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Titlebook: Signal Transduction Mechanisms; Junor A. Barnes,Haldane G. Coore,Rajendra K. Sharm Book 1995 Kluwer Academic Publishers 1995 ATP.Amino aci

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书目名称Signal Transduction Mechanisms
编辑Junor A. Barnes,Haldane G. Coore,Rajendra K. Sharm
视频video
丛书名称Developments in Molecular and Cellular Biochemistry
图书封面Titlebook: Signal Transduction Mechanisms;  Junor A. Barnes,Haldane G. Coore,Rajendra K. Sharm Book 1995 Kluwer Academic Publishers 1995 ATP.Amino aci
描述This volume contains the proceedings of an InternationalSymposium on `Second Messenger Systems - Molecular, Cellularand Behavioural Aspects‘, which was held at Tobago on June16-17, 1994. .The interaction of an extracellular agonist (First Messenger) with itsplasma membrane receptor leads to the transmission of a signal acrossthe cell membrane and results in the production and/or activation ofother signalling molecules (Second Messengers). These SecondMessengers control the action of many protein kinases and proteinphosphatases and so lead to cellular responses. Although thebiochemical basis of the transduction of signals in the mainsignalling systems in eukaryotic cells is probably largely known,intensified research is ongoing in the following areas: the discoveryof specific substrates for many protein kinases, elucidation of thebiological significance of the differential tissue expression andheterogeneity of many signalling proteins, and the unravelling ofdiverse interactions (such as signal potentiation, synergism,antagonism and neuronal co-transmission) between signalling systems.As knowledge from such studies accumulates, it is becoming clear thatthe `cross talk‘ interactions b
出版日期Book 1995
关键词ATP; Amino acid; Calcium; Glycogen; Nucleotide; Translation; proteins
版次1
doihttps://doi.org/10.1007/978-1-4615-2015-3
isbn_softcover978-1-4613-5833-6
isbn_ebook978-1-4615-2015-3
copyrightKluwer Academic Publishers 1995
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High molecular weight calmodulin-binding protein is phosphorylated by calmodulin-dependent protein bstrate specificity of this protein kinase indicates that it is not related to the known protein kinases (I, II, III, IV and V) that have been already characterized, therefore we would like to designate this novel kinase as a CaM-dependent protein kinase VI.
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Modulation of protein kinase C by adenosine: Involvement of adenosine A1 receptor-pertussis toxin sompletely blocked the protective effect of ENBA against the PDBu induced attenuation of ET- 1 contractions. N0861 also completely blocked the increase in ET-1 contractions in the arterial rings incubated with ENBA alone. Another A. receptor antagonist DPCPX also produced similar results as N0861. On
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Phosphorylation and partial sequence of pregnant sheep myometrium myosin light chain kinase,suggesting that the amino acid residues modified by the two kinases are different. Phosphoamino acid analysis of the MLCK revealed that PKC phosphorylated serine and threonine residues. The double reciprocal plots of the enzyme activity and calmodulin concentrations showed that the V. of the reactio
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Regulation of phospholamban and troponin-I phosphorylation in the intact rat cardiomyocytes by adrefound to stimulate myocyte AC. However, the stimulation of the β.-AR only marginally increased while the stimulation of β.-AR markedly increased PLN phosphorylation. Other stimuli that increase tissue cyclic AMP levels also increased PLN and TN-I phosphorylation and these included isobutylmethylxant
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