Nanopublications LDF server

Matches in Nanopublications for { ?s ?p "Activation of PKC-a mediated the sustained decrease in mitochondrial membrane hyperpolarisation and oxidative phosphorylation but not the decrease in electron transfer rate. Sustained mitochondrial dysfunction was also affected by ERK1/2, through a PKC-independent pathway. These findings suggest that activation of PKC-a and/or ERK1/2 lead to decreased activity of ATP synthase, rather than affecting OXPHOS system complexes [40]. Indeed, the a, b, and e subunits of F(1)F(0)- ATPase have PKC consensus motifs [41]. PKC-a phosphorylated the b subunit of F(1)F(0)-ATPase on a serine residue and decreased F(0)F(1)-ATPase activity, oxidative phosphorylation and ATP production [41]." ?g. }

• _5 value "Activation of PKC-a mediated the sustained decrease in mitochondrial membrane hyperpolarisation and oxidative phosphorylation but not the decrease in electron transfer rate. Sustained mitochondrial dysfunction was also affected by ERK1/2, through a PKC-independent pathway. These findings suggest that activation of PKC-a and/or ERK1/2 lead to decreased activity of ATP synthase, rather than affecting OXPHOS system complexes [40]. Indeed, the a, b, and e subunits of F(1)F(0)- ATPase have PKC consensus motifs [41]. PKC-a phosphorylated the b subunit of F(1)F(0)-ATPase on a serine residue and decreased F(0)F(1)-ATPase activity, oxidative phosphorylation and ATP production [41]." provenance.
• _5 value "Activation of PKC-a mediated the sustained decrease in mitochondrial membrane hyperpolarisation and oxidative phosphorylation but not the decrease in electron transfer rate. Sustained mitochondrial dysfunction was also affected by ERK1/2, through a PKC-independent pathway. These findings suggest that activation of PKC-a and/or ERK1/2 lead to decreased activity of ATP synthase, rather than affecting OXPHOS system complexes [40]. Indeed, the a, b, and e subunits of F(1)F(0)- ATPase have PKC consensus motifs [41]. PKC-a phosphorylated the b subunit of F(1)F(0)-ATPase on a serine residue and decreased F(0)F(1)-ATPase activity, oxidative phosphorylation and ATP production [41]." provenance.
• _5 value "Activation of PKC-a mediated the sustained decrease in mitochondrial membrane hyperpolarisation and oxidative phosphorylation but not the decrease in electron transfer rate. Sustained mitochondrial dysfunction was also affected by ERK1/2, through a PKC-independent pathway. These findings suggest that activation of PKC-a and/or ERK1/2 lead to decreased activity of ATP synthase, rather than affecting OXPHOS system complexes [40]. Indeed, the a, b, and e subunits of F(1)F(0)- ATPase have PKC consensus motifs [41]. PKC-a phosphorylated the b subunit of F(1)F(0)-ATPase on a serine residue and decreased F(0)F(1)-ATPase activity, oxidative phosphorylation and ATP production [41]." provenance.
• _5 value "Activation of PKC-a mediated the sustained decrease in mitochondrial membrane hyperpolarisation and oxidative phosphorylation but not the decrease in electron transfer rate. Sustained mitochondrial dysfunction was also affected by ERK1/2, through a PKC-independent pathway. These findings suggest that activation of PKC-a and/or ERK1/2 lead to decreased activity of ATP synthase, rather than affecting OXPHOS system complexes [40]. Indeed, the a, b, and e subunits of F(1)F(0)- ATPase have PKC consensus motifs [41]. PKC-a phosphorylated the b subunit of F(1)F(0)-ATPase on a serine residue and decreased F(0)F(1)-ATPase activity, oxidative phosphorylation and ATP production [41]." provenance.