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Titlebook: Interacting Protein Domains; Their Role in Signal Ludwig Heilmeyer Conference proceedings 1997 Springer-Verlag Berlin Heidelberg 1997 ATP.A

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Substrate Binding and Catalytic Mechanism in Phospholipase C from ,e phospholipids at the phospho moiety liberating the polar head group and .-1,2-diacylglycerol (DAG) or ceramide. Although PLC., is a non-specific enzyme, it prefers phosphatidylcholine (PC) as a substrate. In bacteria PLC is part of a phosphate retrieval system, and in mammals PLC plays an importan
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Identification of Three Active Site Residues Involved in Substrate Binding by Human 43 kDa-D-,-Inosir-mediated activation of phospholipase C (1). Alternatively, PtdIns(4,5)P. is the substrate for a specific receptor-activated 3-kinase to generate another signal molecule, i. e. phosphatidylinositol 3,4,5-.phosphate. Ins(1,4,5)P. is the substrate of a 5-phosphatase to produce Ins(1,4)P. and of a 3-k
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Conference proceedings 1997al Trans­ duction and Protein Phosphorylation" was held on the island of Spezai, Greece, in September 1986. The second one took place in Chateau La Londe, France, in September 1989 on "Cellular Regulation by Protein Phosphorylation", the third one on " Tyrosine Phosphorylation/Dephosphorylation and
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Substrate Binding and Catalytic Mechanism in Phospholipase C from ,ormation on mammalian PC-PLCs is available, but PLC., is regarded as a useful model of mammalian PC-PLCs, since antibodies against PLC., cross react with a PC-PLC in mammalian cells. and since they neutralize the PC-PLC activity in ...
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Interaction Studies Using Biosensorsfhudryl, carboxyl, and other groups are well defined and reproducible. Non covalent, site directed immobilization can be achieved by avidin-biotin interaction, by the use of antibodies or by binding fusion proteins to specific surfaces (Gershon and Khilko, 1995). Surfaces containing lipid monolayers are available, too (Soulages .., 1995).
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