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Title
Setname
Type
1
Activation and inhibition of phosphorylase kinase by monospecific antibodies raised against peptides from the regulatory domain of the gamma-subunit.
ir_uspace
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2
Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase.
ir_uspace
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3
Characterization of the phosphotyrosyl protein phosphatase activity of calmodulin-dependent protein phosphatase.
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4
Characterization of the regulatory domain of the gamma-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory.
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5
Conformationally dynamic C helix of the RIalpha subunit of protein kinase A mediates isoform-specific domain reorganization upon C subunit binding.
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6
Dephosphorylation of cAMP-dependent protein kinase regulatory subunit (type II) by calmodulin-dependent protein phosphatase. Determinants of substrate specificity.
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7
Effects of deletions in the central helix of calmodulin on enzyme activation and peptide binding.
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8
Effects of weak extremely low frequency magnetic fields on calcium/calmodulin interactions.
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9
Gamma-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin.
ir_uspace
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10
Identification of the calmodulin-binding domain of skeletal muscle myosin light
ir_uspace
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11
Identification of the substrate and pseudosubstrate binding sites of phosphorylase kinase gamma-subunit.
ir_uspace
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12
Phosphorylation of cardiac troponin by guanosine 3':5'-monophosphate-dependent protein kinase.
ir_uspace
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13
Photoreceptor cGMP phosphodiesterase delta subunit (PDEdelta) functions as a prenyl-binding protein
ir_uspace
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14
Prenyltransferase. Kinetic studies of the 1'-4 coupling reaction with avian liver enzyme.
ir_uspace
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15
Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain.
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