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1.
Int Rev Immunol ; 34(1): 50-66, 2015 Jan.
Article in English | MEDLINE | ID: mdl-25019278

ABSTRACT

The mammalian target of rapamycin (mTOR), a phosphoinositide-3-kinase-related protein kinase, acts as a rheostat capable of integrating a variety of environmental cues in the form of nutrients, energy, and growth factors to modulate organismal processes and homeostasis. Recently, there is a growing appreciation of mTOR in adaptive immunity for its crucial roles in keeping a proper balance between T cell quiescence and activation. Under steady-state circumstances, mTOR is subtly inhibited by multiple mechanisms to maintain normal T cell homeostasis. Antigen recognition by naïve T cells leads to mTOR activation, which subsequently promotes the differentiation of these cells into distinct effector T cell subsets. This review focuses primarily on the recent literature with respect to the regulatory effects and mechanisms of mTOR signaling in dictating T cell fate, and discusses the therapeutic implications of mTOR modulation in T-cell-mediated autoimmunity.


Subject(s)
Adaptive Immunity , Autoimmune Diseases/metabolism , Autoimmunity , T-Lymphocyte Subsets/metabolism , T-Lymphocytes/metabolism , TOR Serine-Threonine Kinases/immunology , Autoimmune Diseases/drug therapy , Autoimmune Diseases/genetics , Autoimmune Diseases/pathology , Cell Differentiation , Cytokines/genetics , Cytokines/immunology , Energy Metabolism/immunology , Gene Expression Regulation , Homeostasis , Humans , Immunity, Innate , Immunologic Factors/therapeutic use , Lymphocyte Activation , Signal Transduction , T-Lymphocyte Subsets/cytology , T-Lymphocyte Subsets/immunology , T-Lymphocytes/cytology , T-Lymphocytes/immunology , TOR Serine-Threonine Kinases/genetics
2.
Acta Crystallogr Sect E Struct Rep Online ; 67(Pt 11): o3134, 2011 Nov.
Article in English | MEDLINE | ID: mdl-22220136

ABSTRACT

The title compound, C(6)H(5)ClN(2)O(2), crystallizes with two independent mol-ecules in the asymmetric unit. Inter-molecular C-H⋯O hydrogen bonds stabilize the crystal structure.

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