Dimerization in MAP-kinase signaling.
暂无分享,去创建一个
[1] E. Nishida,et al. Interaction of MAP kinase with MAP kinase kinase: its possible role in the control of nucleocytoplasmic transport of MAP kinase , 1997, The EMBO journal.
[2] P. Cohen,et al. EGF triggers neuronal differentiation of PC12 cells that overexpress the EGF receptor , 1994, Current Biology.
[3] S. Green,et al. PC12 cell neuronal differentiation is associated with prolonged p21ras activity and consequent prolonged ERK activity , 1992, Neuron.
[4] J E Ferrell,et al. The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. , 1998, Science.
[5] T. Hunter,et al. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. , 1988, Science.
[6] C. Marshall,et al. Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation , 1995, Cell.
[7] E. Nishida,et al. Two co‐existing mechanisms for nuclear import of MAP kinase: passive diffusion of a monomer and active transport of a dimer , 1999, The EMBO journal.
[8] E. Goldsmith,et al. Phosphorylation of MAP Kinases by MAP/ERK Involves Multiple Regions of MAP Kinases* , 1999, The Journal of Biological Chemistry.
[9] Arthur Weiss,et al. Switching Signals On or Off by Receptor Dimerization , 1998, Cell.
[10] E. Goldsmith,et al. Phosphorylation of the MAP Kinase ERK2 Promotes Its Homodimerization and Nuclear Translocation , 1998, Cell.
[11] E. Nishida,et al. Cytoplasmic Localization of Mitogen-activated Protein Kinase Kinase Directed by Its NH2-terminal, Leucine-rich Short Amino Acid Sequence, Which Acts as a Nuclear Export Signal* , 1996, The Journal of Biological Chemistry.
[12] J. Wilsbacher,et al. The N-terminal ERK-binding Site of MEK1 Is Required for Efficient Feedback Phosphorylation by ERK2 in Vitro and ERK Activation in Vivo * , 1999, The Journal of Biological Chemistry.
[13] E. Goldsmith,et al. How MAP Kinases Are Regulated (*) , 1995, The Journal of Biological Chemistry.
[14] Roger Y Tsien,et al. Identification of a signal for rapid export of proteins from the nucleus , 1995, Cell.
[15] Minoru Yoshida,et al. CRM1 is responsible for intracellular transport mediated by the nuclear export signal , 1997, Nature.
[16] E. Goldsmith,et al. A constitutively active and nuclear form of the MAP kinase ERK2 is sufficient for neurite outgrowth and cell transformation , 1998, Current Biology.
[17] E. Goldsmith,et al. The structure of mitogen-activated protein kinase p38 at 2.1-A resolution. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[18] E. Elion,et al. Nuclear Shuttling of Yeast Scaffold Ste5 Is Required for Its Recruitment to the Plasma Membrane and Activation of the Mating MAPK Cascade , 1999, Cell.
[19] A. Brunet,et al. Growth Factor–induced p42/p44 MAPK Nuclear Translocation and Retention Requires Both MAPK Activation and Neosynthesis of Nuclear Anchoring Proteins , 1998, The Journal of cell biology.
[20] T. Clackson,et al. A hot spot of binding energy in a hormone-receptor interface , 1995, Science.
[21] A. Brunet,et al. Nuclear translocation of p42/p44 mitogen‐activated protein kinase is required for growth factor‐induced gene expression and cell cycle entry , 1999, The EMBO journal.
[22] E. Goldsmith,et al. Autophosphorylation activates the soluble cytoplasmic domain of the insulin receptor in an intermolecular reaction. , 1989, The Journal of biological chemistry.
[23] Elizabeth J. Goldsmith,et al. Activation Mechanism of the MAP Kinase ERK2 by Dual Phosphorylation , 1997, Cell.
[24] Masahiko Hibi,et al. c-Jun Can Recruit JNK to Phosphorylate Dimerization Partners via Specific Docking Interactions , 1996, Cell.
[25] N. Osheroff,et al. Extracellular Signal-Regulated Kinase Activates Topoisomerase IIα through a Mechanism Independent of Phosphorylation , 1999, Molecular and Cellular Biology.
[26] Paul R. Caron,et al. Crystal Structure of p38 Mitogen-activated Protein Kinase* , 1996, The Journal of Biological Chemistry.
[27] P. Caron,et al. Crystal structure of JNK3: a kinase implicated in neuronal apoptosis. , 1998, Structure.
[28] Elizabeth J. Goldsmith,et al. Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution , 1994, Nature.