A new simple method for the benzologation of heterocycles

Ashby, John; AYAD, MEHDI; Meth‐Cohn, Otto

doi:10.1039/c29710001251

Cited by 17 publications

(18 citation statements)

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“…While the heat-stable protein inhibitor (PKI) of the CAMP-dependent protein kinase was first described in skeletal muscle [I] from which it was recently isolated in pure form [2] , its greatest concentration occurs in the brain [3] . This is not surprising in view of the very high concentration of protein kinase found in this tissue [4] .…”

Section: Introductionmentioning

confidence: 99%

Isolation and properties of the bovine brain protein inhibitor of adenosine 3′:5′‐monophosphate‐dependent protein kinases

et al. 1978

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Section: Introductionmentioning

confidence: 99%

Isolation and properties of the bovine brain protein inhibitor of adenosine 3′:5′‐monophosphate‐dependent protein kinases

et al. 1978

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“…Vanadate, an inhibitor of the ATPase activities of the sarcolemmal vesicles 15,361 and digitoxigenin, a membrane permeant inhibitor of the Na,K-ATPase activity have no effect on the activation reaction (Table 3). An inhibitor of CAMPdependent protein kinase activity [37], which fully prevents the phosphorylation of the site responsible for the activation of the Ca2+-pumping ATPase of sarcolemma [18] has no effect.…”

Section: Inhibition Of the Na+-ca'+-exchange Activity By Phosphorylusmentioning

confidence: 99%

The Regulation of the Na⁺ ‐Ca²⁺ Exchanger of Heart Sarcolemma

Caroni¹,

Carafoli²

1983

European Journal of Biochemistry

215

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The Na+/Ca2+ ‐exchange of calf‐heart sarcolemma is activated by a treatment with ATP, Mg2+, and Ca2+, and deactivated by a treatment with phosphorylase phosphatase. The effect of th e latter can be substituted by a treatment with Mg2+, Ca2+, and calmodulin. the activating treatment does not require added calmodulin, but is inhibited by calmodulin antagonists. Evidently, engdogenous calmodulin is required and sufficient. Activation is half‐maximal at about 2μM Ca2+. Added clamodulin, however, decreases the Km (Ca2+) of the activating process to about 0.8 μM. Deactivation is half‐maximal, at optimal calmodulin concentrations, at about 1.5 μM Ca2+. Experiments with adenosine 5′‐[γ‐thio]triphosphate have shown that the activating treatment is mediated by a kinase and the deactivating treatment by a phosphatase. The concerted operation of the two enzymes is made possible by their different Ca2+ affinity. At saturating Ca2+ concentrations, the level of ATP may also influence the balance of the two enzymes.

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“…The freed catalytic subunit is active and cAMP independent. A heat stable protein which inhibits CAMPdependent protein kinase is present in many tissues (APPLEMAN et ASHBY & WALSH, 1972). ASHBY & WALSH (1972) reported that skeletal muscle and brain contain the highest inhibitory activity.…”

mentioning

confidence: 99%

“…A heat stable protein which inhibits CAMPdependent protein kinase is present in many tissues (APPLEMAN et ASHBY & WALSH, 1972). ASHBY & WALSH (1972) reported that skeletal muscle and brain contain the highest inhibitory activity. They also reported (ASHBY & WALSH, 1973) that the inhibitor complexes with the free catalytic subunit (C), but not holoenzyme (RC).…”

mentioning

confidence: 99%

Subcellular Distribution of a Heat‐stable Protein Inhibitor of Cyclic Amp‐dependent Protein Kinase in Rat Brain

Roskoski

Frederick

1977

Journal of Neurochemistry

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Abstract— Cyclic AMP (cAMP)‐dependent protein kinase catalyzes the phosphorylation of polypeptidic serine and threonine residues according to the following chemical equation: ATP + protein → phospho‐protein + ADP. A heat stable, trypsin labile factor present in brain, skeletal muscle and other tissues inhibits enzymatic phosphorylation of some proteins and enhances that of others. Since brain is one of the richest sources of adenylate cyclase, cAMP, cAMP‐dependent protein kinase and the heat stable protein kinase inhibitor and because they may play a role in neurotransmission, an investigation of the subcellular distribution of the heat stable factor in rat brain was undertaken. Although present in the nuclear, mitochondrial and microsomal fractions, the highest activity of protein kinase inhibitor is in the soluble fraction: its activity parallels that of the cytoplasmic enzyme marker, lactate dehydro‐genase. The inhibitory activity is also found in the synaptosome or pinched‐off nerve ending fraction. Following osmotic lysis of this fraction, about 90% of the factor occurs in the soluble fraction. On the other hand, only 40% of the cAMP‐dependent protein kinase is solubilized and 60% remains membrane‐bound. Using this membrane‐bound protein kinase, phosphorylation of endogenous substrate is unaltered by inhibitor, but phosphorylation of added histone substrate is decreased.

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A new simple method for the benzologation of heterocycles

Cited by 17 publications

References 0 publications

Isolation and properties of the bovine brain protein inhibitor of adenosine 3′:5′‐monophosphate‐dependent protein kinases

Isolation and properties of the bovine brain protein inhibitor of adenosine 3′:5′‐monophosphate‐dependent protein kinases

The Regulation of the Na⁺ ‐Ca²⁺ Exchanger of Heart Sarcolemma

Subcellular Distribution of a Heat‐stable Protein Inhibitor of Cyclic Amp‐dependent Protein Kinase in Rat Brain

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A new simple method for the benzologation of heterocycles

Cited by 17 publications

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Isolation and properties of the bovine brain protein inhibitor of adenosine 3′:5′‐monophosphate‐dependent protein kinases

Isolation and properties of the bovine brain protein inhibitor of adenosine 3′:5′‐monophosphate‐dependent protein kinases

The Regulation of the Na+ ‐Ca2+ Exchanger of Heart Sarcolemma

Subcellular Distribution of a Heat‐stable Protein Inhibitor of Cyclic Amp‐dependent Protein Kinase in Rat Brain

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The Regulation of the Na⁺ ‐Ca²⁺ Exchanger of Heart Sarcolemma