Evidence for cytoskeletal associations of the adenylate cyclase system obtained by differential extraction of rat erythrocyte ghosts.

Evidence for cytoskeletal associations of the adenylate cyclase system obtained by differential extraction of rat erythrocyte ghosts.

[Anonymous].  1981.  Evidence for cytoskeletal associations of the adenylate cyclase system obtained by differential extraction of rat erythrocyte ghosts.. Biochemical and biophysical research communications. 101(3):1003-10.

Molecular complexes involved in the regulation of adenylate cyclase.

Skeletal association of the cholera toxin receptor in rat erythrocytes.

Properties of rat erythrocyte membrane cytoskeletal structures produced by digitonin extraction: digitonin-insoluble beta-adrenergic receptor, adenylate cyclase, and cholera toxin substrate.

Properties of rat erythrocyte membrane cytoskeletal structures produced by digitonin extraction: digitonin-insoluble beta-adrenergic receptor, adenylate cyclase, and cholera toxin substrate.

[Anonymous].  1982.  Properties of rat erythrocyte membrane cytoskeletal structures produced by digitonin extraction: digitonin-insoluble beta-adrenergic receptor, adenylate cyclase, and cholera toxin substrate.. The Journal of membrane biology. 64(3):225-31.

Formation and identification of cytoskeletal components from liver cytosolic precursors.

Cytosolic activator of adenylate cyclase: Reconstitution, characterization, and mechanism of action.

Histones H3 and H4 inhibit protein kinase C specifically.

A specific phosphoprotein phosphatase acts on histone H1 phosphorylated by protein kinase C.

Ascorbic acid is an endogenous cytosolic inhibitor of ATP-supported rat liver mitochondrial calcium transport.

Specificity of a phosphatase for phospholipid, Ca2+-dependent protein kinase-phosphorylated histone H1 resides in the catalytic subunit.

Specificity of a phosphatase for phospholipid, Ca2+-dependent protein kinase-phosphorylated histone H1 resides in the catalytic subunit.

[Anonymous].  1984.  Specificity of a phosphatase for phospholipid, Ca2+-dependent protein kinase-phosphorylated histone H1 resides in the catalytic subunit.. Biochemical and biophysical research communications. 118(1):278-83.