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pmid: 2532591
1. Myofibrils isolated from Mercenaria mercenaria were phosphorylated by endogenous kinase. Over a range of ionic strengths only paramyosin was phosphorylated. 2. Thiophosphorylation of paramyosin caused an inhibition of steady-state actin-activated ATPase activity of the myofibrils. 3. It is proposed that the endogenous kinase is the catalytic subunit of the cAMP-dependent protein kinase. 4. The sequence around the phosphorylation site was determined. 5. The phosphorylation site probably is close to the C-terminus of the paramyosin molecule.
Binding Sites, Mollusca, Animals, Ca(2+) Mg(2+)-ATPase, Tropomyosin, Myosins, Phosphorylation, Protein Kinases, Muscle Contraction
Binding Sites, Mollusca, Animals, Ca(2+) Mg(2+)-ATPase, Tropomyosin, Myosins, Phosphorylation, Protein Kinases, Muscle Contraction
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 29 | |
popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |