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Methods in Molecular Biology (Clifton, N.J.)|December 20, 2018
Structural and Biochemical Analyses of the Core Components of the Hippo PathwayLisheng Ni, Xuelian LuoElife|April 16, 2020
STK25 suppresses Hippo signaling by regulating SAV1-STRIPAK antagonismSung Jun Bae, Lisheng Ni, Xuelian LuoProceedings of the National Academy of Sciences of the United States of America|June 11, 2010
Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partitionLisheng Ni, Weijun Xu, Muthiah Kumaraswami, et al.Nucleic Acids Research|December 18, 2012
Structures of the Escherichia coli transcription activator and regulator of diauxie, XylR: an AraC DNA-binding family member with a LacI/GalR ligand-binding domainLisheng Ni, Nam K Tonthat, Nagababu Chinnam, et al.Genes & Development|June 26, 2015
Structural basis for Mob1-dependent activation of the core Mst-Lats kinase cascade in Hippo signalingLisheng Ni, Yonggang Zheng, Mayuko Hara, et al.Biochemistry|February 16, 2006
Cytidine 5'-monophosphate (CMP)-induced structural changes in a multifunctional sialyltransferase from Pasteurella multocidaLisheng Ni, Mingchi Sun, Hai Yu, et al.Nature Structural & Molecular Biology|February 26, 2021
Cryo-EM structure of the Hippo signaling integrator human STRIPAKByung-Cheon Jeong, Sung Jun Bae, Lisheng Ni, et al.Elife|October 25, 2017
SAV1 promotes Hippo kinase activation through antagonizing the PP2A phosphatase STRIPAKSung Jun Bae, Lisheng Ni, Adam Osinski, et al.Structure (London, England : 1993)|August 27, 2013
Structural basis for autoactivation of human Mst2 kinase and its regulation by RASSF5Lisheng Ni, Sheng Li, Jianzhong Yu, et al.Biochemistry|May 10, 2007
Crystal structures of Pasteurella multocida sialyltransferase complexes with acceptor and donor analogues reveal substrate binding sites and catalytic mechanismLisheng Ni, Harshal A Chokhawala, Hongzhi Cao, et al.Pageof 2