The Ability of Sos1 to Oligomerize the Adaptor Protein LAT Is Separable from Its Guanine Nucleotide Exchange Activity in Vivo
Copyright policy )The Ability of Sos1 to Oligomerize the Adaptor Protein LAT Is Separable from Its Guanine Nucleotide Exchange Activity in Vivo
Thymocyte development requires that Sos1 acts both as a guanine nucleotide exchange factor and as a scaffold to cluster adaptor proteins.
- National Institutes of Health United States
- National Cancer Institute United States
- National Institute of Health Pakistan
Male, Nucleotides, T-Lymphocytes, Receptors, Antigen, T-Cell, Membrane Proteins, Cell Differentiation, Mice, Transgenic, Phosphoproteins, Mice, Gene Expression Regulation, Mutation, Animals, Calcium Signaling, Phosphorylation, Extracellular Signal-Regulated MAP Kinases, SOS1 Protein, Adaptor Proteins, Signal Transducing, Cell Proliferation, GRB2 Adaptor Protein, Signal Transduction
Male, Nucleotides, T-Lymphocytes, Receptors, Antigen, T-Cell, Membrane Proteins, Cell Differentiation, Mice, Transgenic, Phosphoproteins, Mice, Gene Expression Regulation, Mutation, Animals, Calcium Signaling, Phosphorylation, Extracellular Signal-Regulated MAP Kinases, SOS1 Protein, Adaptor Proteins, Signal Transducing, Cell Proliferation, GRB2 Adaptor Protein, Signal Transduction
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