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Description:
The immunophilins are a highly conserved family of cis-trans peptidyl-prolyl isomerases that bind to and mediate the effects of immunosuppressive drugs, such as cyclosporin, FK506 and rapamycin. Immunophilins have also been implicated in protein folding and trafficking within the endoplasmic reticulum (ER). FKBP11 (FK506-binding protein 11), also known as FKBP19 or peptidyl-prolyl cis-trans isomerase FKBP11, is a 201 amino acid single-pass membrane protein belonging to the FKBP-type PPIase family, a group of proteins known to catalyze the folding of proline-containing polypeptides. Containing one PPIase FKBP-type domain, FKBP11 is expressed in secretory tissues such as pancreas, pituitary, stomach, lymph node and salivary gland, and is encoded by a gene that maps to human chromosome 12q13.12. FK506 and rapamycin are known to inhibit FKBP11’s peptidyl-prolyl isomerase activity.
Description:
The immunophilins are a highly conserved family of cis-trans peptidyl-prolyl isomerases that bind to and mediate the effects of immunosuppressive drugs, such as cyclosporin, FK506 and rapamycin. Immunophilins have also been implicated in protein folding and trafficking within the endoplasmic reticulum (ER). FKBP11 (FK506-binding protein 11), also known as FKBP19 or peptidyl-prolyl cis-trans isomerase FKBP11, is a 201 amino acid single-pass membrane protein belonging to the FKBP-type PPIase family, a group of proteins known to catalyze the folding of proline-containing polypeptides. Containing one PPIase FKBP-type domain, FKBP11 is expressed in secretory tissues such as pancreas, pituitary, stomach, lymph node and salivary gland, and is encoded by a gene that maps to human chromosome 12q13.12. FK506 and rapamycin are known to inhibit FKBP11’s peptidyl-prolyl isomerase activity.
Description:
ECHS1 (Enoyl Coenzyme A hydratase, short chain, 1) catalyzes the hydration of 2-trans-enoyl-coenzyme A (CoA) intermediates to L-3-hydroxyacyl-CoAs, in the second step of the mitochondrial fatty acid beta-oxidation pathway.
Description:
Interleukin 15 (IL-15) is a four-alpha helix bundle cytokine with many similar properties to IL-2, with which it shares components of its receptor. The IL-15 receptor is a heterotrimeric receptor composed of IL-15Ra, the high-affinity receptor for IL-15, as well as IL-2/15Rb (CD122) and common gamma chain (CD132). IL-15 binds to IL-15Rα receptor and can then be presented in trans to IL-2/15Rb and common gamma chain on other cells. Trans-presentation is thought to be the major mechanism by which IL-15-mediated responses occur in mice, although may not be necessary in humans (Castillo <i>et al.</i>). The cytoplasmic domains of IL-2/15Rb and common gamma chain mediate signaling to activate JAK/STAT and PI3K pathways. IL-15 supports the survival and proliferation of naive CD4+ and CD8+ T cells, and promotes homeostasis of memory T cells. IL-15 also promotes the survival and differentiation of NK cells and regulates their cytolytic activity (Ma <i>et al.</i>).
Description:
ECHS1 (Enoyl Coenzyme A hydratase, short chain, 1) catalyzes the hydration of 2-trans-enoyl-coenzyme A (CoA) intermediates to L-3-hydroxyacyl-CoAs, in the second step of the mitochondrial fatty acid beta-oxidation pathway.
Description:
ECHS1 (Enoyl Coenzyme A hydratase, short chain, 1) catalyzes the hydration of 2-trans-enoyl-coenzyme A (CoA) intermediates to L-3-hydroxyacyl-CoAs, in the second step of the mitochondrial fatty acid beta-oxidation pathway.
Description:
A phenolic product found in both grape skin and wines. Has antifungal, antitumor and antioxidative properties. A specific inhibitor of cyclooxygenase-1 (COX-1; ED50=15µM). Also inhibits the hydroxyperoxidase activity of COX-1 (ED50=3.7µM). Inhibits phorbol ester-induced free radical formation in HL-60 cells (ED50=27µM) and acts as an anti-mutagenic agent (ED50=15µM) in TM677 cells treated with DMBA. Also a selective inhibitor of P450 1A1.
Description:
PPWD1 is a putative peptidylprolyl isomerase (PPIase). PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPWD1 may be involved in pre-mRNA splicing.