Lie Min, Ph.D.
Affiliations: | 2008 | Biochemistry, Biophysics, and Molecular Biology | Iowa State University, Ames, IA, United States |
Area:
Nuclear magnetic resonance, Macromolecular structure and recognitionGoogle:
"Lie Min"Mean distance: 8.15 | S | N | B | C | P |
Parents
Sign in to add mentor| Amy H. Andreotti | grad student | 2008 | Iowa State | |
| (Interleukin-2-tyrosine kinase substrate docking and its regulation by an intramolecular interaction in phospholipase Cgamma1.) | ||||
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Publications
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| Devkota S, Joseph RE, Min L, et al. (2015) Scaffold Protein SLP-76 Primes PLCγ1 for Activation by ITK-Mediated Phosphorylation. Journal of Molecular Biology |
| Zhao H, Wang R, Tao Z, et al. (2014) Activation of T-LAK-cell-originated protein kinase-mediated antioxidation protects against focal cerebral ischemia-reperfusion injury. The Febs Journal. 281: 4411-20 |
| Levytskyy RM, Hirve N, Guimond DM, et al. (2012) In Vivo Consequences of Disrupting SH3-Mediated Interactions of the Inducible T-Cell Kinase. Journal of Signal Transduction. 2012: 694386 |
| Min L, Wu W, Joseph RE, et al. (2010) Disrupting the intermolecular self-association of Itk enhances T cell signaling. Journal of Immunology (Baltimore, Md. : 1950). 184: 4228-35 |
| Min L, Joseph RE, Fulton DB, et al. (2009) Itk tyrosine kinase substrate docking is mediated by a nonclassical SH2 domain surface of PLCgamma1. Proceedings of the National Academy of Sciences of the United States of America. 106: 21143-8 |
| Joseph RE, Severin A, Min L, et al. (2009) SH2-dependent autophosphorylation within the Tec family kinase Itk. Journal of Molecular Biology. 391: 164-77 |
| Joseph RE, Min L, Xu R, et al. (2007) A remote substrate docking mechanism for the tec family tyrosine kinases. Biochemistry. 46: 5595-603 |
| Joseph RE, Min L, Andreotti AH. (2007) The linker between SH2 and kinase domains positively regulates catalysis of the Tec family kinases. Biochemistry. 46: 5455-62 |
| Min L, Fulton DB, Andreotti AH. (2005) A case study of proline isomerization in cell signaling. Frontiers in Bioscience : a Journal and Virtual Library. 10: 385-97 |