AbstractThe α-subunit of the E1 component of branched-chain 2-oxoacid dehydrogenase is phosphorylated at 3 sites by an endogenous kinase. Inactivation of the complex correlates with rapid phosphorylation of one of these sites. The similarities with the covalent regulation of pyruvate dehydrogenase complex are discussed
The 2-oxoacid dehydrogenase multienzyme complexes are high Mr assemblies occupying key positions in ...
Monospecific, polyclonal antisera were raised to purified bovine heart succinate dehydrogenase (SDH)...
A comprehensive investigation of the optimal conditions for reconstitution of bovine heart pyruvate ...
AbstractThe α-subunit of the E1 component of branched-chain 2-oxoacid dehydrogenase is phosphorylate...
AbstractInactivation of branched-chain 2-oxoacid dehydrogenase complex correlates with phosphorylati...
AbstractBranched-chain 2-oxoacid dehydrogenase complex has been purified to near homogeneity by a si...
AbstractTryptic [32P]phosphopeptides were prepared from [32P]phosphorylated ox-kidney branched-chain...
AbstractThe branched-chain 2 oxoacid dehydrogenase complex has been purified from well-washed ox-kid...
AbstractThe α subunit of the E1 component of branched-chain 2-oxoacid dehydrogenase complex becomes ...
AbstractBranched-chain 2-oxoacid dehydrogenase complex is inactivated by phosphorylation of the α-su...
SummaryWe report the crystal structures of the phosporylated pyruvate dehydrogenase (E1p) component ...
AbstractPhosphorylation of the pyruvate dehydrogenase component (E1) of the muscle pyruvate dehydrog...
AbstractIt is generally believed that mammalian pyruvate dehydrogenase kinase is a heterodimer consi...
AbstractThe mechanism of regulatory phosphorylation of the pyruvate dehydrogenase component (E1) of ...
AbstractBovine kidney mitochondria were separated into matrix and membrane fractions by treatment wi...
The 2-oxoacid dehydrogenase multienzyme complexes are high Mr assemblies occupying key positions in ...
Monospecific, polyclonal antisera were raised to purified bovine heart succinate dehydrogenase (SDH)...
A comprehensive investigation of the optimal conditions for reconstitution of bovine heart pyruvate ...
AbstractThe α-subunit of the E1 component of branched-chain 2-oxoacid dehydrogenase is phosphorylate...
AbstractInactivation of branched-chain 2-oxoacid dehydrogenase complex correlates with phosphorylati...
AbstractBranched-chain 2-oxoacid dehydrogenase complex has been purified to near homogeneity by a si...
AbstractTryptic [32P]phosphopeptides were prepared from [32P]phosphorylated ox-kidney branched-chain...
AbstractThe branched-chain 2 oxoacid dehydrogenase complex has been purified from well-washed ox-kid...
AbstractThe α subunit of the E1 component of branched-chain 2-oxoacid dehydrogenase complex becomes ...
AbstractBranched-chain 2-oxoacid dehydrogenase complex is inactivated by phosphorylation of the α-su...
SummaryWe report the crystal structures of the phosporylated pyruvate dehydrogenase (E1p) component ...
AbstractPhosphorylation of the pyruvate dehydrogenase component (E1) of the muscle pyruvate dehydrog...
AbstractIt is generally believed that mammalian pyruvate dehydrogenase kinase is a heterodimer consi...
AbstractThe mechanism of regulatory phosphorylation of the pyruvate dehydrogenase component (E1) of ...
AbstractBovine kidney mitochondria were separated into matrix and membrane fractions by treatment wi...
The 2-oxoacid dehydrogenase multienzyme complexes are high Mr assemblies occupying key positions in ...
Monospecific, polyclonal antisera were raised to purified bovine heart succinate dehydrogenase (SDH)...
A comprehensive investigation of the optimal conditions for reconstitution of bovine heart pyruvate ...