotein binds to the endosomal receptor NPC1 in a distinct orientation with higher affinity compared with Ebola virus glycoprotein, accompanied by fusion-relevant rearrangements, enabling more efficient viral entry.
11 March 2026 at 08:00

Structures of Marburgvirus glycoprotein and its complex with NPC1 receptor

Nature - Issue - nature.com science feeds

By: Gang Ye · Fan Bu · Hailey Turner-Hubbard · Morgan Herbst · Lanying Du · Ge Yang · Bin Liu · Fang Li

11 March 2026 at 08:00

Nature, Published online: 11 March 2026; doi:10.1038/s41586-026-10240-0

Marburgvirus glycoprotein binds to the endosomal receptor NPC1 in a distinct orientation with higher affinity compared with Ebola virus glycoprotein, accompanied by fusion-relevant rearrangements, enabling more efficient viral entry.