872 Results for: "Síran+inditý+hydrát"

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran (ras-related nuclear protein) is a small GTP binding protein belonging to the RAS superfamily that is essential for the translocation of RNA and proteins through the nuclear pore complex. The Ran protein is also involved in control of DNA synthesis and cell cycle progression. Nuclear localization of Ran requires the presence of regulator of chromosome condensation 1 (RCC1). Mutations in Ran disrupt DNA synthesis. Because of its many functions, it is likely that Ran interacts with several other proteins. Ran regulates formation and organization of the microtubule network independently of its role in the nucleus-cytosol exchange of macromolecules. Ran could be a key signaling molecule regulating microtubule polymerization during mitosis. RCC1 generates a high local concentration of Ran-GTP around chromatin which, in turn, induces the local nucleation of microtubules. Ran is an androgen receptor (AR) coactivator that binds differentially with different lengths of polyglutamine within the androgen receptor. Polyglutamine repeat expansion in the AR is linked to Kennedy's disease (X-linked spinal and bulbar muscular atrophy). Ran coactivation of the AR diminishes with polyglutamine expansion within the AR, and this weak coactivation may lead to partial androgen insensitivity during the development of Kennedy's disease.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.

Supplier: Bioss

Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.

Supplier: Bioss

Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.

Supplier: Bioss

Ran (ras-related nuclear protein) is a small GTP binding protein belonging to the RAS superfamily that is essential for the translocation of RNA and proteins through the nuclear pore complex. The Ran protein is also involved in control of DNA synthesis and cell cycle progression. Nuclear localization of Ran requires the presence of regulator of chromosome condensation 1 (RCC1). Mutations in Ran disrupt DNA synthesis. Because of its many functions, it is likely that Ran interacts with several other proteins. Ran regulates formation and organisation of the microtubule network independently of its role in the nucleus-cytosol exchange of macromolecules. Ran could be a key signaling molecule regulating microtubule polymerization during mitosis. RCC1 generates a high local concentration of Ran-GTP around chromatin which, in turn, induces the local nucleation of microtubules. Ran is an androgen receptor (AR) coactivator that binds differentially with different lengths of polyglutamine within the androgen receptor. Polyglutamine repeat expansion in the AR is linked to Kennedy's disease (X-linked spinal and bulbar muscular atrophy). Ran coactivation of the AR diminishes with polyglutamine expansion within the AR, and this weak coactivation may lead to partial androgen insensitivity during the development of Kennedy's disease.

Supplier: Bioss

Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.

Supplier: Bioss

Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.

Supplier: Bioss

Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Ran GTPase plays important roles in nucleocytoplasmic transport in interphase and in both spindle formation and nuclear envelope (NE) assembly during mitosis. The latter functions rely on the presence of high local concentrations of GTP bound Ran near mitotic chromatin. RanGTP localization has been proposed to result from the association of Ran's GDP/GTP exchange factor, RCC1, with chromatin , but Ran is shown here to bind directly to chromatin in two modes, either dependent or independent of RCC1, and, where bound, to increase the affinity of chromatin for NE membranes.

Supplier: Bioss

Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.

Supplier: Bioss

Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.

Supplier: Bioss

Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1 trimeric complex. Increase GTP hydrolysis induced by the Ran GTPase activating protein RANGAP1. May act in an intracellular signaling pathway which may control the progression through the cell cycle by regulating the transport of protein and nucleic acids across the nuclear membrane.