Nanopublications LDF server

Matches in Nanopublications for { ?s ?p "It has been proposed that the association of RyR2 channels with their regulators PP1, PP2A, and PKA is mediated by specific targetting molecules that bind via leucine zipper interactions (242). In the case of PP1, it is Neurabin-II that functions as the targetting subunit. It is puzzling, however, that the suggested leucine zipper motif in Neurabin-II partially overlaps with the well-documented PDZ domain (242). Given the substantially different three-dimensional structures adopted by these interaction modules, the binding of RyR2 to this putative leucine zipper motif of Neurabin-II would implicate a dramatic conformational change. Recently, it has been demonstrated that PP1-alpha also occurs in a complex with IP3R1 (105, 358). The conductance of the IP3R1 channel, like that of RyR channels, is increased after phosphorylation by PKA (105)," ?g. }

• _4 value "It has been proposed that the association of RyR2 channels with their regulators PP1, PP2A, and PKA is mediated by specific targetting molecules that bind via leucine zipper interactions (242). In the case of PP1, it is Neurabin-II that functions as the targetting subunit. It is puzzling, however, that the suggested leucine zipper motif in Neurabin-II partially overlaps with the well-documented PDZ domain (242). Given the substantially different three-dimensional structures adopted by these interaction modules, the binding of RyR2 to this putative leucine zipper motif of Neurabin-II would implicate a dramatic conformational change. Recently, it has been demonstrated that PP1-alpha also occurs in a complex with IP3R1 (105, 358). The conductance of the IP3R1 channel, like that of RyR channels, is increased after phosphorylation by PKA (105)," provenance.
• _5 value "It has been proposed that the association of RyR2 channels with their regulators PP1, PP2A, and PKA is mediated by specific targetting molecules that bind via leucine zipper interactions (242). In the case of PP1, it is Neurabin-II that functions as the targetting subunit. It is puzzling, however, that the suggested leucine zipper motif in Neurabin-II partially overlaps with the well-documented PDZ domain (242). Given the substantially different three-dimensional structures adopted by these interaction modules, the binding of RyR2 to this putative leucine zipper motif of Neurabin-II would implicate a dramatic conformational change. Recently, it has been demonstrated that PP1-alpha also occurs in a complex with IP3R1 (105, 358). The conductance of the IP3R1 channel, like that of RyR channels, is increased after phosphorylation by PKA (105)," provenance.
• _4 value "It has been proposed that the association of RyR2 channels with their regulators PP1, PP2A, and PKA is mediated by specific targetting molecules that bind via leucine zipper interactions (242). In the case of PP1, it is Neurabin-II that functions as the targetting subunit. It is puzzling, however, that the suggested leucine zipper motif in Neurabin-II partially overlaps with the well-documented PDZ domain (242). Given the substantially different three-dimensional structures adopted by these interaction modules, the binding of RyR2 to this putative leucine zipper motif of Neurabin-II would implicate a dramatic conformational change. Recently, it has been demonstrated that PP1-alpha also occurs in a complex with IP3R1 (105, 358). The conductance of the IP3R1 channel, like that of RyR channels, is increased after phosphorylation by PKA (105)," provenance.
• _5 value "It has been proposed that the association of RyR2 channels with their regulators PP1, PP2A, and PKA is mediated by specific targetting molecules that bind via leucine zipper interactions (242). In the case of PP1, it is Neurabin-II that functions as the targetting subunit. It is puzzling, however, that the suggested leucine zipper motif in Neurabin-II partially overlaps with the well-documented PDZ domain (242). Given the substantially different three-dimensional structures adopted by these interaction modules, the binding of RyR2 to this putative leucine zipper motif of Neurabin-II would implicate a dramatic conformational change. Recently, it has been demonstrated that PP1-alpha also occurs in a complex with IP3R1 (105, 358). The conductance of the IP3R1 channel, like that of RyR channels, is increased after phosphorylation by PKA (105)," provenance.
• _6 value "It has been proposed that the association of RyR2 channels with their regulators PP1, PP2A, and PKA is mediated by specific targetting molecules that bind via leucine zipper interactions (242). In the case of PP1, it is Neurabin-II that functions as the targetting subunit. It is puzzling, however, that the suggested leucine zipper motif in Neurabin-II partially overlaps with the well-documented PDZ domain (242). Given the substantially different three-dimensional structures adopted by these interaction modules, the binding of RyR2 to this putative leucine zipper motif of Neurabin-II would implicate a dramatic conformational change. Recently, it has been demonstrated that PP1-alpha also occurs in a complex with IP3R1 (105, 358). The conductance of the IP3R1 channel, like that of RyR channels, is increased after phosphorylation by PKA (105)," provenance.
• _6 value "It has been proposed that the association of RyR2 channels with their regulators PP1, PP2A, and PKA is mediated by specific targetting molecules that bind via leucine zipper interactions (242). In the case of PP1, it is Neurabin-II that functions as the targetting subunit. It is puzzling, however, that the suggested leucine zipper motif in Neurabin-II partially overlaps with the well-documented PDZ domain (242). Given the substantially different three-dimensional structures adopted by these interaction modules, the binding of RyR2 to this putative leucine zipper motif of Neurabin-II would implicate a dramatic conformational change. Recently, it has been demonstrated that PP1-alpha also occurs in a complex with IP3R1 (105, 358). The conductance of the IP3R1 channel, like that of RyR channels, is increased after phosphorylation by PKA (105)," provenance.