Fifth International Conference on Cyclic Nucleotides and Protein Phosphorylation, Milan Italy (ADVANCES IN SECOND MESSENGER AND PHOSPHOPROTEIN RESEARCH) ePub download
by Paul Greengard,G. Alan Robison,Rodolfo Paoletti,Simonetta Nicosia
- ISBN: 0890043493
- ISBN13: 978-0890043493
- ePub: 1937 kb | FB2: 1801 kb
- Language: English
- Category: Science & Mathematics
- Publisher: Raven Press (April 1, 1984)
- Rating: 4.6/5
- Votes: 668
- Format: txt azw rtf docx
Paul Greengard, G. Alan Robiso.
Paul Greengard, G. Fifth International Conference on Cyclic Nucleotides and Protein Phosp. 1 2 3 4 5. Want to Read.
Milan, June 27-July 1, 1983. Paul Greengard, G. Alan Robison, Rodolfo Paoletti, Simonetta Nicosia. Published 1983 by Raven Press in New York. Congresses, Cyclic nucleotides, Phosphorylation, Life Sciences - Cytology, Nucleotides, Science.
Paul Greengard’s most popular book is Protein Phosphorylation in the Nervous System.
This conference and the proceedings focused on the role of cyclic nucleotides, calcium and protein kinases as second messengers in signal transduction systems
Volume 21A. Abstracts Volume. How we measure 'reads'. This conference and the proceedings focused on the role of cyclic nucleotides, calcium and protein kinases as second messengers in signal transduction systems. This volume contains abstracts of papers presented at the Conference.
Rodolfo Paoletti, G. Alan Robison, Paul Greengard. Nicolás G. Bazán, James M. Iacono, Rodolfo Paoletti.
Paul Greengard and G. Alan Robison, Eds. Vol. 1, Physiology and Pharmacology of Cyclic AMP. 610 p. illus. 2, New Assay Methods for Cyclic Nucleotides. A conference, Milan, July 1971. Alan Robison, and Rodolfo Paoletti, Eds. Raven, New York, 1972. Paul Greengard and G.
Paul Greengard (Ed. Simonetta Nicosia (Ed. Rodolfo Paoletti (Ed. G. Alan Robison (Ed. data.
International Standard Book Number (ISBN) .
International Standard Book Number (ISBN): 0890043493.
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Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or modifying its function. Approximately 13000 human proteins have sites that are phosphorylated.