Download Biochemistry of Cell Membranes: A Compendium of Selected by J. L. Bos, B. M. T. Burgering, G. J. Pronk, A. M. M. de PDF

By J. L. Bos, B. M. T. Burgering, G. J. Pronk, A. M. M. de Vries-Smits, J. P. Medema (auth.), Prof. Dr. S. Papa, Prof. Dr. J. M. Tager (eds.)

This publication comprises a chain of reports on chosen subject matters in the quickly and enormously increasing box of membrane biology. Its goal is to spotlight the main major and critical advances which were made lately in knowing the constitution, dynamics and features of mobile membranes. parts lined during this monograph contain: • sign Transduction • Membrane site visitors: Protein and Lipids • Bioenergetics: power move and Membrane shipping • mobile Ion Homeostasis • progress elements and Adhesion Molecules • Structural research of Membrane Proteins • Membranes and illness. Biochemistry of mobile Membranes should still function a benchmark for indicating crucial strains for destiny learn in those components.

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Chem. 267: 13943-13951. W. and Luscher, B. (1993) Casein kinase II in signal transduction and cell regulation. Mol. Cell. Biochem. 127/128: 187-199. M. D. (1993) Copurification of casein kinase II with 20S proteasome and phosphorylation of a 30 kDa proteasome subunit. J. Bioi. Chem. 268: 17413-17417. A. and Salviati, G. (1993) Dystrophin is phosphorylated by endogenous protein kinases. Biochem. J. 293: 243-247. G. N. (1989) Myc oncoproteins are phosphorylated by casein kinase II. EMBO J. 8: 1111-1119.

Bioi. 10: 4089-4099. Palvimo, J. and Linnala-Kankkunen (1989) Identification of sites on chromosomal protein HMGl phosphorylated by casein kinase II. FEBS Lett. 257: 101-104. A. Pinna, F. Meggio and S. A. (1990) Casein kinase 2: an eminence grise in cellular regulation? Biochim. Biophys. Acta 1054: 267-284. A. (1991) "Independent" protein kinases: a challenge to canons. , Jr. Heilmeyer, Jr. ): Cellular Regulation and Protein Phosphorylation. NATO ASI Series, Vol. 56, Springer-Verlag, Berlin, Heidelberg, pp.

3). The P 2yl purinoceptor shares 21 % to 17% identity with the receptors for adenosine and cAMP while the P 2y2 and P2y3 sequences have less than 14% with these sequences. The lack of sequence identity shared between the recombinant P2 and PI purinoceptors is at first surprising, given that the endogenous ligands for both contain a nucleoside. However, the inactivity of both adenosine and AMP at the P2 purinoceptors and of ADP and ATP at PI purinoceptors must be taken into consideration. E. A.

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