Titlebook: Activation of Hormone and Growth Factor Receptors; Molecular Mechanisms Michael N. Alexis,Constantin E. Sekeris (Director) Book 1990 Spring

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Activation of Hormone and Growth Factor Receptors978-94-009-1936-5Series ISSN 1389-2185

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East Timor in the Arc of Instability,ogenes code for aberrant hormone and growth factor receptors (e.g. v-erbA and v-erbB). The deregulated action of these products interferes with normal signal transduction for cellular proliferation and differentiation, thus leading to cellular transformation. In this context, receptor-mediated trans

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https://doi.org/10.1007/978-981-15-6145-0its specific cell surface receptor. This receptor is an oligomer consisting of two α-subunits with Mr 130 kDa, and two?-subunits with Mr 95 kDa; the different subunits are linked together by disulfide bridges. The α-subunit contains most — if not all — of the hormone binding domain, whereas the ?- s

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The Energy Transition as a System,itiate their action by binding to specific, high affinity receptor molecules on the cell surface. Interest in growth factors and their receptors has been dramatically intensified by the discovery that at least some of these molecules show a striking structural homology with certain viral oncogene pr

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The Right to Health in Australia,and B, in a molar ratio of 1:5. Subunit A consists of two polypeptides, A. (M.=23000) and A. (M.=7500), linked to each other by a single disulfide bond. Subunit B is a single chain polypeptides. Only the holotoxin which contains both subunits A and B. is capable of exerting its action on intact cell

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The Establishment of the Austrian Republictransduction. Thus, it is thought that . p21 is involved in the generation of the two second messengers diacylglycerol and inositol 1,4,5 triphosphate. More recent evidence suggests that . proteins are unlikely to control the action of a phospholipase. Other cytoplasmic proteins which may interact w

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Foreign Loans and Internal Politicsdomains. We have investigated the possible differences in regulation of transcription and the binding to thyroid hormone responsive elements (TREs) by these proteins. The results show that in chicken erythroblasts P75. constitutively represses expression of the genes for band 3 and carbonic anhydras